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 26 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 18 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 15 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
Ligand no: 1; Ligand: PHE GLU ALA ILE PRO ALA GLU TYR LEU; Similar ligands found: 217
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 0.697183 0.936508
3 LYS LEU PRO ALA GLN PHE TYR ILE LEU 0.692308 0.967742
4 PHE TYR ALA PRO GLU PRO ILE THR SER LEU 0.648649 0.882353
5 ALA ILE ALA TYR PHE ILE PRO ASP GLN ALA 0.608392 0.967213
6 ASP PHE GLU GLU ILE PRO GLY GLU TYS LEU 0.601307 0.766234
7 ASP PHE GLU GLU ILE PRO GLY GLU TYR LEU 0.590909 0.952381
8 SER ILE TYR PHE TPO PRO GLU LEU TYR ASP 0.583851 0.821918
9 TYR MET PHE PRO ASN ALA PRO TYR LEU 0.578947 0.830986
10 TRP GLU TYR ILE PRO ASN VAL 0.574194 0.895522
11 PHE ALA PRO GLY ASN TYR PRO ALA LEU 0.569536 0.867647
12 LEU PRO PHE GLU ARG ALA THR ILE MET 0.567901 0.723684
13 ASP PHE GLU GLU ILE PRO GLU GLU TYS 0.562914 0.763158
14 LEU TYR ALA SER PRO GLN LEU GLU GLY PHE 0.559748 0.907692
15 PHE ALA PRO GLY PHE PHE PRO TYR LEU 0.554054 0.921875
16 GLY TYR GLN ASP TYR GLU PRO GLU ALA 0.547445 0.885246
17 TRP ASP ILE PRO PHE 0.546875 0.836066
18 TRP MET ASP PHE ASP ASP ASP ILE PRO PHE 0.546875 0.836066
19 TYR GLN PHE GLY PRO ASP PHE PRO ILE ALA 0.537037 0.907692
20 GLU GLU TYR LEU GLN ALA PHE THR TYR 0.534722 0.703125
21 LEU PRO PHE GLU ARG ALA THR VAL MET 0.530488 0.710526
22 TYR TYR SER ILE ILE PRO HIS SER ILE 0.529412 0.828571
23 LYS TYR TYR SER ILE ILE PRO HIS SER ILE 0.529412 0.828571
24 LYS PRO ILE VAL GLN TYR ASP ASN PHE 0.52795 0.909091
25 ASP PHE GLU GLU ILE PRO GLU GLU TYS LEU 0.52439 0.766234
26 ALA ILE MET PRO ALA ARG PHE TYR PRO LYS 0.523529 0.783784
27 GLU SER ASP PRO ILE VAL ALA GLN TYR 0.522293 0.865672
28 GLY TYR GLU ASN PRO THR TYR LYS PHE PHE 0.522013 0.863636
29 SER SER PHE TYR PRO SEP ALA GLU GLY 0.516556 0.788732
30 ALA PRO GLN PRO ALA PRO GLU ASN ALA TYR 0.513158 0.820895
31 ASP ALA ASP GLU TYR LEU 0.51145 0.677419
32 PRO GLN PTR GLU PTR ILE PRO ALA 0.509554 0.828571
33 ALA PRO ALA TRP LEU PHE GLU ALA 0.509434 0.859375
34 ARG MET PHE PRO ASN ALA PRO TYR LEU 0.509091 0.75641
35 ARG ILE PRO SER TYR ARG TYR ARG TYR 0.506494 0.77027
36 ILE PRO ALA TYR GLY VAL LEU THR ILE 0.50641 0.90625
37 PHE GLN PRO GLN ASN GLY GLN PHE ILE 0.503268 0.818182
38 ARG ARG LEU PRO ILE PHE SER ARG LEU 0.503185 0.716216
39 LEU LEU PHE GLY LYS PRO VAL TYR VAL 0.496894 0.983607
40 SER SER LEU GLU ASN PHE ALA ALA TYR VAL 0.496689 0.661765
41 TYR LEU GLU PRO ALA PRO VAL THR ALA 0.496689 0.863636
42 TYR GLU LEU ASP GLU LYS PHE ASP ARG LEU 0.496689 0.676056
43 ILE GLY PRO GLY ARG ALA PHE TYR THR ILE 0.494118 0.830986
44 ASP PHE GLU GLU ILE PRO GLY GLU PTR 0.493976 0.816901
45 THR PRO TYR ASP ILE ASN GLN MET LEU 0.493902 0.828571
46 PHE SER ALA PTR PRO SER GLU GLU ASP 0.49375 0.767123
47 PRO GLN PTR GLU GLU ILE PRO ILE 0.493671 0.8
48 LEU LEU PHE GLY TYR PRO VAL TYR VAL 0.493671 0.967213
49 LYS GLN GLU PRO GLN GLU ILE ASP PHE 0.493671 0.825397
50 LEU LEU PHE GLY PHE PRO VAL TYR VAL 0.493671 0.967213
51 SER ALA GLU PRO VAL PRO LEU GLN LEU 0.493151 0.764706
52 ALA VAL ALA PHE TYR ILE PRO ASP GLN ALA 0.493056 0.966667
53 ASP ARG VAL TYR ILE HIS PRO PHE 0.491329 0.833333
54 PHE ALA PRO GLY ASN TYI PRO ALA LEU 0.490683 0.808219
55 PHE LEU ALA TYR LYS 0.488889 0.783333
56 GLU TYR LEU GLY LEU ASP VAL PRO VAL 0.487179 0.919355
57 LEU PHE GLY TYR PRO VAL TYR VAL 0.487013 0.967213
58 ACE GLN PM3 GLU GLU ILE PRO 0.486111 0.753623
59 GLN LEU SER PRO PHE PRO PHE ASP LEU 0.483871 0.794118
60 PHE GLU ALA ASN GLY ASN LEU ILE 0.482993 0.636364
61 PHE ASN PHE PRO GLN ILE THR 0.48 0.848485
62 LEU ALA ILE TYR SER 0.477273 0.666667
63 LEU PRO PHE GLU LYS SER THR VAL MET 0.47561 0.760563
64 PHE PRO THR LYS ASP VAL ALA LEU 0.474359 0.830769
65 PHE LEU PRO SER ASP PHE PHE PRO SER VAL 0.473333 0.835821
66 LYS PRO PHE PTR VAL ASN VAL GLU PHE 0.473054 0.780822
67 LYS LEU TYR GLN ASN PRO THR THR TYR ILE 0.472727 0.880597
68 ILE GLY PRO GLY ARG ALA PHE TYR ALA 0.472727 0.867647
69 ACE LEU TYR ALA SER SER ASN PRO ALA PTR 0.47205 0.776316
70 ASN ARG PRO VAL TYR ILE PRO ARG PRO PRO 0.471338 0.8
71 TYR LEU GLY GLY PRO ASP PHE PRO THR ILE 0.470588 0.909091
72 TYR PRO PHE PHE NH2 0.470149 0.883333
73 ARG ILE ILE PRO ARG HIS LEU GLN LEU 0.46988 0.736111
74 THR ASN GLU PHE TYR PHE 0.469231 0.634921
75 TYR TYR SER ILE ALA PRO HIS SER ILE 0.469136 0.802817
76 VAL TYR ILE HIS PRO PHE 0.46875 0.90625
77 GLY ARG PRO ARG THR THR SER PHE ALA GLU 0.466667 0.702703
78 VAL MET ALA PRO ARG THR LEU PHE LEU 0.466667 0.688312
79 ASP GLU LEU GLU ILE LYS ALA TYR 0.466216 0.758065
80 DHI PRO PHE HIS LEU LEU VAL TYR 0.464706 0.90625
81 ARG LEU TYR GLN ASN PRO THR THR TYR ILE 0.464706 0.797297
82 PHE TYR ARG ALA LEU MET 0.463087 0.638889
83 GLU GLU PRO THR VAL ILE LYS LYS TYR 0.462963 0.90625
84 PHE LEU ARG GLY ARG ALA TYR VAL LEU 0.462025 0.695652
85 ILE LEU ALA LYS PHE LEU HIS GLU LEU 0.461039 0.75
86 LEU PRO PHE ASP LYS THR THR ILE MET 0.460606 0.797101
87 ACE ILE TYR GLU SER LEU 0.459259 0.676923
88 TYR LEU GLU PRO GLY PRO VAL THR VAL 0.459119 0.863636
89 ASN TRP SER HIS PRO GLN PHE GLU LYS 0.458599 0.769231
90 TYR PRO LYS ARG ILE ALA 0.458065 0.811594
91 GLU GLU TYR LEU LYS ALA TRP THR PHE 0.457831 0.787879
92 ASN GLY TYR GLU ASN PRO THR TYR LYS 0.457317 0.823529
93 ASN TYR THR PRO GLY PRO GLY ILE ARG PHE 0.457143 0.808219
94 SER GLU ASP GLU PHE TYR ASP ALA LEU SER 0.456954 0.707692
95 TYR LEU GLU PRO GLY PRO VAL THR ALA 0.45625 0.863636
96 TYR PRO ASN VAL ASN ILE HIS ASN PHE 0.455621 0.882353
97 ACE TYR PRO ILE GLN GLU THR 0.454545 0.904762
98 SER ASP ILE LEU PHE PRO ALA ASP SER 0.454545 0.818182
99 PHE ALA PRO GLY ASN TYR PRO ALA TRP 0.454023 0.814286
100 PHE LEU ARG GLY ARG ALA TYR GLY LEU 0.453947 0.695652
101 THR ASN GLU TYR TYR VAL 0.453846 0.68254
102 ASP PHE GLU GLU ILE 0.453846 0.622951
103 GLU ASP GLU ASP PHE GLU ILE LEU SER LEU 0.453333 0.636364
104 PRO ALA ILE LEU TYR ALA LEU LEU SER SER 0.453333 0.772727
105 SER ILE ILE ASN PHE GLU LYS LEU 0.452703 0.632353
106 HIS SER ILE THR TYR LEU LEU PRO VAL 0.452381 0.828571
107 LEU PRO PRO VAL VAL ALA LYS GLU ILE 0.452229 0.83871
108 ARG PRO MET THR TYR LYS GLY ALA LEU 0.451429 0.74026
109 LEU PRO PHE ASP LYS SER THR ILE MET 0.450292 0.774648
110 LEU PRO PRO LEU ASP ILE THR PRO TYR 0.447853 0.90625
111 ILE ARG ALA ALA PRO PRO PRO LEU PHE 0.447205 0.746479
112 LEU PRO PHE ASP ARG THR THR ILE MET 0.447059 0.714286
113 GLY ALA ASP ILE PHE TYR LEU ASP GLY ALA 0.445205 0.725806
114 ILE THR ASP GLN VAL PRO PHE SER VAL 0.445122 0.820895
115 LYS PRO ILE VAL VAL LEU HIS GLY TYR 0.444444 0.907692
116 PTR VAL PRO MET LEU 0.443709 0.763889
117 GLU ILE ILE ASN PHE GLU LYS LEU 0.442953 0.646154
118 GLN ASN TYR PRO ILE VAL GLN 0.441558 0.90625
119 TYR PRO TYR 0.440945 0.883333
120 DTY ILE ARG LEU LPD 0.440789 0.823529
121 ARG PRO MET THR PHE LYS GLY ALA LEU 0.44 0.701299
122 GLY ILE LEU GLU PHE VAL PHE THR LEU 0.439189 0.698413
123 ASN ASP LYS TYR GLU PRO PHE TRP GLU 0.438889 0.820895
124 TYR ASP GLN ILE LEU 0.438849 0.693548
125 PHE ARG TYR LEU GLY 0.4375 0.705882
126 SER SER LEU GLU ASN PHE ARG ALA TYR VAL 0.437126 0.635135
127 GLU ASN GLN LYS GLU TYR PHE PHE 0.43662 0.6875
128 TYR LEU LYS GLU PRO VAL HIS GLY VAL 0.436047 0.892308
129 THR PRO ASP TYR PHE LEU 0.435714 0.868852
130 PHE LEU SER TYR LYS 0.435714 0.723077
131 SER PHE PHE GLU ASP ASN PHE VAL PRO GLU 0.435065 0.808824
132 ARG GLN PHE GLY PRO ASP PHE PRO THR ILE 0.435028 0.780822
133 ILE MET ASP GLN VAL PRO PHE SER VAL 0.434524 0.760563
134 LYS PRO SEP GLN GLU LEU 0.433566 0.684932
135 DPN PRO DAR ILE NH2 0.433566 0.720588
136 ARG VAL ALA GLN LEU GLU GLN VAL TYR ILE 0.433121 0.676471
137 ARG ARG ILE TYR ASP LEU ILE GLU LEU 0.433121 0.647887
138 ASN PRO ARG ALA MET GLN ALA LEU LEU 0.433121 0.666667
139 TYR MET ASP PHE ASP ASP ASP ILE PRO PHE 0.430769 0.816667
140 GLY ASN TYR SER PHE TYR ALA LEU 0.430556 0.661765
141 TYR LEU ALA PRO GLY PRO VAL THR ALA 0.43038 0.850746
142 GLU ASN LEU TYR PHE GLN 0.429577 0.703125
143 GLN MET PRO THR GLU ASP GLU TYR 0.429448 0.8
144 ARG GLN ALA SEP ILE GLU LEU PRO SER MET 0.428571 0.619048
145 SER ILE ILE GLY PHE GLU LYS LEU 0.427632 0.676923
146 LEU ASN PHE PRO ILE SER PRO 0.427632 0.797101
147 SER ASN TRP SER HIS PRO GLN PHE GLU LYS 0.426966 0.732394
148 LYS THR PHE PRO PRO THR GLU PRO LYS 0.426829 0.815385
149 VAL ASN ASP ILE PHE GLU ALA ILE 0.426667 0.6
150 ASN TYR THR PRO GLY PRO GLY THR ARG PHE 0.426136 0.77027
151 GLU VAL ALA PRO PRO GLU TYR HIS ARG LYS 0.424731 0.780822
152 ASP VAL GLN THR GLY ARG ARG PRO TYR GLU 0.424419 0.767123
153 LEU GLN ARG VAL LEU SEP ALA PRO PHE 0.424242 0.64557
154 SER GLU CYS THR THR PRO CYS 0.423611 0.746269
155 SER LEU TYR ASN THR ILE ALA THR LEU 0.422819 0.632353
156 THR ASN GLU PHE TYR ALA 0.422535 0.636364
157 GLU ARG THR ILE PRO ILE THR ARG GLU 0.422078 0.712329
158 TYR GLN PHE 0.421875 0.655738
159 GLY SER ASP PRO PHE LYS 0.421769 0.731343
160 PRO GLN PTR ILE PTR VAL PRO ALA 0.421687 0.842857
161 SER GLN TYR TYR TYR ASN SER LEU 0.421429 0.661765
162 MET TYR TRP TYR PRO TYR 0.421384 0.835821
163 PRO PRO ALA TYR PRO PRO PRO PRO VAL PRO 0.421053 0.873016
164 GLU GLY GLN PTR GLN PRO GLN PRO ALA 0.420732 0.746479
165 LEU PRO GLU THR GLY 0.42029 0.8125
166 LEU ASP GLU GLU THR GLY GLU PHE LEU 0.42 0.661538
167 ASN ARG PRO VAL TYR ILE PRO PRO PRO PRO 0.419355 0.903226
168 GLU GLN TYR LYS PHE TYR SER VAL 0.418919 0.701493
169 ALA ASN SER ARG TYR PRO THR SER ILE ILE 0.417647 0.77027
170 LYS GLN TRP ASP ASN TYR GLU PHE ILE TRP 0.417647 0.705882
171 PHE SER HIS PRO GLN ASN THR 0.417178 0.746479
172 SER LEU PHE HIS 22G THR PRO 0.417143 0.828571
173 GLU PRO GLN ALA PRO TRP MET GLU GLN 0.416667 0.757143
174 ASN PHE ASP ASN PRO VAL TYR ARG LYS THR 0.416667 0.783784
175 ILE LEU ALA LYS PHE LEU HIS THR LEU 0.416149 0.731343
176 SER PRO LEU ASP SER LEU TRP TRP ILE 0.415663 0.826087
177 GLN VAL PRO LEU ARG PRO MET THR TYR LYS 0.415301 0.74026
178 GLU PHE SER PRO 0.414815 0.765625
179 ALA VAL PRO ILE ALA GLN 0.414286 0.836066
180 GLU LEU ASP LYS TYR ALA SER 0.412162 0.707692
181 SER SER TYR ARG ARG PRO VAL GLY ILE 0.411765 0.77027
182 THR ASN GLU TYR LYS VAL 0.411348 0.714286
183 VAL SER GLN ASN TYR PRO ILE VAL GLN ASN 0.411043 0.838235
184 PHE VAL PHE LEU GLU ILE NH2 0.410959 0.666667
185 ARG TYR PRO LEU THR PHE GLY TRP 0.410811 0.797297
186 PHE LEU GLU LYS 0.410448 0.683333
187 TYR GLY GLY PHE LEU 0.410072 0.770492
188 ALA THR ALA ALA ALA THR GLU ALA TYR 0.410072 0.625
189 ARG PRO ARG PRO ASP ASP LEU GLU ILE 0.409938 0.732394
190 THR TYR LYS PHE PHE GLU GLN 0.409722 0.692308
191 ALA LEU TYR ASN THR ALA ALA ALA LEU 0.409722 0.606061
192 GLU ASN PRO THR TYR LYS PHE PHE GLU GLN 0.409722 0.692308
193 GLN ASN GLY PTR GLU ASN PRO THR TYR 0.408537 0.739726
194 ALA LEU PRO HIS ALA ILE LEU ARG LEU 0.408284 0.732394
195 PHE GLN TRP MET GLY TYR GLU LEU TRP 0.408046 0.753623
196 PHE LEU TRP GLY PRO ARG ALA LEU VAL 0.407821 0.774648
197 ASN LEU VAL PRO GLN VAL ALA THR VAL 0.407643 0.787879
198 GLN VAL PRO SER ASP PRO TYR ASN TYR 0.407407 0.811594
199 LYS ALA LEU TYR ASN PHE ALA THR MET 0.407407 0.685714
200 LYS PRO PHE PTR VAL ASN VAL NH2 0.407186 0.767123
201 TYR GLN SER LYS LEU 0.407143 0.69697
202 ARG GLY PRO GLY ARG ALA PHE VAL THR ILE 0.40678 0.753425
203 ALA ALA SER LEU TYR GLU LYS LYS ALA ALA 0.406667 0.69697
204 GLU ALA ASP PRO THR GLY HIS SER TYR 0.404494 0.8
205 DPN PRO DAR DTH NH2 0.40411 0.7
206 TYR SEP PRO THR SEP PRO SER 0.403974 0.716216
207 PHE ASN ARG PRO VAL 0.403974 0.71831
208 ASN ASP TRP LEU LEU PRO SER TYR 0.403409 0.830986
209 SER ASP TYR GLN ARG LEU 0.402778 0.652174
210 GLY GLU ARG THR ILE PRO ILE THR ARG GLU 0.402516 0.712329
211 ALA LEU TRP GLY PHE VAL PRO VAL LEU 0.402299 0.859375
212 ALA ARG THR GLU LEU TYR ARG SER LEU 0.401274 0.608108
213 LEU SER SER PRO VAL THR LYS SER PHE 0.401235 0.791045
214 LEU LEU TYR GLY PHE VAL ASN TYR ILE 0.4 0.723077
215 PRO ALA PRO PHE ALA SER ALA 0.4 0.746269
216 SER LEU TYR LEU THR VAL ALA THR LEU 0.4 0.606061
217 ACE VAL PHE PHE ALA GLU ASP NH2 0.4 0.622951
Similar Binding Sites (Proteins are less than 50% similar to leader)
Pocket No.: 1; Query (leader) PDB : 1D9I; Ligand: 00P; Similar sites found: 34
This union binding pocket(no: 1) in the query (biounit: 1d9i.bio1) has 26 residues
No: Leader PDB Ligand P-value (APoc) PS_Score (APoc) Sequence Similarity
1 1PVS 7HP 0.0462 0.40793 1.41844
2 2GMM MAN MAN 0.02928 0.40697 1.98413
3 1FQJ ALF 0.01696 0.4184 2.43056
4 1FQK ALF 0.02852 0.40599 2.43056
5 2POC UD1 0.02711 0.40247 2.43056
6 2XCF BBQ 0.006371 0.41401 3.0303
7 2G30 ALA ALA PHE 0.01625 0.40562 3.10078
8 3ESS 18N 0.01788 0.41899 3.91304
9 1G4U AF3 0.02946 0.40114 4.34783
10 1HE1 AF3 0.03349 0.40145 4.54545
11 4B4Q A2G GAL NAG FUC GAL GLC 0.02087 0.41255 4.63576
12 3NOJ PYR 0.006264 0.45256 5.46218
13 2YY8 MTA 0.0166 0.40545 5.47264
14 3P7G MAN 0.04903 0.4025 5.47945
15 3MMG GLU THR VAL ARG PHE GLN SER ASP 0.0004634 0.44434 6.25
16 2CJU PHX 0.01968 0.4101 7.07965
17 1HPG BOC ALA ALA PRO GLU 0.0002116 0.49701 8.02139
18 4SGA ACE PRO ALA PRO PHE 0.00004752 0.43822 8.83978
19 4F8L AES 0.0267 0.41564 8.96552
20 3HNB 768 0.008445 0.42004 9.43396
21 2OUA AES 0.00002644 0.56095 9.57447
22 3SUD SUE 0.001657 0.42913 9.85222
23 4OVZ P85 0.03213 0.40552 15.9722
24 1FIW PBZ 0.000000000394 0.57198 44.0972
25 5A8Y VBM 0.000004474 0.48771 45.8716
26 1GJC 130 0.0000000001522 0.6471 46.2451
27 1OSS BEN 0.00000000003163 0.56916 47.0852
28 1RTF BEN 0.0000000001225 0.53686 48.0159
29 1SQA UI1 0.000000001182 0.68589 48.5714
30 3N7O N7O 0.000001974 0.52699 48.6726
31 2AIQ BEN 0.00000003965 0.4931 48.9177
32 1IAU ACE ILE GLU PRO ASJ 0.0000006996 0.60019 49.3392
33 1PQ7 ARG 0.000000000008412 0.66419 49.5536
34 4NFE BEN 0.0000001866 0.46347 49.789
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