Receptor
PDB id Resolution Class Description Source Keywords
5E1D 1.45 Å EC: 2.1.1.244 NTMT1 IN COMPLEX WITH YPKRIA PEPTIDE HOMO SAPIENS STRUCTURAL GENOMICS STRUCTURAL GENOMICS CONSORTIUM SGC TR
Ref.: STRUCTURAL BASIS FOR SUBSTRATE RECOGNITION BY THE H N-TERMINAL METHYLTRANSFERASE 1. GENES DEV. V. 29 2343 2015
Ligand
Ligand Chain:Residue Validity Ligand Warnings Binding Data NGL Viewer Molecular Weight (Da) Formula SMILES
UNX A:319;
A:312;
A:326;
B:316;
A:333;
A:317;
A:332;
A:331;
B:308;
B:306;
B:313;
A:328;
A:306;
A:327;
A:305;
A:324;
A:334;
A:336;
B:321;
B:311;
A:313;
A:335;
A:318;
A:339;
A:310;
B:319;
A:308;
A:337;
A:340;
A:316;
A:311;
A:330;
A:309;
B:309;
A:321;
B:304;
A:307;
A:320;
B:303;
B:317;
B:310;
A:341;
A:338;
A:315;
A:325;
A:314;
A:329;
B:312;
B:315;
A:322;
B:314;
B:307;
A:323;
B:320;
B:322;
B:305;
B:318;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
Invalid;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
none;
submit data
n/a X *
TYR PRO LYS ARG ILE ALA E:1;
D:1;
Valid;
Valid;
Atoms found LESS than expected: % Diff = 0;
Atoms found LESS than expected: % Diff = 0;
Kd = 0.1 uM
748.927 n/a O=C([...
GOL A:302;
A:303;
B:302;
A:304;
Invalid;
Invalid;
Invalid;
Invalid;
none;
none;
none;
none;
submit data
92.094 C3 H8 O3 C(C(C...
SAH A:301;
B:301;
Valid;
Valid;
none;
none;
submit data
384.411 C14 H20 N6 O5 S c1nc(...
View in 3D viewer
90% Homology Family
Leader
PDB id Resolution Class Description Source Keywords
5E1M 1.75 Å EC: 2.1.1.244 CRYSTAL STRUCTURE OF NTMT1 IN COMPLEX WITH PPKRIA PEPTIDE HOMO SAPIENS STRUCTURAL GENOMICS STRUCTURAL GENOMICS CONSORTIUM SGC TR
Ref.: STRUCTURAL BASIS FOR SUBSTRATE RECOGNITION BY THE H N-TERMINAL METHYLTRANSFERASE 1. GENES DEV. V. 29 2343 2015
Members (8)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 1 families.
1 5E1O Kd = 0.3 uM ARG PRO LYS ARG ILE ALA n/a n/a
2 5CVE - SAH C14 H20 N6 O5 S c1nc(c2c(n....
3 5E1M Kd = 2.8 nM PRO PRO LYS ARG ILE ALA n/a n/a
4 5E1B Kd = 0.8 uM SER PRO LYS ARG ILE ALA n/a n/a
5 5E2A - SAH C14 H20 N6 O5 S c1nc(c2c(n....
6 5E1D Kd = 0.1 uM TYR PRO LYS ARG ILE ALA n/a n/a
7 5CVD Kd = 0.39 uM DMG PRO ARG ARG ARG SER ARG LYS PRO n/a n/a
8 5E2B - SAH C14 H20 N6 O5 S c1nc(c2c(n....
70% Homology Family (8)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 1 families.
1 5E1O Kd = 0.3 uM ARG PRO LYS ARG ILE ALA n/a n/a
2 5CVE - SAH C14 H20 N6 O5 S c1nc(c2c(n....
3 5E1M Kd = 2.8 nM PRO PRO LYS ARG ILE ALA n/a n/a
4 5E1B Kd = 0.8 uM SER PRO LYS ARG ILE ALA n/a n/a
5 5E2A - SAH C14 H20 N6 O5 S c1nc(c2c(n....
6 5E1D Kd = 0.1 uM TYR PRO LYS ARG ILE ALA n/a n/a
7 5CVD Kd = 0.39 uM DMG PRO ARG ARG ARG SER ARG LYS PRO n/a n/a
8 5E2B - SAH C14 H20 N6 O5 S c1nc(c2c(n....
50% Homology Family (10)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 1 families.
1 5E1O Kd = 0.3 uM ARG PRO LYS ARG ILE ALA n/a n/a
2 5CVE - SAH C14 H20 N6 O5 S c1nc(c2c(n....
3 5E1M Kd = 2.8 nM PRO PRO LYS ARG ILE ALA n/a n/a
4 5E1B Kd = 0.8 uM SER PRO LYS ARG ILE ALA n/a n/a
5 5E2A - SAH C14 H20 N6 O5 S c1nc(c2c(n....
6 5E1D Kd = 0.1 uM TYR PRO LYS ARG ILE ALA n/a n/a
7 5CVD Kd = 0.39 uM DMG PRO ARG ARG ARG SER ARG LYS PRO n/a n/a
8 5E2B - SAH C14 H20 N6 O5 S c1nc(c2c(n....
9 1XTP - SAI C14 H20 N6 O5 Se c1nc(c2c(n....
10 6DUB - SAH C14 H20 N6 O5 S c1nc(c2c(n....
Polypharmacology
Similar Ligands
Ligand no: 1; Ligand: TYR PRO LYS ARG ILE ALA; Similar ligands found: 216
No: Ligand ECFP6 Tc MDL keys Tc
1 TYR PRO LYS ARG ILE ALA 1 1
2 ARG PRO LYS ARG ILE ALA 0.793103 0.878788
3 3BY PRO LYS ARG ILE ALA 0.677165 0.842857
4 PRO PRO LYS ARG ILE ALA 0.664062 0.907692
5 SER PRO LYS ARG ILE ALA 0.655738 0.852941
6 DPN PRO DAR ILE NH2 0.604839 0.876923
7 LYS PRO VAL LEU ARG THR ALA 0.604478 0.855072
8 ALA ILE MET PRO ALA ARG PHE TYR PRO LYS 0.597484 0.902778
9 DTY ILE ARG LEU LPD 0.59542 0.954545
10 DPN PRO DAR DTH NH2 0.579365 0.838235
11 ARG ILE PRO SER TYR ARG TYR ARG TYR 0.57554 0.888889
12 ALA ASN SER ARG TYR PRO THR SER ILE ILE 0.574324 0.888889
13 ARG PRO MET THR TYR LYS GLY ALA LEU 0.552795 0.853333
14 ILE ARG TYR PRO LYS THR PHE GLY TRP 0.546512 0.890411
15 DPN PRO DAR CYS NH2 0.543307 0.791045
16 SER GLU LEU GLU ILE LYS ARG TYR 0.542857 0.760563
17 ASN PHE ASP ASN PRO VAL TYR ARG LYS THR 0.533742 0.851351
18 DPN PRO ARG 0.532787 0.830769
19 5JP PRO LYS ARG ILE ALA 0.531746 0.788732
20 TYR PRO SER LYS PRO ASP ASN PRO GLY GLU 0.530769 0.771429
21 ALA PHE ARG ILE PRO LEU THR ARG 0.530201 0.885714
22 GLU VAL ALA PRO PRO GLU TYR HIS ARG LYS 0.526316 0.875
23 ARG PRO PRO ILE PHE ILE ARG ARG LEU 0.52349 0.910448
24 LEU PRO PHE ASP ARG THR THR ILE MET 0.522293 0.826667
25 ASN ARG PRO VAL TYR ILE PRO ARG PRO PRO 0.52027 0.955224
26 LEU PRO PHE GLU ARG ALA THR ILE MET 0.518519 0.837838
27 GLU ARG THR ILE PRO ILE THR ARG GLU 0.518248 0.855072
28 GLN VAL PRO LEU ARG PRO MET THR TYR LYS 0.517857 0.853333
29 GLU GLU PRO THR VAL ILE LYS LYS TYR 0.51634 0.842857
30 VAL PRO LEU ARG PRO MET THR TYR 0.51634 0.864865
31 GLU LEU LYS ARG LYS MET ILE TYR MET 0.513514 0.760563
32 SER SER ARG LYS GLU TYR TYR ALA 0.51145 0.764706
33 ARG ILE ILE PRO ARG HIS LEU GLN LEU 0.509677 0.857143
34 ARG ARG LEU PRO ILE PHE SER ARG LEU 0.506579 0.859155
35 GLY GLU ARG THR ILE PRO ILE THR ARG GLU 0.503448 0.857143
36 ARG PRO MET THR PHE LYS GLY ALA LEU 0.5 0.813333
37 SER SER TYR ARG ARG PRO VAL GLY ILE 0.5 0.888889
38 LYS LEU PRO ALA GLN PHE TYR ILE LEU 0.496855 0.855072
39 ALA LEU PRO HIS ALA ILE LEU ARG LEU 0.496774 0.882353
40 THR LYS PRO ARG 0.495868 0.815385
41 TYR GLN PHE GLY PRO ASP PHE PRO ILE ALA 0.49375 0.842857
42 ALA ASN SER ARG PHE PRO THR SER ILE ILE 0.493671 0.847222
43 PRO SER ILE ASP ARG SER THR LYS PRO 0.493506 0.859155
44 LEU PRO PHE ASP LYS THR THR ILE MET 0.490446 0.746667
45 ALA ASN SER ARG TRP PRO ALY SER ILE ILE 0.488372 0.805195
46 ASN TYR THR PRO GLY PRO GLY ILE ARG PHE 0.48503 0.890411
47 GLU LEU ASN ARG LYS MET ILE TYR MET 0.484076 0.72973
48 PRO PRO ARG PRO ILE TYR ASN ARG ASN 0.483871 0.914286
49 PHE PRO THR LYS ASP VAL ALA LEU 0.48366 0.774648
50 GLN ASN TYR PRO ILE VAL GLN 0.482759 0.814286
51 ALA ASN SER ARG VAL PRO THR SER ILE ILE 0.482759 0.830986
52 ASP VAL GLN THR GLY ARG ARG PRO TYR GLU 0.481481 0.887324
53 HIS HIS ALA SER PRO ARG LYS 0.480519 0.802817
54 ARG LEU PRO ALA LYS ALA PRO LEU LEU 0.479452 0.852941
55 ALA MET ALA PRO ARG THR LEU LEU LEU 0.479452 0.797297
56 LYS PRO ILE VAL VAL LEU HIS GLY TYR 0.478528 0.857143
57 SER HIS PRO ARG PRO ILE ARG VAL 0.477124 0.835616
58 ALA ASN SER ARG ALA PRO THR SER ILE ILE 0.476821 0.808219
59 ARG LEU TYR GLN ASN PRO THR THR TYR ILE 0.47561 0.864865
60 TYR LEU LYS GLU PRO VAL HIS GLY VAL 0.47561 0.842857
61 VAL MET ALA PRO ARG THR LEU PHE LEU 0.475 0.824324
62 ARG THR TYR SEP GLY PRO MET ASN LYS VAL 0.474576 0.771084
63 VAL LYS VAL VAL ALA LYS LYS TYR ARG ASN 0.474453 0.742857
64 ARG GLN PRO ALA LYS ALA PRO LEU LEU 0.473333 0.84058
65 PHE PRO ARG 0.472441 0.8
66 TYR PRO PHE PHE NH2 0.472441 0.776119
67 THR PRO ARG ARG SER MLZ SER ALA 0.471014 0.783784
68 LEU PRO PHE GLU ARG ALA THR VAL MET 0.46988 0.824324
69 ARG MET PHE PRO ASN ALA PRO TYR LEU 0.46988 0.820513
70 LEU PRO PHE ASP LYS SER THR ILE MET 0.469512 0.736842
71 TYR PRO ASN VAL ASN ILE HIS ASN PHE 0.46875 0.797297
72 ILE GLY PRO GLY ARG ALA PHE TYR ALA 0.46875 0.941176
73 LYS ALA PRO ARG ALY GLN LEU ALA THR LYS 0.468085 0.797101
74 LYS PRO ILE VAL GLN TYR ASP ASN PHE 0.466258 0.808219
75 LYS GLN GLU PRO GLN GLU ILE ASP PHE 0.464968 0.80597
76 ILE ARG ALA ALA PRO PRO PRO LEU PHE 0.464516 0.897059
77 GLY ARG PRO ARG THR THR SER PHE ALA GLU 0.462963 0.84507
78 ALA ASN SER ARG ALY PRO THR SER ILE ILE 0.4625 0.810811
79 ARG PRO ARG PRO ASP ASP LEU GLU ILE 0.46 0.855072
80 ASN PRO ARG ALA MET GLN ALA LEU LEU 0.46 0.77027
81 ALA ARG MLZ SER ALA PRO ALA THR 0.459459 0.797297
82 ARG THR PHE SER PRO THR TYR GLY LEU 0.45679 0.851351
83 ARG PRO LYS PRO LEU VAL ASP PRO 0.456522 0.835821
84 SER ALA PRO ASP THR ARG PRO ALA 0.455782 0.819444
85 PRO LYS ARG PRO THR THR LEU ASN LEU PHE 0.455621 0.847222
86 ASN ARG PRO ILE LEU SER LEU 0.455172 0.794521
87 ILE ARG LYS ILE LEU PHE LEU ASP GLY ILE 0.455128 0.724638
88 MET CYS PRO ARG MET THR ALA VAL MET 0.455128 0.797297
89 GLU LEU LYS TPO GLU ARG TYR 0.453947 0.710526
90 GLY TYR GLN ASP TYR GLU PRO GLU ALA 0.453901 0.80597
91 GLY GLY LYS LYS LYS TYR ARG LEU 0.453237 0.80597
92 GLY GLY ARG LYS LYS TYR LYS LEU 0.453237 0.80597
93 GLY GLY LYS LYS ARG TYR LYS LEU 0.453237 0.80597
94 ARG ARG ARG GLU ARG SER PRO THR ARG 0.452703 0.802817
95 GLY LEU LEU GLY SER PRO VAL ARG ALA 0.452703 0.814286
96 LYS VAL PRO ARG ASN GLN ASP TRP LEU 0.451429 0.810811
97 GLY TYR GLU ASN PRO THR TYR LYS PHE PHE 0.451219 0.767123
98 PRO ARG PRO ILE LEU LEU PRO TRP ARG NH2 0.450617 0.842857
99 TYR LEU GLU PRO ALA PRO VAL THR ALA 0.450331 0.791667
100 ASN TYR THR PRO GLY PRO GLY THR ARG PHE 0.449704 0.863014
101 LYS ARG ARG ARG HIS PRO SER 0.449664 0.8
102 LEU PRO PRO LEU ASP ILE THR PRO TYR 0.448718 0.828571
103 ILE GLY PRO GLY ARG ALA PHE TYR THR 0.448485 0.927536
104 ILE GLY PRO GLY ARG ALA PHE TYR VAL 0.448485 0.927536
105 LEU PRO LYS MYK THR GLY GLY 0.448052 0.736111
106 TYR GLU LEU ASP GLU LYS PHE ASP ARG LEU 0.447368 0.746479
107 ILE GLY PRO GLY ARG ALA PHE TYR THR ILE 0.447059 0.901408
108 ILE SER PRO ARG THR LEU ASP ALA TRP 0.446328 0.84
109 LEU GLN ARG VAL LEU SEP ALA PRO PHE 0.44586 0.753247
110 CYS THR PRO SER ARG 0.445255 0.788732
111 LYS LEU TYR GLN ASN PRO THR THR TYR ILE 0.445122 0.783784
112 PHE ASN ARG PRO VAL 0.444444 0.814286
113 ASN GLY TYR GLU ASN PRO THR TYR LYS 0.444444 0.767123
114 TYR LEU ALA PRO GLY PRO VAL THR ALA 0.443709 0.805556
115 ALA ARG SER HIS SEP TYR PRO ALA 0.443114 0.78481
116 PHE ASN PHE PRO GLN ILE THR 0.442953 0.739726
117 LYS TYR TYR SER ILE ILE PRO HIS SER ILE 0.442308 0.810811
118 TYR TYR SER ILE ILE PRO HIS SER ILE 0.442308 0.810811
119 ALA ASN SER ARG LEU PRO THR SER ILE ILE 0.442177 0.830986
120 GLU LEU ARG ARG LYS MET MET TYR MET 0.442177 0.736111
121 ARG ARG ILE TYR ASP LEU ILE GLU LEU 0.440789 0.768116
122 TYR TYR SER ILE ALA PRO HIS SER ILE 0.440252 0.786667
123 ARG GLN PHE GLY PRO ASP TRP ILE VAL ALA 0.440217 0.847222
124 ALA PRO ASP THR ARG PRO 0.439716 0.830986
125 VAL MET ALA PRO ARG ALA LEU LEU LEU 0.439189 0.802817
126 TYR PRO TYR ASP VAL PRO ASP TYR ALA 0.438356 0.788732
127 ARG TYR PRO LEU THR PHE GLY TRP 0.438202 0.864865
128 LYS ARG ARG ARG HIS PRO SER GLY 0.437909 0.767123
129 ACE GLN GLU ARG GLU VAL PRO CYS 0.4375 0.811594
130 1IP CYS PHE SER LYS PRO ARG 0.4375 0.783784
131 THR PRO TYR ASP ILE ASN GLN MET LEU 0.435583 0.75
132 SER ARG ILE ARG ILE ARG GLY TYR VAL ARG 0.435374 0.75
133 ASP GLU LEU GLU ILE LYS ALA TYR 0.435374 0.705882
134 GLY ARG PHE ALA ALA ALA ILE ALA LYS 0.434483 0.757576
135 GLY HIS LYS ILE LEU HIS ARG LEU LEU GLN 0.434211 0.771429
136 PHE GLU ALA ILE PRO ALA GLU TYR LEU 0.433962 0.826087
137 ACE TYR PRO ILE GLN GLU THR 0.433333 0.838235
138 LEU PRO PRO GLU GLU ARG LEU ILE 0.432432 0.880597
139 LEU GLU LYS ALA ARG GLY SER THR TYR 0.432099 0.75
140 ARG LEU TYR HIS SEP LEU PRO ALA 0.431953 0.797468
141 GLU LEU PRO LEU VAL LYS ILE 0.431507 0.776119
142 LEU PRO PRO VAL VAL ALA LYS GLU ILE 0.431373 0.779412
143 ALA ARG LYS ILE ASP ASN LEU ASP 0.430556 0.661972
144 SER ASP ILE LEU PHE PRO ALA ASP SER 0.430464 0.75
145 TYR LEU GLU PRO GLY PRO VAL THR ALA 0.43038 0.816901
146 ALA GLN ASP ILE TYR ARG ALA SER TYR 0.43038 0.712329
147 ILE PRO ALA TYR GLY VAL LEU THR ILE 0.43038 0.828571
148 HIS SER ILE THR TYR LEU LEU PRO VAL 0.430303 0.810811
149 ALA ASN SER ARG TRP PRO THR SER ALY ILE 0.430168 0.818182
150 HIS LYS ILE LEU HIS ARG LEU LEU GLN ASP 0.429487 0.728571
151 ARG PRO GLN VAL PRO LEU ARG PRO MET 0.429487 0.805556
152 MET SER LEU PRO GLY ARG TRP LYS PRO LYS 0.429348 0.772152
153 SER ARG LYS ILE ASP ASN LEU ASP 0.428571 0.657534
154 PTR LEU ARG VAL ALA 0.428571 0.69863
155 PRO ARG ARG PRO VAL ILE MET ARG ARG 0.428571 0.802817
156 ALA PRO ASP THR ARG PRO ALA PRO 0.427586 0.830986
157 ALA ASN SER ARG HIS PRO THR SER ILE ILE 0.426752 0.861111
158 GLY LEU LEU GLY SEP PRO VAL ARG ALA 0.426752 0.727273
159 HIS LYS ILE LEU HIS ARG LEU LEU GLN GLU 0.425926 0.757143
160 LEU PRO PHE GLU LYS SER THR VAL MET 0.424242 0.723684
161 THR PRO ARG VAL THR GLY GLY GLY ALA MET 0.424051 0.776316
162 ARG GLN ALA SEP ILE GLU LEU PRO SER MET 0.423729 0.719512
163 ALA ASN SER ARG TRP PRO THR THR ARG LEU 0.423529 0.815789
164 ARG GLN PHE GLY PRO ASP PHE PRO THR ILE 0.421965 0.875
165 PHE TYR ALA PRO GLU PRO ILE THR SER LEU 0.421687 0.786667
166 SER THR GLY GLY VAL M3L LYS PRO HIS ARG 0.420765 0.75
167 ASP TYR GLU PRO ILE PRO GLU GLU ALA PHE 0.420732 0.828571
168 LEU SER SER PRO VAL THR LYS SER PHE 0.420382 0.760563
169 ALA ARG THR MLY GLN THR ALA ARG TYR 0.42 0.746667
170 SER ILE TYR PHE TPO PRO GLU LEU TYR ASP 0.41954 0.7375
171 ALA PRO PRO PRO ARG PRO PRO LYS PRO 0.41844 0.791045
172 ILE LEU LYS GLU PRO VAL HIS GLY VAL 0.418182 0.797101
173 GLU TYR GLY PRO LYS TRP ASN LYS 0.418182 0.739726
174 ARG TYR PRO LEU THR LEU GLY TRP CYS PHE 0.417989 0.842105
175 TYR LEU GLY GLY PRO ASP PHE PRO THR ILE 0.417647 0.808219
176 SER ARG ASP HIS SER ARG THR PRO MET 0.417647 0.792208
177 ALA ALA ARG KCR SER ALA PRO ALA 0.416667 0.802817
178 PHE PRO ARG PRO TRP LEU HIS GLY LEU 0.416667 0.821918
179 TYR SEP PRO THR SEP PRO SER 0.416667 0.75
180 GLY MET PRO ARG GLY ALA 0.416667 0.802817
181 VAL SER GLN ASN TYR PRO ILE VAL GLN ASN 0.416667 0.780822
182 GLY GLN VAL PRO PHE SER LYS GLU GLU CYS 0.416149 0.716216
183 ASP ARG VAL TYR ILE HIS PRO PHE 0.415493 0.852941
184 GLU SER ASP PRO ILE VAL ALA GLN TYR 0.414634 0.805556
185 ALA ARG THR LYS GLN THR ALA ARG LYS 0.414286 0.642857
186 ASN ALA LEU LEU ARG TYR LEU LEU ASP 0.413793 0.71831
187 ALA ASN SER ARG TRP PRO THR SER FAK ILE 0.413043 0.797468
188 SER LEU SER ARG THR PRO ALA ASP GLY ARG 0.4125 0.816901
189 ALA ARG THR M3L GLN THR ALA ALA LYS ALA 0.410959 0.649351
190 LEU PRO SER PHE GLU THR ALA LEU 0.410256 0.75
191 ARG VAL SER PRO SER THR SER TYR THR PRO 0.409722 0.774648
192 SER PRO ARG LEU PRO LEU LEU GLU SER 0.409722 0.848485
193 ALA ASN SER ARG TRP PRO THR SER 2KK ILE 0.409574 0.7875
194 PHE LEU TRP GLY PRO ARG ALA LEU VAL 0.409091 0.84507
195 TYR MET PHE PRO ASN ALA PRO TYR LEU 0.408537 0.730769
196 SER GLU ILE GLU PHE ALA ARG LEU 0.407895 0.676056
197 ALA ARG THR GLU LEU TYR ARG SER LEU 0.407895 0.722222
198 ASP ARG VAL GLU LEU ASN ALA PRO ARG GLN 0.407643 0.802817
199 DMG PRO ARG ARG ARG SER ARG LYS PRO 0.407407 0.791667
200 SER ASP TYR GLN ARG LEU 0.407143 0.75
201 ARG PHE PRO LEU THR PHE GLY TRP 0.40678 0.837838
202 SER SER GLY LYS VAL PRO LEU 0.405594 0.732394
203 GLN PRO PRO VAL PRO PRO GLN ARG PRO MET 0.405063 0.805556
204 GLN ALA SER TPO PRO ARG NIT 0.404762 0.705882
205 SER ARG TYR TRP ALA ILE ARG THR ARG 0.404762 0.77027
206 SER SER GLY LYS VAL PRO LEU SER 0.40411 0.722222
207 ARG SEP PRO VAL PHE SER 0.403727 0.75
208 LEU TYR ALA SER PRO GLN LEU GLU GLY PHE 0.403509 0.791667
209 VAL TYR PRO IAS HIS ALA 0.402597 0.791667
210 LEU LEU PHE GLY LYS PRO VAL TYR VAL 0.402439 0.828571
211 PHE ARG TYR LEU GLY 0.401408 0.753623
212 ILE PRO LEU THR GLU GLU ALA GLU LEU 0.401361 0.757143
213 ARG ARG ALA SEP ALA PRO LEU PRO 0.401274 0.74026
214 ACE ARG THR PRO SEP LEU PRO THR PIP 0.401274 0.759494
215 ARG TYR PRO LEU THR PHE GLY TRP CYS PHE 0.401042 0.828947
216 ASP PHE GLU GLU ILE PRO GLY GLU TYR LEU 0.4 0.842857
Ligand no: 2; Ligand: SAH; Similar ligands found: 211
No: Ligand ECFP6 Tc MDL keys Tc
1 SAH 1 1
2 5X8 0.759494 0.969697
3 A7D 0.734177 0.926471
4 TT8 0.709302 0.970588
5 DSH 0.692308 0.914286
6 SXZ 0.692308 0.916667
7 DTA 0.666667 0.857143
8 3DH 0.662338 0.869565
9 S8M 0.655556 0.901408
10 SFG 0.635294 0.954545
11 SA8 0.62069 0.915493
12 EEM 0.617977 0.890411
13 MTA 0.615385 0.869565
14 SAI 0.613636 0.955882
15 S7M 0.586957 0.916667
16 36A 0.586538 0.90411
17 K15 0.583333 0.878378
18 ADN 0.573333 0.84058
19 RAB 0.573333 0.84058
20 XYA 0.573333 0.84058
21 62X 0.572917 0.855263
22 5CD 0.571429 0.852941
23 0UM 0.5625 0.876712
24 5N5 0.558442 0.84058
25 A4D 0.551282 0.867647
26 SAM 0.537634 0.916667
27 SMM 0.536842 0.88
28 SSA 0.536842 0.712644
29 KB1 0.534653 0.902778
30 A5D 0.532609 0.857143
31 SIB 0.53125 0.928571
32 EP4 0.530864 0.819444
33 DSZ 0.530612 0.732558
34 GSU 0.53 0.752941
35 A 0.529412 0.763158
36 LMS 0.529412 0.694118
37 AMP 0.529412 0.763158
38 5CA 0.525773 0.712644
39 ME8 0.524752 0.8125
40 M2T 0.52439 0.821918
41 6RE 0.523256 0.824324
42 GJV 0.522727 0.813333
43 AAT 0.515789 0.863014
44 LSS 0.515152 0.696629
45 KAA 0.514852 0.727273
46 J7C 0.511364 0.835616
47 A5A 0.510417 0.697674
48 SON 0.505495 0.805195
49 SRP 0.505155 0.805195
50 F0P 0.504505 0.915493
51 54H 0.5 0.681818
52 VMS 0.5 0.681818
53 ADX 0.5 0.694118
54 CA0 0.5 0.769231
55 AMO 0.5 0.805195
56 5AL 0.5 0.779221
57 KH3 0.5 0.866667
58 NVA LMS 0.49505 0.707865
59 AHX 0.49505 0.753086
60 TSB 0.494949 0.689655
61 53H 0.494949 0.674157
62 G5A 0.494737 0.712644
63 ABM 0.494382 0.74359
64 A2D 0.494382 0.74359
65 ZAS 0.494253 0.808219
66 A6D 0.490196 0.759494
67 8QN 0.49 0.779221
68 GEK 0.49 0.956522
69 GAP 0.489583 0.769231
70 AN2 0.48913 0.734177
71 A3S 0.48913 0.884058
72 S4M 0.488889 0.831169
73 SRA 0.488636 0.746835
74 LAD 0.485437 0.810127
75 52H 0.484848 0.674157
76 A12 0.483516 0.759494
77 BA3 0.483516 0.74359
78 AP2 0.483516 0.759494
79 NEC 0.483146 0.788732
80 AOC 0.483146 0.842857
81 Y3J 0.481481 0.768116
82 VRT 0.479167 0.861111
83 50T 0.478723 0.734177
84 B4P 0.478261 0.74359
85 ADP 0.478261 0.74359
86 5AS 0.478261 0.655556
87 AP5 0.478261 0.74359
88 A3N 0.477778 0.830986
89 YSA 0.476636 0.712644
90 XAH 0.476636 0.768293
91 0XU 0.473684 0.897059
92 AT4 0.473118 0.7375
93 WAQ 0.471154 0.807692
94 NSS 0.470588 0.712644
95 5AD 0.468354 0.791045
96 AU1 0.468085 0.725
97 M33 0.468085 0.734177
98 MAO 0.467391 0.797468
99 TXA 0.466667 0.759494
100 NB8 0.466667 0.775
101 A3G 0.466667 0.871429
102 3AM 0.465909 0.727273
103 DAL AMP 0.465347 0.779221
104 8X1 0.465347 0.707865
105 A3T 0.463158 0.842857
106 ATP 0.463158 0.74359
107 HEJ 0.463158 0.74359
108 ACP 0.463158 0.746835
109 7D7 0.4625 0.785714
110 LEU LMS 0.461538 0.688889
111 9ZA 0.460784 0.740741
112 9ZD 0.460784 0.740741
113 5FA 0.458333 0.74359
114 AQP 0.458333 0.74359
115 AR6 0.458333 0.766234
116 APC 0.458333 0.759494
117 APR 0.458333 0.766234
118 PRX 0.458333 0.746835
119 F2R 0.457627 0.75
120 IOT 0.456897 0.761905
121 4AD 0.456311 0.794872
122 PAJ 0.456311 0.722892
123 WSA 0.45614 0.72093
124 YAP 0.453704 0.794872
125 8PZ 0.453704 0.712644
126 FA5 0.453704 0.805195
127 ADP PO3 0.453608 0.763158
128 ADV 0.453608 0.782051
129 NVA 2AD 0.453608 0.849315
130 SAP 0.453608 0.728395
131 AGS 0.453608 0.728395
132 RBY 0.453608 0.782051
133 AD9 0.453608 0.725
134 PTJ 0.45283 0.731707
135 MHZ 0.452632 0.797468
136 00A 0.451923 0.740741
137 A3P 0.451613 0.74026
138 YLP 0.451327 0.771084
139 7MD 0.45045 0.768293
140 ALF ADP 0.45 0.707317
141 ADP ALF 0.45 0.707317
142 2VA 0.447917 0.819444
143 OOB 0.446602 0.779221
144 ANP 0.444444 0.725
145 T99 0.444444 0.7375
146 ACQ 0.444444 0.746835
147 TAT 0.444444 0.7375
148 P5A 0.443396 0.719101
149 7D5 0.443182 0.708861
150 A1R 0.442308 0.7625
151 YLC 0.439655 0.790123
152 2AM 0.438202 0.717949
153 DLL 0.438095 0.779221
154 ARG AMP 0.4375 0.759036
155 A22 0.436893 0.734177
156 D3Y 0.436893 0.859155
157 ATF 0.435644 0.716049
158 MYR AMP 0.435185 0.746988
159 80F 0.434426 0.75
160 SO8 0.434343 0.808219
161 OAD 0.433962 0.769231
162 3UK 0.433962 0.769231
163 TAD 0.433628 0.765432
164 25A 0.432692 0.74359
165 6YZ 0.431373 0.746835
166 VO4 ADP 0.431373 0.734177
167 ADP VO4 0.431373 0.734177
168 9SN 0.431193 0.731707
169 TYM 0.431034 0.805195
170 B5V 0.429907 0.759494
171 PR8 0.429907 0.8
172 ADQ 0.428571 0.746835
173 YLB 0.42735 0.771084
174 9K8 0.425926 0.67033
175 1ZZ 0.425926 0.746988
176 FYA 0.425926 0.779221
177 3OD 0.425926 0.769231
178 PPS 0.425743 0.674419
179 MAP 0.423077 0.707317
180 A2P 0.421053 0.727273
181 4YB 0.421053 0.735632
182 9X8 0.420561 0.75
183 ADP BMA 0.420561 0.746835
184 TYR AMP 0.419643 0.794872
185 5SV 0.419048 0.731707
186 3NZ 0.416667 0.824324
187 YLA 0.416667 0.771084
188 8Q2 0.415254 0.688889
189 A3R 0.415094 0.7625
190 B5Y 0.414414 0.75
191 B5M 0.414414 0.75
192 48N 0.413793 0.753086
193 LPA AMP 0.413793 0.768293
194 AYB 0.413223 0.761905
195 ACK 0.413043 0.710526
196 QQY 0.413043 0.696203
197 BIS 0.412844 0.719512
198 JB6 0.412844 0.7625
199 PAP 0.41 0.730769
200 DQV 0.408696 0.75641
201 OVE 0.408602 0.7125
202 AMP DBH 0.40708 0.746835
203 4UV 0.40708 0.75
204 3AD 0.406977 0.852941
205 AF3 ADP 3PG 0.40678 0.743902
206 OMR 0.40678 0.738095
207 LAQ 0.405172 0.768293
208 A A 0.40367 0.74359
209 7C5 0.403509 0.789474
210 7MC 0.403361 0.75
211 4UU 0.4 0.75
Similar Binding Sites (Proteins are less than 50% similar to leader)
Pocket No.: 1; Query (leader) PDB : 5E1M; Ligand: PRO PRO LYS ARG ILE ALA; Similar sites found with APoc: No similar binding sites found, or similarity not calculated due to duplicate pocket.
This union binding pocket(no: 1) in the query (biounit: 5e1m.bio2) has 54 residues
No: Leader PDB Ligand Sequence Similarity
Pocket No.: 2; Query (leader) PDB : 5E1M; Ligand: SAH; Similar sites found with APoc: No similar binding sites found, or similarity not calculated due to duplicate pocket.
This union binding pocket(no: 2) in the query (biounit: 5e1m.bio2) has 54 residues
No: Leader PDB Ligand Sequence Similarity
Pocket No.: 3; Query (leader) PDB : 5E1M; Ligand: SAH; Similar sites found with APoc: No similar binding sites found, or similarity not calculated due to duplicate pocket.
This union binding pocket(no: 3) in the query (biounit: 5e1m.bio1) has 42 residues
No: Leader PDB Ligand Sequence Similarity
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