Receptor
PDB id Resolution Class Description Source Keywords
1G37 2 Å EC: 3.4.21.5 CRYSTAL STRUCTURE OF HUMAN ALPHA-THROMBIN COMPLEXED WITH BCH EXOSITE-DIRECTED PEPTIDE HOMO SAPIENS PROTEASE THROMBIN INHIBITOR BLOOD CLOTTING HYDROLASE-HYDINHIBITOR COMPLEX
Ref.: POTENT AND SELECTIVE BICYCLIC LACTAM INHIBITORS OF PART 4: TRANSITION STATE INHIBITORS. BIOORG.MED.CHEM.LETT. V. 11 287 2001
Ligand
Ligand Chain:Residue Validity Ligand Warnings Binding Data NGL Viewer Molecular Weight (Da) Formula SMILES
110 A:900;
 Invalid;
 none;
 submit data
574.689 C28 H38 N4 O7 S CCCCO...
PHE GLU ALA ILE PRO ALA GLU TYR LEU B:356;
 Valid;
 none;
 submit data
1050.18 n/a O=C([...
View in 3D viewer
90% Homology Family
Leader
PDB id Resolution Class Description Source Keywords
1D9I 2.3 Å EC: 3.4.21.5 STRUCTURE OF THROMBIN COMPLEXED WITH SELECTIVE NON-ELECTOPHI INHIBITORS HAVING CYCLOHEXYL MOIETIES AT P1 HOMO SAPIENS GLOBULAR HYDROLASE-HYDROLASE INHIBITOR COMPLEX
Ref.: STRUCTURE OF THROMBIN COMPLEXED WITH SELECTIVE NON-ELECTROPHILIC INHIBITORS HAVING CYCLOHEXYL MOIE P1. ACTA CRYSTALLOGR.,SECT.D V. 56 294 2000
Members (9)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 27 families.
1 1D9I Ki = 0.78 nM 00P C22 H29 N5 O5 S c1ccc(cc1)....
2 1JWT Ki = 14 nM BLI C22 H32 N6 O5 S c1ccc(cc1)....
3 1XM1 - GAH C38 H61 N11 O6 [H]/N=C(N)....
4 1HAG - ASP PHE GLU GLU ILE PRO GLU GLU TYS LEU n/a n/a
5 1ZGV ic50 ~ 1 uM 501 C17 H21 Cl N6 CCCCNc1cc(....
6 2BDY ic50 = 0.017 uM UNB C27 H26 N4 O4 S [H]/N=C(c1....
7 1G37 - PHE GLU ALA ILE PRO ALA GLU TYR LEU n/a n/a
8 1ZGI Ki = 4.6 uM 382 C22 H23 F2 N7 O c1ccc(c(c1....
9 1D6W Ki = 1100 nM 00R C24 H29 N7 O5 S c1ccc(cc1)....
70% Homology Family (9)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 19 families.
1 1D9I Ki = 0.78 nM 00P C22 H29 N5 O5 S c1ccc(cc1)....
2 1JWT Ki = 14 nM BLI C22 H32 N6 O5 S c1ccc(cc1)....
3 1XM1 - GAH C38 H61 N11 O6 [H]/N=C(N)....
4 1HAG - ASP PHE GLU GLU ILE PRO GLU GLU TYS LEU n/a n/a
5 1ZGV ic50 ~ 1 uM 501 C17 H21 Cl N6 CCCCNc1cc(....
6 2BDY ic50 = 0.017 uM UNB C27 H26 N4 O4 S [H]/N=C(c1....
7 1G37 - PHE GLU ALA ILE PRO ALA GLU TYR LEU n/a n/a
8 1ZGI Ki = 4.6 uM 382 C22 H23 F2 N7 O c1ccc(c(c1....
9 1D6W Ki = 1100 nM 00R C24 H29 N7 O5 S c1ccc(cc1)....
50% Homology Family (9)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 16 families.
1 1D9I Ki = 0.78 nM 00P C22 H29 N5 O5 S c1ccc(cc1)....
2 1JWT Ki = 14 nM BLI C22 H32 N6 O5 S c1ccc(cc1)....
3 1XM1 - GAH C38 H61 N11 O6 [H]/N=C(N)....
4 1HAG - ASP PHE GLU GLU ILE PRO GLU GLU TYS LEU n/a n/a
5 1ZGV ic50 ~ 1 uM 501 C17 H21 Cl N6 CCCCNc1cc(....
6 2BDY ic50 = 0.017 uM UNB C27 H26 N4 O4 S [H]/N=C(c1....
7 1G37 - PHE GLU ALA ILE PRO ALA GLU TYR LEU n/a n/a
8 1ZGI Ki = 4.6 uM 382 C22 H23 F2 N7 O c1ccc(c(c1....
9 1D6W Ki = 1100 nM 00R C24 H29 N7 O5 S c1ccc(cc1)....
Polypharmacology
Similar Ligands (2D)
Ligand no: 1; Ligand: PHE GLU ALA ILE PRO ALA GLU TYR LEU; Similar ligands found: 219
No: Ligand ECFP6 Tc MDL keys Tc
1 PHE GLU ALA ILE PRO ALA GLU TYR LEU 1 1
2 ASP TYR GLU PRO ILE PRO GLU GLU ALA PHE 0.673611 0.9375
3 LYS LEU PRO ALA GLN PHE TYR ILE LEU 0.662162 0.968254
4 PHE TYR ALA PRO GLU PRO ILE THR SER LEU 0.648649 0.884058
5 LEU PRO SER PHE GLU THR ALA LEU 0.605634 0.820895
6 TYR MET PHE PRO ASN ALA PRO TYR LEU 0.582781 0.84507
7 ASP PHE GLU GLU ILE PRO GLY GLU TYR LEU 0.576923 0.953125
8 PHE ALA PRO GLY ASN TYR PRO ALA LEU 0.576159 0.882353
9 TRP GLU TYR ILE PRO ASN VAL 0.566879 0.910448
10 ASP PHE GLU GLU ILE PRO GLY GLU TYS LEU 0.566879 0.75
11 LEU TYR ALA SER PRO GLN LEU GLU GLY PHE 0.559748 0.923077
12 SER ILE TYR PHE TPO PRO GLU LEU TYR ASP 0.554878 0.824324
13 ILE PRO LEU THR GLU GLU ALA GLU LEU 0.539568 0.830769
14 ASP PHE GLU GLU ILE PRO GLU GLU TYS 0.535948 0.746835
15 TYR GLN PHE GLY PRO ASP PHE PRO ILE ALA 0.534162 0.923077
16 LEU PRO PHE GLU ARG ALA THR ILE MET 0.53012 0.736842
17 GLU GLU TYR LEU GLN ALA PHE THR TYR 0.527397 0.71875
18 TYR TYR SER ILE ILE PRO HIS SER ILE 0.522876 0.830986
19 GLU SER ASP PRO ILE VAL ALA GLN TYR 0.518987 0.880597
20 GLN ILE MET TYR ASN TYR PRO ALA MET 0.518987 0.869565
21 ALA PRO GLN PRO ALA PRO GLU ASN ALA TYR 0.516556 0.835821
22 ALA ILE MET PRO ALA ARG PHE TYR PRO LYS 0.514451 0.797297
23 ALA THR PRO PHE GLN GLU 0.514085 0.84127
24 PRO GLN PTR GLU PTR ILE PRO ALA 0.509677 0.830986
25 ILE PRO ALA TYR GLY VAL LEU THR ILE 0.509677 0.907692
26 ALA PRO ALA TRP LEU PHE GLU ALA 0.509434 0.861538
27 ARG MET PHE PRO ASN ALA PRO TYR LEU 0.508982 0.769231
28 ASP ALA ASP GLU TYR LEU 0.507576 0.68254
29 GLY TYR GLN ASP TYR GLU PRO GLU ALA 0.507143 0.887097
30 ASP TYR ASN PRO TYR LEU LEU PHE LEU LYS 0.506494 0.895522
31 TYR LEU GLU PRO ALA PRO VAL THR ALA 0.503311 0.865672
32 THR PRO TYR ASP ILE ASN GLN MET LEU 0.503106 0.842857
33 PHE LEU PRO HIS ALY TYR ASP VAL LYS LEU 0.502924 0.852941
34 LEU PRO PHE GLU ARG ALA THR VAL MET 0.5 0.723684
35 LYS PRO ILE VAL GLN TYR ASP ASN PHE 0.49697 0.910448
36 PHE ALA PRO GLY ASN TYI PRO ALA LEU 0.496894 0.821918
37 ASP ILE ASN TYR TYR ALA SER GLU PRO 0.496774 0.882353
38 PHE GLN PRO GLN ASN GLY GLN PHE ILE 0.496774 0.833333
39 ALA ILE ALA TYR PHE ILE PRO ASP GLN ALA 0.496504 0.95082
40 ALA PHE ARG ILE PRO LEU THR ARG 0.493671 0.753425
41 PRO GLN PTR GLU GLU ILE PRO ILE 0.49359 0.802817
42 ARG ILE PRO SER TYR ARG TYR ARG TYR 0.493421 0.783784
43 ARG ARG LEU PRO ILE PHE SER ARG LEU 0.490566 0.72973
44 TYR PRO PHE PHE NH2 0.48855 0.885246
45 ARG THR PHE SER PRO THR TYR GLY LEU 0.487805 0.821918
46 GLU TYR LEU GLY LEU ASP VAL PRO VAL 0.487179 0.920635
47 ALA VAL ALA PHE TYR ILE PRO ASP GLN ALA 0.482759 0.967213
48 PHE LEU ALA TYR LYS 0.481752 0.774194
49 TRP ASP ILE PRO PHE 0.481203 0.854839
50 TYR GLU LEU ASP GLU LYS PHE ASP ARG LEU 0.480519 0.690141
51 SER ALA GLU PRO VAL PRO LEU GLN LEU 0.47973 0.779412
52 ASP PHE GLU GLU ILE PRO GLY GLU PTR 0.479042 0.819444
53 ILE GLY PRO GLY ARG ALA PHE TYR VAL 0.479042 0.897059
54 ILE GLY PRO GLY ARG ALA PHE TYR THR 0.479042 0.869565
55 PHE PRO THR LYS ASP VAL ALA LEU 0.477987 0.820895
56 PHE ASN PHE PRO GLN ILE THR 0.476821 0.863636
57 ILE GLY PRO GLY ARG ALA PHE TYR THR ILE 0.476744 0.84507
58 PHE GLU ALA ASN GLY ASN LEU ILE 0.47619 0.651515
59 VAL PRO LEU THR GLU ASP ALA GLU LEU 0.47619 0.815385
60 PHE LEU PRO SER ASP PHE PHE PRO SER VAL 0.473684 0.838235
61 TYR LEU GLY GLY PRO ASP PHE PRO THR ILE 0.473373 0.910448
62 GLY TYR GLU ASN PRO THR TYR LYS PHE PHE 0.473054 0.838235
63 ILE GLY PRO GLY ARG ALA PHE TYR ALA 0.472727 0.882353
64 ACE LEU TYR ALA SER SER ASN PRO ALA PTR 0.47205 0.789474
65 LEU LEU PHE GLY TYR PRO VAL TYR VAL 0.471698 0.967742
66 LEU LEU PHE GLY PHE PRO VAL TYR VAL 0.471698 0.967742
67 ILE LEU ALA LYS PHE LEU HIS GLU LEU 0.470588 0.742424
68 LEU ALA ILE TYR SER 0.469697 0.671875
69 LYS GLN GLU PRO GLN GLU ILE ASP PHE 0.469136 0.828125
70 LEU LEU PHE GLY LYS PRO VAL TYR VAL 0.469136 0.968254
71 ARG PRO PRO ILE PHE ILE ARG ARG LEU 0.46875 0.771429
72 SER SER LEU GLU ASN PHE ALA ALA TYR VAL 0.467532 0.676471
73 ACE TYR PRO ILE GLN GLU THR 0.467105 0.920635
74 LYS LEU TYR GLN ASN PRO THR THR TYR ILE 0.467066 0.882353
75 ASP PHE GLN GLU SER ALA ASP SER PHE LEU 0.465753 0.656716
76 PHE ALA PRO GLY PHE PHE PRO TYR LEU 0.465409 0.907692
77 TYR TYR SER ILE ALA PRO HIS SER ILE 0.462963 0.805556
78 TYR LEU GLU PRO GLY PRO VAL THR VAL 0.4625 0.865672
79 TYR LEU GLU PRO GLY PRO VAL THR ALA 0.4625 0.865672
80 LEU PHE GLY TYR PRO VAL TYR VAL 0.461538 0.967742
81 VAL MET ALA PRO ARG THR LEU PHE LEU 0.461078 0.701299
82 PHE LEU ARG GLY ARG ALA TYR VAL LEU 0.459119 0.710145
83 GLY ARG PRO ARG THR THR SER PHE ALA GLU 0.458333 0.716216
84 ARG ILE ILE PRO ARG HIS LEU GLN LEU 0.457831 0.75
85 ASP ILE ALA TYR TYR THR SER GLU PRO 0.457516 0.895522
86 PHE ALA PRO GLY ASN TYR PRO ALA TRP 0.457143 0.828571
87 PHE TYR ARG ALA LEU MET 0.456954 0.652778
88 GLY GLN VAL PRO PHE SER LYS GLU GLU CYS 0.45679 0.757143
89 SER PRO ILE VAL PRO SER PHE ASP MET 0.45679 0.777778
90 ACE ILE TYR GLU SER LEU 0.455882 0.666667
91 TYR ASP LEU SEP LEU PRO PHE PRO 0.454545 0.821918
92 ARG LEU TYR GLN ASN PRO THR THR TYR ILE 0.453488 0.810811
93 PRO ALA ILE LEU TYR ALA LEU LEU SER SER 0.453333 0.776119
94 TYR PRO TYR ASP VAL PRO ASP TYR ALA 0.453333 0.921875
95 ACE GLN PM3 GLU GLU ILE PRO 0.452703 0.768116
96 HIS SER ILE THR TYR LEU LEU PRO VAL 0.452381 0.830986
97 PHE LEU ARG GLY ARG ALA TYR GLY LEU 0.45098 0.710145
98 LYS TYR TYR SER ILE ILE PRO HIS SER ILE 0.450617 0.830986
99 ASP GLU LEU GLU ILE LYS ALA TYR 0.450331 0.75
100 ASN GLY TYR GLU ASN PRO THR TYR LYS 0.449102 0.838235
101 ASP PHE ALA ASN THR PHE LEU PRO 0.448052 0.878788
102 SER GLY ILE PHE LEU GLU THR SER 0.446809 0.626866
103 GLU ILE ILE ASN PHE GLU LYS LEU 0.446667 0.651515
104 PTR VAL PRO MET LEU 0.446667 0.767123
105 LEU PRO PHE GLU LYS SER THR VAL MET 0.446429 0.763889
106 TYR PRO ASN VAL ASN ILE HIS ASN PHE 0.446429 0.897059
107 GLU GLU PRO THR VAL ILE LYS LYS TYR 0.445783 0.893939
108 SER SER PHE TYR PRO SEP ALA GLU GLY 0.44375 0.791667
109 THR PRO ASP TYR PHE LEU 0.442029 0.857143
110 LYS PRO PHE PTR VAL ASN VAL GLU PHE 0.44186 0.783784
111 GLU PRO VAL GLU THR THR ASP TYR 0.441558 0.876923
112 SER ILE ILE GLN PHE GLU HIS LEU 0.441558 0.685714
113 ARG PRO MET THR TYR LYS GLY ALA LEU 0.441341 0.753247
114 DHI PRO PHE HIS LEU LEU VAL TYR 0.441176 0.907692
115 TYR LEU ALA PRO GLY PRO VAL THR ALA 0.43949 0.852941
116 GLU GLU TYR LEU LYS ALA TRP THR PHE 0.439306 0.779412
117 GLN ASN TYR PRO ILE VAL GLN 0.43871 0.921875
118 ASP PHE GLU GLU ILE PRO GLU GLU TYS LEU 0.438202 0.759494
119 ASN TYR THR PRO GLY PRO GLY ILE ARG PHE 0.438202 0.810811
120 PHE ARG TYR LEU GLY 0.4375 0.720588
121 LEU PRO PHE GLU LEU ARG GLY HIS LEU VAL 0.4375 0.774648
122 TYR LEU LYS GLU PRO VAL HIS GLY VAL 0.436782 0.893939
123 LYS PRO SEP GLN GLU LEU 0.43662 0.69863
124 ILE THR ASP GLN VAL PRO PHE SER VAL 0.436364 0.835821
125 PHE SER ALA PTR PRO SER GLU GLU ASP 0.435897 0.743243
126 ARG PRO MET THR PHE LYS GLY ALA LEU 0.435754 0.714286
127 GLN MET PRO THR GLU ASP GLU TYR 0.435583 0.814286
128 ILE MET ASP GLN VAL PRO PHE SER VAL 0.434524 0.774648
129 SER ILE ILE ASN PHE GLU LYS LEU 0.434211 0.647059
130 TYR PRO LYS ARG ILE ALA 0.433962 0.826087
131 GLU ASN LEU TYR PHE GLN 0.433566 0.71875
132 GLY ASN TYR SER PHE TYR ALA LEU 0.433566 0.676471
133 PRO PRO ALA TYR PRO PRO PRO PRO VAL PRO 0.433333 0.875
134 TYR PRO TYR 0.433071 0.885246
135 ILE ARG ALA ALA PRO PRO PRO LEU PHE 0.432927 0.760563
136 ASN ARG PRO VAL TYR ILE PRO ARG PRO PRO 0.432927 0.814286
137 LEU PRO PHE ASP LYS THR THR ILE MET 0.431953 0.788732
138 GLY ALA ASP ILE PHE TYR LEU ASP GLY ALA 0.431507 0.714286
139 ACE ALA GLU GLY PHE PRO ALA TPO VAL 0.430556 0.732394
140 PHE LEU SER TYR LYS 0.429577 0.727273
141 GLY ILE LEU GLU PHE VAL PHE THR LEU 0.42953 0.692308
142 ARG ARG ILE TYR ASP LEU ILE GLU LEU 0.427673 0.661972
143 TYR ASP GLN ILE LEU 0.427536 0.709677
144 LEU PRO PRO LEU ASP ILE THR PRO TYR 0.426829 0.907692
145 ASP ILE ASN TYR TYR THR SER GLU PRO 0.425926 0.882353
146 THR ASN GLU PHE TYR ALA 0.425532 0.651515
147 TYR GLN PHE 0.425197 0.672131
148 ASP PHE GLU GLU ILE 0.424242 0.629032
149 SER SER LEU GLU ASN PHE ARG ALA TYR VAL 0.423529 0.648649
150 PRO GLN PTR ILE PTR VAL PRO ALA 0.423313 0.84507
151 SER GLU ASP GLU PHE TYR ASP ALA LEU SER 0.423077 0.712121
152 LEU PRO PHE ASP LYS SER THR ILE MET 0.422857 0.777778
153 LYS PRO ILE VAL VAL LEU HIS GLY TYR 0.422857 0.909091
154 TYR SEP PRO THR SEP PRO SER 0.422819 0.72
155 ARG GLN PRO ALA LYS ALA PRO LEU LEU 0.42236 0.732394
156 ARG GLN ALA SEP ILE GLU LEU PRO SER MET 0.420765 0.630952
157 PHE SER HIS PRO GLN ASN THR 0.420732 0.760563
158 LYS THR PHE PRO PRO THR GLU PRO LYS 0.420732 0.80597
159 TYR GLY GLY PHE LEU 0.42029 0.774194
160 LEU ASP GLU GLU THR GLY GLU PHE LEU 0.42 0.666667
161 LEU PRO PHE ASP ARG THR THR ILE MET 0.41954 0.727273
162 GLU PHE SER PRO 0.419118 0.769231
163 ARG GLN PHE GLY PRO ASP PHE PRO THR ILE 0.418994 0.794521
164 LEU PRO PRO VAL VAL ALA LYS GLU ILE 0.41875 0.828125
165 ARG VAL ALA GLN LEU GLU GLN VAL TYR ILE 0.41875 0.691176
166 SER GLN TYR TYR TYR ASN SER LEU 0.41844 0.676471
167 DTY ILE ARG LEU LPD 0.418301 0.838235
168 GLU GLY GLN PTR GLN PRO GLN PRO ALA 0.418182 0.760563
169 ASP PHE GLU ASP TYR GLU PHE ASP 0.417266 0.661538
170 VAL ASN ASP ILE PHE GLU ALA ILE 0.417219 0.615385
171 SER PHE PHE GLU ASP ASN PHE VAL PRO GLU 0.416667 0.823529
172 ASP VAL GLN THR GLY ARG ARG PRO TYR GLU 0.416185 0.780822
173 GLN VAL PRO SER ASP PRO TYR ASN TYR 0.416149 0.826087
174 ILE LEU ALA LYS PHE LEU HIS THR LEU 0.416149 0.724638
175 LEU ASN PHE PRO ILE SER PRO 0.414474 0.811594
176 ASN TYR THR PRO GLY PRO GLY THR ARG PHE 0.413408 0.783784
177 GLU LEU ASP LYS TYR ALA SER 0.413333 0.712121
178 ALA THR ALA ALA ALA THR GLU ALA TYR 0.413043 0.630769
179 SER ILE ILE GLY PHE GLU LYS LEU 0.412903 0.681818
180 GLU ALA ASP PRO THR GLY HIS SER TYR 0.412429 0.802817
181 ALA LEU MET PRO GLY GLN PHE PHE VAL 0.412121 0.833333
182 ALA VAL PRO ILE ALA GLN 0.411348 0.852459
183 MET TYR TRP TYR PRO TYR 0.411043 0.838235
184 GLN LEU SER PRO PHE PRO PHE ASP LEU 0.411043 0.850746
185 ACE GLU LEU LEU MET VAL PRO ASP MET TYR 0.411043 0.878788
186 SER GLU CYS THR THR PRO CYS 0.410959 0.75
187 ALA ALA SER LEU TYR GLU LYS LYS ALA ALA 0.410596 0.701493
188 THR ASN GLU PHE TYR PHE 0.410448 0.640625
189 ASP TYR ILE ASN THR ASN VAL LEU PRO 0.409938 0.893939
190 ASN PRO ARG ALA MET GLN ALA LEU LEU 0.409938 0.671053
191 PRO GLU ALA THR ALA PRO PRO GLU GLU 0.409091 0.764706
192 ASN ARG PRO VAL TYR ILE PRO PRO PRO PRO 0.409091 0.890625
193 ARG LEU PRO ALA LYS ALA PRO LEU LEU 0.408805 0.71831
194 ACE GLY LYS SER PHE SER LYS PRO ARG 0.408805 0.742857
195 DPN PRO DAR ILE NH2 0.408163 0.735294
196 PHE GLN TRP MET GLY TYR GLU LEU TRP 0.408046 0.768116
197 SER LEU TYR ASN THR ILE ALA THR LEU 0.407895 0.647059
198 GLU GLN TYR LYS PHE TYR SER VAL 0.407895 0.716418
199 ASP ASP LEU ASP VAL PRO SER PHE LEU GLN 0.407407 0.820895
200 SER LEU PHE HIS 22G THR PRO 0.40678 0.830986
201 PHE LEU TRP GLY PRO ARG ALA LEU VAL 0.406593 0.788732
202 GLN VAL PRO LEU ARG PRO MET THR TYR LYS 0.406417 0.753247
203 SER ALA ASN SER PHE THR LEU ILE GLY GLU 0.40625 0.656716
204 PRO PRO THR LEU HIS GLU LEU TYR ASP LEU 0.405714 0.842857
205 GLU ASP GLU ASP PHE GLU ILE LEU SER LEU 0.405063 0.641791
206 VAL SER GLN ASN TYR PRO ILE VAL GLN ASN 0.404908 0.852941
207 BOC HIS PRO PHE ALA LOV ILE HIS 0.404494 0.802817
208 PHE LEU GLU LYS 0.404412 0.677419
209 ACE PRO ALA PRO TYR 0.404412 0.815385
210 ASN ASP LYS TYR GLU PRO PHE TRP GLU 0.404255 0.811594
211 ARG TYR PRO LEU THR PHE GLY TRP 0.404255 0.810811
212 ALA LEU PRO HIS ALA ILE LEU ARG LEU 0.403509 0.746479
213 ILE SER TYR GLY ASN ASP ALA LEU MET PRO 0.403409 0.819444
214 ACE VAL PHE PHE ALA GLU ASP NH2 0.402878 0.629032
215 ALA LEU TYR ASN THR ALA ALA ALA LEU 0.402778 0.621212
216 PHE ASN ARG PRO VAL 0.402597 0.732394
217 SER LEU ARG PHE LEU TYR GLU GLY 0.401274 0.680556
218 THR THR ALA PRO PHE LEU SER GLY LYS 0.4 0.797101
219 GLU VAL PTR GLU SER PRO 0.4 0.780822
Similar Ligands (3D)
Ligand no: 1; Ligand: PHE GLU ALA ILE PRO ALA GLU TYR LEU; Similar ligands found: 0
No: Ligand Similarity coefficient
Similar Binding Sites (Proteins are less than 50% similar to leader)
Pocket No.: 1; Query (leader) PDB : 1D9I; Ligand: 00P; Similar sites found with APoc: 3
This union binding pocket(no: 1) in the query (biounit: 1d9i.bio1) has 26 residues
No: Leader PDB Ligand Sequence Similarity
1 1FIW PBZ 44.0972
2 1OSS BEN 47.0852
3 1PQ7 ARG 49.5536
APoc FAQ
Feedback