Receptor
PDB id Resolution Class Description Source Keywords
6EWO 2.3 Å NON-ENZYME: IMMUNE CRYSTAL STRUCTURE OF NON-PHOSPHORYLATED FORM OF RTF PHOSPHOP BOUND TO HLA-A2 IN COMPLEX WITH LILRB1 HOMO SAPIENS LILRB1 NONPHOSPHOPEPTIDE PEPTIDE-MHC COMPLEX HLA-A2 TUMOANTIGEN CRYSTALLISATION CHAPERONE IMMUNE SYSTEM
Ref.: APPLICATION OF THE IMMUNOREGULATORY RECEPTOR LILRB1 CRYSTALLISATION CHAPERONE FOR HUMAN CLASS I MHC COM J. IMMUNOL. METHODS V. 464 47 2019
Ligand
Ligand Chain:Residue Validity Ligand Warnings Binding Data NGL Viewer Molecular Weight (Da) Formula SMILES
ARG THR PHE SER PRO THR TYR GLY LEU C:1;
G:1;
Valid;
Valid;
none;
none;
submit data
1042.18 n/a O=C([...
View in 3D viewer
90% Homology Family
Leader
PDB id Resolution Class Description Source Keywords
2X4T 2.3 Å NON-ENZYME: IMMUNE CRYSTAL STRUCTURE OF MHC CLASS I HLA-A2.1 BOUND TO A PEIODATE-CLEAVABLE PEPTIDE HOMO SAPIENS MHC CLASS I IMMUNOGLOBULIN DOMAIN HOST-VIRUS INTERACTION GLYCATION AMYLOIDOSIS AMYLOID PHOTOCLEAVABLE PEPTIDE IMMUNE RESPONSE IMMUNE SYSTEM
Ref.: CLASS I MAJOR HISTOCOMPATIBILITY COMPLEXES LOADED BY A PERIODATE TRIGGER. J.AM.CHEM.SOC. V. 131 12305 2009
Members (6)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 225 families.
1 6EWA - ILE LEU LYS GLU PRO VAL HIS GLY VAL n/a n/a
2 6EWO - ARG THR PHE SER PRO THR TYR GLY LEU n/a n/a
3 2X4Q - MSE ILE LEU GLY PRV VAL PHE PRQ VAL n/a n/a
4 2X4T ic50 = 7.33 uM ASN LEU VAL PRW MET VAL ALA THR VAL n/a n/a
5 1IM3 - LEU LEU PHE GLY TYR PRO VAL TYR VAL n/a n/a
6 4N8V - MET LEU ILE TYR SER MET TRP GLY LYS n/a n/a
70% Homology Family (14)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 67 families.
1 2DYP - ARG ILE ILE PRO ARG HIS LEU GLN LEU n/a n/a
2 6EWA - ILE LEU LYS GLU PRO VAL HIS GLY VAL n/a n/a
3 6EWO - ARG THR PHE SER PRO THR TYR GLY LEU n/a n/a
4 2X4Q - MSE ILE LEU GLY PRV VAL PHE PRQ VAL n/a n/a
5 2X4T ic50 = 7.33 uM ASN LEU VAL PRW MET VAL ALA THR VAL n/a n/a
6 1IM3 - LEU LEU PHE GLY TYR PRO VAL TYR VAL n/a n/a
7 4N8V - MET LEU ILE TYR SER MET TRP GLY LYS n/a n/a
8 6V3J - LEU SER SER PRO VAL THR LYS SER PHE n/a n/a
9 5B39 - LEU SER SER PRO VAL THR LYS SER PHE n/a n/a
10 5T6Z - THR SER THR LEU GLN GLU GLN ILE GLY TRP n/a n/a
11 5T70 Kd = 102 uM THR SER ASN LEU GLN GLU GLN ILE GLY TRP n/a n/a
12 5B38 - LEU SER SER PRO VAL THR LYS SER PHE n/a n/a
13 3VH8 - LEU SER SER PRO VAL THR LYS SER PHE n/a n/a
14 4PGC - PHE ALA PRO GLY ASN TYI PRO ALA LEU n/a n/a
50% Homology Family (14)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 45 families.
1 2DYP - ARG ILE ILE PRO ARG HIS LEU GLN LEU n/a n/a
2 6EWA - ILE LEU LYS GLU PRO VAL HIS GLY VAL n/a n/a
3 6EWO - ARG THR PHE SER PRO THR TYR GLY LEU n/a n/a
4 2X4Q - MSE ILE LEU GLY PRV VAL PHE PRQ VAL n/a n/a
5 2X4T ic50 = 7.33 uM ASN LEU VAL PRW MET VAL ALA THR VAL n/a n/a
6 1IM3 - LEU LEU PHE GLY TYR PRO VAL TYR VAL n/a n/a
7 4N8V - MET LEU ILE TYR SER MET TRP GLY LYS n/a n/a
8 6V3J - LEU SER SER PRO VAL THR LYS SER PHE n/a n/a
9 5B39 - LEU SER SER PRO VAL THR LYS SER PHE n/a n/a
10 5T6Z - THR SER THR LEU GLN GLU GLN ILE GLY TRP n/a n/a
11 5T70 Kd = 102 uM THR SER ASN LEU GLN GLU GLN ILE GLY TRP n/a n/a
12 5B38 - LEU SER SER PRO VAL THR LYS SER PHE n/a n/a
13 3VH8 - LEU SER SER PRO VAL THR LYS SER PHE n/a n/a
14 4PGC - PHE ALA PRO GLY ASN TYI PRO ALA LEU n/a n/a
Polypharmacology
Similar Ligands (2D)
Ligand no: 1; Ligand: ARG THR PHE SER PRO THR TYR GLY LEU; Similar ligands found: 257
No: Ligand ECFP6 Tc MDL keys Tc
1 ARG THR PHE SER PRO THR TYR GLY LEU 1 1
2 ARG TYR PRO LEU THR PHE GLY TRP 0.689441 0.933333
3 ARG PHE PRO LEU THR PHE GLY TRP 0.645963 0.906667
4 ARG ARG LEU PRO ILE PHE SER ARG LEU 0.633333 0.878378
5 ARG TYR PRO LEU THR LEU GLY TRP CYS PHE 0.622857 0.934211
6 ARG PRO MET THR TYR LYS GLY ALA LEU 0.621951 0.871795
7 LEU PHE GLY TYR PRO VAL TYR VAL 0.616438 0.847222
8 ARG PRO MET THR PHE LYS GLY ALA LEU 0.615854 0.833333
9 ARG LEU TYR GLN ASN PRO THR THR TYR ILE 0.6125 0.933333
10 ARG TYR PRO LEU THR PHE GLY TRP CYS PHE 0.610169 0.921053
11 LEU LEU PHE GLY LYS PRO VAL TYR VAL 0.607843 0.824324
12 ARG PHE PRO LEU THR PHE GLY TRP CYS PHE 0.606936 0.907895
13 ALA PHE ARG ILE PRO LEU THR ARG 0.605263 0.878378
14 LEU LEU PHE GLY TYR PRO VAL TYR VAL 0.602649 0.847222
15 LEU LEU PHE GLY PHE PRO VAL TYR VAL 0.602649 0.847222
16 ARG MET PHE PRO ASN ALA PRO TYR LEU 0.595092 0.886076
17 ILE ARG TYR PRO LYS THR PHE GLY TRP 0.58427 0.907895
18 ARG VAL ALA SER PRO THR SER GLY VAL 0.575342 0.888889
19 ARG PRO PRO GLY PHE SER PRO PHE ALA 0.566879 0.876712
20 PHE TYR ALA PRO GLU PRO ILE THR SER LEU 0.565217 0.88
21 ASN TYR THR PRO GLY PRO GLY THR ARG PHE 0.562874 0.932432
22 ARG SEP PRO VAL PHE SER 0.56129 0.794872
23 ARG GLN PHE GLY PRO ASP PHE PRO THR ILE 0.559524 0.918919
24 ARG GLY TYR VAL TYR GLN GLY LEU 0.557823 0.777778
25 ARG ILE PRO SER TYR ARG TYR ARG TYR 0.556291 0.932432
26 GLY ARG PRO ARG THR THR SER PHE ALA GLU 0.552147 0.890411
27 LEU TYR ALA SER PRO GLN LEU GLU GLY PHE 0.551515 0.888889
28 VAL PRO LEU ARG PRO MET THR TYR 0.55 0.883117
29 ARG PRO PRO ILE PHE ILE ARG ARG LEU 0.547771 0.824324
30 THR THR ALA PRO PHE LEU SER GLY LYS 0.54717 0.824324
31 VAL MET ALA PRO ARG THR LEU PHE LEU 0.546012 0.820513
32 ASN GLY TYR GLU ASN PRO THR TYR LYS 0.54321 0.837838
33 ASP VAL GLN THR GLY ARG ARG PRO TYR GLU 0.542683 0.931507
34 ILE PRO ALA TYR GLY VAL LEU THR ILE 0.541401 0.849315
35 ILE GLY PRO GLY ARG ALA PHE TYR THR ILE 0.541176 0.945205
36 GLN VAL PRO LEU ARG PRO MET THR TYR LYS 0.539773 0.896104
37 ILE GLY PRO GLY ARG ALA PHE TYR THR 0.536145 0.917808
38 ARG VAL ALA SEP PRO THR SER GLY VAL 0.535032 0.820513
39 ASN TYR THR PRO GLY PRO GLY ILE ARG PHE 0.534884 0.933333
40 ALA ASN SER ARG PHE PRO THR SER ILE ILE 0.527273 0.891892
41 ALA ASN SER ARG TYR PRO THR SER ILE ILE 0.524691 0.932432
42 ARG GLY TYR LEU TYR GLN GLY LEU 0.52381 0.777778
43 PHE LEU ARG GLY ARG ALA TYR GLY LEU 0.523179 0.791667
44 LEU PRO SER PHE GLU THR ALA LEU 0.522581 0.847222
45 LYS LEU PRO ALA GLN PHE TYR ILE LEU 0.520958 0.824324
46 TYR LEU GLY GLY PRO ASP PHE PRO THR ILE 0.52071 0.878378
47 SER SER TYR ARG ARG PRO VAL GLY ILE 0.515337 0.932432
48 ARG TYR GLY PHE VAL ALA ASN PHE 0.509677 0.780822
49 GLU TYR LEU GLY LEU ASP VAL PRO VAL 0.509434 0.833333
50 PHE LEU ARG GLY ARG ALA TYR VAL LEU 0.509434 0.791667
51 ASN ARG PRO VAL TYR ILE PRO ARG PRO PRO 0.509317 0.864865
52 ILE GLY PRO GLY ARG ALA PHE TYR VAL 0.508876 0.917808
53 LEU PRO PHE ASP ARG THR THR ILE MET 0.508876 0.846154
54 ARG LEU TYR HIS SEP LEU PRO ALA 0.508772 0.839506
55 ALA ILE MET PRO ALA ARG PHE TYR PRO LYS 0.50838 0.846154
56 LYS LEU TYR GLN ASN PRO THR THR TYR ILE 0.505952 0.853333
57 PHE PRO ARG PRO TRP LEU HIS GLY LEU 0.505556 0.842105
58 ILE GLY PRO GLY ARG ALA PHE TYR ALA 0.502994 0.90411
59 GLY TYR GLU ASN PRO THR TYR LYS PHE PHE 0.502959 0.837838
60 LEU PRO PHE GLU ARG ALA THR VAL MET 0.50289 0.844156
61 ARG GLY PRO GLY CYS ALA PHE VAL THR ILE 0.50289 0.891892
62 PHE ALA PRO GLY ASN TYR PRO ALA LEU 0.5 0.853333
63 HIS SER ILE THR TYR LEU LEU PRO VAL 0.5 0.855263
64 LEU PRO PHE GLU LEU ARG GLY HIS LEU VAL 0.5 0.826667
65 TYR SEP PRO THR SEP PRO SER 0.496599 0.772152
66 DPN PRO DAR DTH NH2 0.493056 0.833333
67 ASP TYR ASN PRO TYR LEU LEU PHE LEU LYS 0.490683 0.864865
68 PRO SER TYR SEP PRO THR SEP PRO SER 0.490446 0.772152
69 GLY LEU LEU GLY SER PRO VAL ARG ALA 0.490323 0.861111
70 ARG THR TYR SEP GLY PRO MET ASN LYS VAL 0.489247 0.833333
71 LEU PRO PHE GLU ARG ALA THR ILE MET 0.488636 0.833333
72 ALA LEU TRP GLY PHE PHE PRO VAL LEU 0.488235 0.76
73 PHE GLU ALA ILE PRO ALA GLU TYR LEU 0.487805 0.821918
74 ALA ASN SER ARG TRP PRO THR THR ARG LEU 0.48538 0.907895
75 SER THR SEP PRO THR PHE ASN LYS 0.485207 0.7375
76 PHE ASN ARG PRO VAL 0.483444 0.835616
77 LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE 0.481928 0.780822
78 N7P THR SEP PRO SER TYR SET 0.480769 0.753086
79 ARG PRO GLY ASN PHE LEU GLN SER ARG LEU 0.480226 0.878378
80 ARG GLY PRO GLY ARG ALA PHE VAL THR ILE 0.48 0.878378
81 TYR MET PHE PRO ASN ALA PRO TYR LEU 0.479042 0.797468
82 LYS THR PHE PRO PRO THR GLU PRO LYS 0.478528 0.808219
83 PHE ALA PRO GLY PHE PHE PRO TYR LEU 0.478528 0.824324
84 LYS PRO ILE VAL VAL LEU HIS GLY TYR 0.477012 0.802632
85 ASP PHE GLU GLU ILE PRO GLY GLU TYR LEU 0.476744 0.837838
86 LEU SER SER PRO VAL THR LYS SER PHE 0.475309 0.808219
87 ALA ARG THR GLU LEU TYR ARG SER LEU 0.474359 0.794521
88 GLU ALA ASP PRO THR GLY HIS SER TYR 0.474286 0.853333
89 ACE GLY PHE GLY VAL VAL PRO SER PHE TYR 0.474026 0.805556
90 ARG PRO GLY ASN PHE LEU GLN SER ARG PRO 0.473988 0.866667
91 ARG PHE MET ASP TYR TRP GLU GLY LEU 0.47191 0.782051
92 DPN PRO ARG 0.471014 0.75
93 GLY ASP CYS PHE SER LYS PRO ARG 0.470238 0.837838
94 ARG VAL SER PRO SER THR SER TYR THR PRO 0.469799 0.833333
95 GLN ASN GLY PTR VAL ASN PRO THR TYR 0.469136 0.822785
96 ALA LEU TRP GLY PHE VAL PRO VAL LEU 0.468208 0.76
97 ALA ASN SER ARG LEU PRO THR SER ILE ILE 0.467949 0.876712
98 LEU GLU LYS ALA ARG GLY SER THR TYR 0.467456 0.821918
99 GLU PHE SER PRO 0.467153 0.75
100 ARG GLY TYR VAL TYR ESC GLY LEU GAL GLA 0.464865 0.797468
101 1IP CYS PHE SER LYS PRO ARG 0.464286 0.828947
102 LEU GLN ARG VAL LEU SEP ALA PRO PHE 0.463855 0.797468
103 PRO LYS ARG PRO THR THR LEU ASN LEU PHE 0.463687 0.891892
104 PHE ARG TYR LEU GLY 0.462585 0.777778
105 DHI PRO PHE HIS LEU LEU VAL TYR 0.462428 0.8
106 ARG ILE ILE PRO ARG HIS LEU GLN LEU 0.461988 0.802632
107 GLN LEU SER PRO PHE PRO PHE ASP LEU 0.460123 0.849315
108 ALA MET ALA PRO ARG THR LEU LEU LEU 0.459119 0.794872
109 ALA THR PRO PHE GLN GLU 0.457516 0.763889
110 LEU ASN PHE PRO ILE SER PRO 0.457516 0.813333
111 TYR PRO LYS ARG ILE ALA 0.45679 0.851351
112 ASP TYR GLU PRO ILE PRO GLU GLU ALA PHE 0.45614 0.824324
113 ARG THR PRO SEP LEU PRO THR 0.455696 0.797468
114 ARG THR PRO SEP LEU PRO THR 49F 0.455696 0.797468
115 ASN ARG PRO ILE LEU SER LEU 0.455128 0.864865
116 PHE PRO THR LYS ASP VAL ALA LEU 0.45509 0.821918
117 PHE GLN PRO GLN ASN GLY GLN PHE ILE 0.454545 0.76
118 ARG THR PRO SEP LEU PRO GLY D4K 0.453552 0.875
119 GLY GLU ARG THR ILE PRO ILE THR ARG GLU 0.453416 0.851351
120 LYS PRO VAL LEU ARG THR ALA 0.45283 0.849315
121 THR THR ALA PRO SER LEU SER GLY LYS 0.45283 0.797297
122 ASP PHE ALA ASN THR PHE LEU PRO 0.45283 0.849315
123 DPN PRO DAR ILE NH2 0.452703 0.767123
124 ALA ARG SER HIS SEP TYR PRO ALA 0.451977 0.82716
125 ALA LEU MET PRO GLY GLN PHE PHE VAL 0.451807 0.736842
126 ARG ARG GLU VAL HIS THR TYR TYR 0.451807 0.826667
127 DTY ILE ARG LEU LPD 0.451613 0.863014
128 ASP PHE GLU GLU ILE PRO GLY GLU TYS LEU 0.451429 0.715909
129 GLY PHE ARG PRO 0.450704 0.777778
130 GLU GLU PRO THR VAL ILE LYS LYS TYR 0.450292 0.837838
131 PHE LEU PRO SER ASP PHE PHE PRO SER VAL 0.45 0.863014
132 TYR PRO PHE PHE NH2 0.45 0.75
133 TYR GLN PHE GLY PRO ASP PHE PRO ILE ALA 0.448864 0.837838
134 GLY ILE LEU GLY LEU VAL PHE THR LEU 0.447368 0.630137
135 PRO PRO ARG PRO ILE TYR ASN ARG ASN 0.447059 0.88
136 ILE SER PRO ARG THR LEU ASP ALA TRP 0.446809 0.907895
137 SER ALA PRO ASP THR ARG PRO ALA 0.446541 0.864865
138 ALA TRP ARG HIS PRO GLN PHE GLY GLY 0.446237 0.789474
139 GLY LEU LEU GLY SEP PRO VAL ARG ALA 0.445783 0.794872
140 SER LEU PHE HIS 22G THR PRO 0.44382 0.88
141 LEU PRO PHE GLU LYS SER THR VAL MET 0.442529 0.792208
142 DPN PRO DAR CYS NH2 0.442177 0.739726
143 ARG ARG ILE TYR ASP LEU ILE GLU LEU 0.441718 0.743243
144 TYR LEU GLU PRO ALA PRO VAL THR ALA 0.441718 0.837838
145 TYR LEU LYS GLU PRO VAL HIS GLY VAL 0.441341 0.813333
146 LYS PRO ILE VAL GLN TYR ASP ASN PHE 0.440678 0.853333
147 GLN MET PRO THR GLU ASP GLU TYR 0.440476 0.792208
148 TYR LEU GLU PRO GLY PRO VAL THR VAL 0.440476 0.863014
149 TYR LEU GLU PRO GLY PRO VAL THR ALA 0.440476 0.863014
150 ILE ARG ALA ALA PRO PRO PRO LEU PHE 0.43787 0.813333
151 THR PRO PRO SER PRO PHE 0.4375 0.780822
152 SER ILE TYR PHE TPO PRO GLU LEU TYR ASP 0.437158 0.848101
153 LEU TYR LEU VAL CYS GLY GLU ARG VAL 0.437126 0.753425
154 SER ARG ILE ARG ILE ARG GLY TYR VAL ARG 0.436709 0.797297
155 TYR GLY GLY PHE LEU 0.43662 0.680556
156 ARG GLN PRO ALA LYS ALA PRO LEU LEU 0.436364 0.810811
157 LEU PRO PHE ASP LYS SER THR ILE MET 0.435754 0.782051
158 TYR LEU ALA PRO GLY PRO VAL THR ALA 0.435583 0.851351
159 ARG ARG ARG GLU ARG SER PRO THR ARG 0.434783 0.849315
160 TYR TYR SER ILE ILE PRO HIS SER ILE 0.434524 0.855263
161 THR PRO ARG VAL THR GLY GLY GLY ALA MET 0.434524 0.820513
162 ALA ASN SER ARG HIS PRO THR SER ILE ILE 0.434524 0.855263
163 GLY GLY ARG LYS LYS TYR LYS LEU 0.434211 0.753425
164 GLY GLY LYS LYS ARG TYR LYS LEU 0.434211 0.753425
165 GLY GLY LYS LYS LYS TYR ARG LEU 0.434211 0.753425
166 SER LEU ARG PHE LEU TYR GLU GLY 0.433962 0.833333
167 LEU TYR LEU VAL CYS GLY GLU ARG GLY 0.433735 0.753425
168 LEU LEU TYR GLY PHE VAL ASN TYR VAL 0.433121 0.684932
169 ASP TYR ILE ASN THR ASN VAL LEU PRO 0.432927 0.837838
170 ILE THR ASP GLN VAL PRO PHE SER VAL 0.432749 0.835616
171 ARG LEU PRO ALA LYS ALA PRO LEU LEU 0.432099 0.797297
172 ACE GLY LYS SER PHE SER LYS PRO ARG 0.432099 0.773333
173 PHE ALA PRO GLY ASN TYI PRO ALA LEU 0.431034 0.8
174 MET CYS PRO ARG MET THR ALA VAL MET 0.429412 0.818182
175 LEU PRO PHE ASP LYS THR THR ILE MET 0.428571 0.769231
176 THR PRO TYR ASP ILE ASN GLN MET LEU 0.428571 0.794872
177 ALA VAL TYR ASP GLY ARG GLU HIS THR VAL 0.428571 0.826667
178 GLU PRO VAL GLU THR THR ASP TYR 0.428571 0.847222
179 GLU THR PHE TYR VAL ASP GLY 0.427632 0.722222
180 SER SER GLY LYS VAL PRO LEU 0.427632 0.780822
181 SER PRO ILE VAL PRO SER PHE ASP MET 0.426901 0.782051
182 ARG ARG LEU LEU ARG GLY HIS ASN GLN TYR 0.426901 0.826667
183 TYR PRO ASN VAL ASN ILE HIS ASN PHE 0.426136 0.842105
184 ACE ARG THR PRO SEP LEU PRO THR 60H 0.426136 0.8375
185 GLU GLU PHE GLY ARG ALA PHE SER PHE 0.425926 0.736111
186 PHE TYR ARG ALA LEU MET 0.425 0.710526
187 ARG SER HIS SEP SER PRO ALA SER LEU GLN 0.424731 0.802469
188 ILE LEU GLY PRO PRO GLY SER VAL TYR 0.424419 0.864865
189 GLU THR VAL ARG PHE GLN SER ASP 0.423313 0.736111
190 ARG GLY PHE ALA LEU M3L SER THR HIS GLY 0.423077 0.802469
191 ASP ILE ASN TYR TYR THR SER GLU PRO 0.422619 0.878378
192 ALA ASN SER ARG ALA PRO THR SER ILE ILE 0.422619 0.853333
193 LEU LEU TYR GLY PHE VAL ASN TYR ILE 0.42236 0.675676
194 GLN VAL PRO SER ASP PRO TYR ASN TYR 0.421687 0.851351
195 GLU PRO GLY GLY SER ARG 0.421053 0.808219
196 ARG ILE PHE SER 0.42069 0.657534
197 ALA ASN SER ARG ALY PRO THR SER ILE ILE 0.420455 0.831169
198 MET THR SER ALA ILE GLY ILE LEU PRO VAL 0.420118 0.766234
199 ALA ASN SER ARG VAL PRO THR SER ILE ILE 0.419753 0.876712
200 GLU ARG THR ILE PRO ILE THR ARG GLU 0.417722 0.824324
201 PHE SER HIS PRO GLN ASN THR 0.417647 0.813333
202 GLN ASN TYR PRO ILE VAL GLN 0.417178 0.810811
203 ASP ILE ALA TYR TYR THR SER GLU PRO 0.417178 0.890411
204 PHE ASN PHE PRO GLN ILE THR 0.417178 0.810811
205 ALA LEU PRO HIS ALA ILE LEU ARG LEU 0.417143 0.776316
206 PHE LEU PRO HIS ALY TYR ASP VAL LYS LEU 0.417112 0.779221
207 ALA ASN SER ARG TRP PRO THR SER ALY ILE 0.416667 0.860759
208 GLN ASN GLY PTR GLU ASN PRO THR TYR 0.416667 0.772152
209 ILE SER TYR GLY ASN ASP ALA LEU MET PRO 0.416667 0.820513
210 MET SER LEU PRO GLY ARG TRP LYS PRO LYS 0.416244 0.860759
211 ARG VAL ALA GLN LEU GLU GLN VAL TYR ILE 0.415663 0.726027
212 GLY SER ASP PRO PHE LYS 0.415584 0.767123
213 ALA ASN SER ARG TRP PRO THR SER FAK ILE 0.415385 0.839506
214 GLY ALA GLU THR PHE TYR VAL ASP GLY ALA 0.41358 0.712329
215 GLY GLY CYS PHE SER LYS PRO LYS MYR 0.413408 0.753247
216 THR GLU ASN LEU TYR PHE GLN SER GLY THR 0.413174 0.753425
217 TYR GLU LEU ASP GLU LYS PHE ASP ARG LEU 0.413174 0.794521
218 GLY TYR GLN ASP TYR GLU PRO GLU ALA 0.412903 0.777778
219 LEU GLY TYR GLY PHE VAL ASN TYR ILE 0.4125 0.675676
220 ARG GLN PHE GLY PRO ASP TRP ILE VAL ALA 0.41206 0.842105
221 ALA ASN SER ARG TRP PRO THR SER 2KK ILE 0.41206 0.851852
222 ALA VAL ALA PHE TYR ILE PRO ASP GLN ALA 0.411392 0.794521
223 ARG GLN ALA SEP ILE GLU LEU PRO SER MET 0.410526 0.761905
224 GLY VAL TYR ASP GLY ARG GLU HIS THR VAL 0.410112 0.826667
225 SER ASP TYR GLN ARG LEU 0.409396 0.75
226 TYR ASP LEU SEP LEU PRO PHE PRO 0.409091 0.822785
227 GLU SER ASP PRO ILE VAL ALA GLN TYR 0.409091 0.876712
228 ASP PHE GLU GLU ILE PRO GLY GLU PTR 0.40884 0.775
229 ARG SER LEU SEP ALA PRO GLY ASN 0.408537 0.797468
230 GLU GLU TYR LEU GLN ALA PHE THR TYR 0.408537 0.680556
231 MET TYR TRP TYR PRO TYR 0.408284 0.721519
232 PIV HIS PRO PHE HIS LPL TYR TYR SER 0.407609 0.782051
233 MET VAL TRP GLY PRO ASP PRO LEU TYR VAL 0.407216 0.797468
234 GLU GLY GLN PTR GLN PRO GLN PRO ALA 0.406977 0.721519
235 PHE ALA PRO GLY ASN TYR PRO ALA TRP 0.406417 0.805195
236 GLY ILE TRP GLY PHE VAL PHE THR LEU 0.405882 0.706667
237 ARG PRO GLN VAL PRO LEU ARG PRO MET 0.405882 0.779221
238 ALA ILE ALA TYR PHE ILE PRO ASP GLN ALA 0.405063 0.780822
239 ALA PRO ASP THR ARG PRO ALA PRO 0.405063 0.851351
240 ACE ARG THR PRO SEP LEU PRO THR PIP 0.404762 0.780488
241 LYS PRO PHE PTR VAL ASN VAL NH2 0.404624 0.775
242 ARG SER ALA SEP GLU PRO SER LEU 0.404624 0.810127
243 LYS TYR TYR SER ILE ILE PRO HIS SER ILE 0.404624 0.855263
244 SER ARG ASP HIS SER ARG THR PRO MET 0.404372 0.835443
245 ASN ASP TRP LEU LEU PRO SER TYR 0.404372 0.868421
246 PHE TYR ARG TYR GLY PHE VAL ALA ASN PHE 0.40411 0.680556
247 SER GLY ILE PHE LEU GLU THR SER 0.403974 0.643836
248 SER SER ILE GLU PHE ALA ARG LEU 0.403614 0.739726
249 ILE LEU GLY LYS PHE LEU HIS ARG LEU 0.403509 0.736842
250 SER GLU ILE GLU PHE ALA ARG LEU 0.402439 0.726027
251 LEU ARG ASN GLN SER VAL PHE ASN PHE 0.402439 0.780822
252 ALA THR ARG ASN PHE SER GLY 0.401274 0.726027
253 SER SER GLY LYS VAL PRO LEU SER 0.401274 0.794521
254 ALA CYS SEP PRO GLN PHE GLY 0.401198 0.708861
255 VAL VAL ARG PRO GLY SER LEU ASP LEU PRO 0.40113 0.890411
256 SER THR GLY GLY VAL M3L LYS PRO HIS ARG 0.401015 0.814815
257 PHE PRO ARG 0.4 0.722222
Similar Ligands (3D)
Ligand no: 1; Ligand: ARG THR PHE SER PRO THR TYR GLY 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 : 2X4T; Ligand: ASN LEU VAL PRW MET VAL ALA THR VAL; 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: 2x4t.bio2) has 27 residues
No: Leader PDB Ligand Sequence Similarity
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