Receptor
PDB id Resolution Class Description Source Keywords
1NTV 1.5 Å NON-ENZYME: SIGNAL_HORMONE CRYSTAL STRUCTURE OF THE DISABLED-1 (DAB1) PTB DOMAIN-APOER2 COMPLEX MUS MUSCULUS BETA-SANDWICH SIGNALING PROTEIN
Ref.: ORIGINS OF PEPTIDE SELECTIVITY AND PHOSPHOINOSITIDE REVEALED BY STRUCTURES OF DISABLED-1 PTB DOMAIN COM STRUCTURE V. 11 569 2003
Ligand
Ligand Chain:Residue Validity Ligand Warnings Binding Data NGL Viewer Molecular Weight (Da) Formula SMILES
ASN PHE ASP ASN PRO VAL TYR ARG LYS THR B:5;
Valid;
none;
submit data
1239.4 n/a O=C(N...
PO4 A:200;
Invalid;
none;
submit data
94.971 O4 P [O-]P...
View in 3D viewer
90% Homology Family
Leader
PDB id Resolution Class Description Source Keywords
1NTV 1.5 Å NON-ENZYME: SIGNAL_HORMONE CRYSTAL STRUCTURE OF THE DISABLED-1 (DAB1) PTB DOMAIN-APOER2 COMPLEX MUS MUSCULUS BETA-SANDWICH SIGNALING PROTEIN
Ref.: ORIGINS OF PEPTIDE SELECTIVITY AND PHOSPHOINOSITIDE REVEALED BY STRUCTURES OF DISABLED-1 PTB DOMAIN COM STRUCTURE V. 11 569 2003
Members (3)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 286 families.
1 1NTV - ASN PHE ASP ASN PRO VAL TYR ARG LYS THR n/a n/a
2 1OQN - I3P C6 H15 O15 P3 [C@H]1([C@....
3 1NU2 - I3P C6 H15 O15 P3 [C@H]1([C@....
70% Homology Family (4)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 209 families.
1 1M7E - ASN GLY TYR GLU ASN PRO THR TYR LYS n/a n/a
2 1NTV - ASN PHE ASP ASN PRO VAL TYR ARG LYS THR n/a n/a
3 1OQN - I3P C6 H15 O15 P3 [C@H]1([C@....
4 1NU2 - I3P C6 H15 O15 P3 [C@H]1([C@....
50% Homology Family (4)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 174 families.
1 1M7E - ASN GLY TYR GLU ASN PRO THR TYR LYS n/a n/a
2 1NTV - ASN PHE ASP ASN PRO VAL TYR ARG LYS THR n/a n/a
3 1OQN - I3P C6 H15 O15 P3 [C@H]1([C@....
4 1NU2 - I3P C6 H15 O15 P3 [C@H]1([C@....
Polypharmacology
Similar Ligands
Ligand no: 1; Ligand: ASN PHE ASP ASN PRO VAL TYR ARG LYS THR; Similar ligands found: 211
No: Ligand ECFP6 Tc MDL keys Tc
1 ASN PHE ASP ASN PRO VAL TYR ARG LYS THR 1 1
2 GLY TYR GLU ASN PRO THR TYR LYS PHE PHE 0.624242 0.888889
3 ARG LEU TYR GLN ASN PRO THR THR TYR ILE 0.572254 0.959459
4 LYS PRO ILE VAL GLN TYR ASP ASN PHE 0.563953 0.878378
5 ASN GLY TYR GLU ASN PRO THR TYR LYS 0.56213 0.888889
6 ASN ASP LYS TYR GLU PRO PHE TRP GLU 0.554348 0.837838
7 ILE ARG TYR PRO LYS THR PHE GLY TRP 0.549738 0.907895
8 ALA ASN SER ARG TYR PRO THR SER ILE ILE 0.547059 0.906667
9 ASN TYR THR PRO GLY PRO GLY THR ARG PHE 0.544944 0.986111
10 SER SER TYR ARG ARG PRO VAL GLY ILE 0.544379 0.906667
11 ALA ILE MET PRO ALA ARG PHE TYR PRO LYS 0.543478 0.846154
12 LYS LEU TYR GLN ASN PRO THR THR TYR ILE 0.543353 0.878378
13 ASN TYR THR PRO GLY PRO GLY ILE ARG PHE 0.535912 0.959459
14 TYR PRO LYS ARG ILE ALA 0.533742 0.851351
15 GLN VAL PRO LEU ARG PRO MET THR TYR LYS 0.532258 0.896104
16 LEU PRO PHE ASP ARG THR THR ILE MET 0.528409 0.846154
17 ARG ILE PRO SER TYR ARG TYR ARG TYR 0.527607 0.906667
18 ARG THR TYR SEP GLY PRO MET ASN LYS VAL 0.52356 0.833333
19 ARG MET PHE PRO ASN ALA PRO TYR LEU 0.522222 0.910256
20 ARG THR PHE SER PRO THR TYR GLY LEU 0.52 0.945946
21 PRO LYS ARG PRO THR THR LEU ASN LEU PHE 0.516484 0.917808
22 ARG SEP PRO VAL PHE SER 0.514793 0.772152
23 1IP CYS PHE SER LYS PRO ARG 0.511628 0.853333
24 ASN ARG PRO VAL TYR ILE PRO ARG PRO PRO 0.508876 0.864865
25 GLU VAL ALA PRO PRO GLU TYR HIS ARG LYS 0.507772 0.918919
26 PHE ASN ARG PRO VAL 0.506329 0.861111
27 LEU PHE GLY TYR PRO VAL TYR VAL 0.506024 0.821918
28 TYR GLU LEU ASP GLU LYS PHE ASP ARG LEU 0.506024 0.794521
29 ALA ASN SER ARG PHE PRO THR SER ILE ILE 0.502825 0.866667
30 LEU PRO PHE ASP LYS THR THR ILE MET 0.5 0.769231
31 ALA PHE ARG ILE PRO LEU THR ARG 0.5 0.878378
32 ARG PRO MET THR TYR LYS GLY ALA LEU 0.497326 0.871795
33 LEU PRO PHE ASP LYS SER THR ILE MET 0.497238 0.759494
34 ARG ARG LEU PRO ILE PHE SER ARG LEU 0.49711 0.853333
35 LEU SER SER PRO VAL THR LYS SER PHE 0.497041 0.783784
36 LYS VAL PRO ARG ASN GLN ASP TRP LEU 0.494737 0.88
37 ARG PRO MET THR PHE LYS GLY ALA LEU 0.491979 0.833333
38 LEU PRO PHE GLU ARG ALA THR VAL MET 0.48913 0.844156
39 SER THR SEP PRO THR PHE ASN LYS 0.488764 0.759494
40 LEU LEU PHE GLY TYR PRO VAL TYR VAL 0.488372 0.821918
41 LEU LEU PHE GLY PHE PRO VAL TYR VAL 0.488372 0.821918
42 PRO PRO ARG PRO ILE TYR ASN ARG ASN 0.485714 0.905405
43 LEU LEU PHE GLY LYS PRO VAL TYR VAL 0.485714 0.8
44 ACE TYR PRO ILE GLN GLU THR 0.484848 0.76
45 LYS PRO VAL LEU ARG THR ALA 0.484848 0.849315
46 ARG GLN PHE GLY PRO ASP PHE PRO THR ILE 0.483871 0.918919
47 ARG TYR PRO LEU THR PHE GLY TRP 0.481865 0.933333
48 GLN VAL PRO SER ASP PRO TYR ASN TYR 0.47929 0.876712
49 TYR LEU LYS GLU PRO VAL HIS GLY VAL 0.478261 0.837838
50 ASP TYR GLU PRO ILE PRO GLU GLU ALA PHE 0.477528 0.824324
51 DPN PRO DAR DTH NH2 0.477419 0.833333
52 PHE PRO THR LYS ASP VAL ALA LEU 0.477012 0.821918
53 ASP VAL GLN THR GLY ARG ARG PRO TYR GLU 0.47541 0.958333
54 GLY ARG PRO ARG THR THR SER PHE ALA GLU 0.475138 0.890411
55 SER SER LEU GLU ASN PHE ARG ALA TYR VAL 0.47486 0.797297
56 GLU GLU PRO THR VAL ILE LYS LYS TYR 0.47191 0.837838
57 TYR GLN PHE GLY PRO ASP PHE PRO ILE ALA 0.469945 0.837838
58 PHE LEU PRO HIS ALY TYR ASP VAL LYS LEU 0.468421 0.802632
59 GLY SER ASP PRO PHE LYS 0.468354 0.767123
60 VAL SER GLN ASN TYR PRO ILE VAL GLN ASN 0.467836 0.826667
61 GLY ASP GLU VAL LYS VAL PHE ARG 0.467066 0.708333
62 ARG TYR PRO LEU THR PHE GLY TRP CYS PHE 0.465686 0.921053
63 LEU PRO PHE GLU LYS SER THR VAL MET 0.464088 0.769231
64 TYR PRO TYR ASP VAL PRO ASP TYR ALA 0.463415 0.861111
65 ARG PRO GLY ASN PHE LEU GLN SER ARG LEU 0.460317 0.878378
66 LYS PRO PHE PTR VAL ASN VAL NH2 0.460227 0.820513
67 ARG PRO PRO ILE PHE ILE ARG ARG LEU 0.460227 0.824324
68 ASN ALA LEU LEU ARG TYR LEU LEU ASP 0.459627 0.767123
69 SER PRO LYS ARG ILE ALA 0.459119 0.797297
70 VAL LYS VAL VAL ALA LYS LYS TYR ARG ASN 0.459119 0.791667
71 TYR MET PHE PRO ASN ALA PRO TYR LEU 0.458101 0.820513
72 SER PRO ILE VAL PRO SER PHE ASP MET 0.457627 0.759494
73 ALA ARG SER HIS SEP TYR PRO ALA 0.456989 0.85
74 LYS LEU PRO ALA GLN PHE TYR ILE LEU 0.456522 0.824324
75 ILE GLY PRO GLY ARG ALA PHE TYR ALA 0.456044 0.878378
76 GLY ARG PHE GLN VAL THR 0.455696 0.694444
77 VAL PRO LEU ARG PRO MET THR TYR 0.455556 0.883117
78 ALA ASN SER ARG TRP PRO THR THR ARG LEU 0.454545 0.907895
79 ILE GLY PRO GLY ARG ALA PHE TYR VAL 0.454054 0.891892
80 ILE GLY PRO GLY ARG ALA PHE TYR THR 0.454054 0.891892
81 VAL MET ALA PRO ARG THR LEU PHE LEU 0.453552 0.820513
82 GLU LEU ASN ARG LYS MET ILE TYR MET 0.453039 0.730769
83 LEU PRO PHE GLU ARG ALA THR ILE MET 0.452632 0.833333
84 LYS GLN GLU PRO GLN GLU ILE ASP PHE 0.452514 0.72973
85 LEU TYR ALA SER PRO GLN LEU GLU GLY PHE 0.451613 0.837838
86 LYS PRO PHE PTR VAL ASN VAL GLU PHE 0.451613 0.833333
87 GLY TYR GLN ASP TYR GLU PRO GLU ALA 0.450617 0.777778
88 THR PRO TYR ASP ILE ASN GLN MET LEU 0.450549 0.794872
89 ASN ASP TRP LEU LEU PRO SER TYR 0.449198 0.868421
90 SER ARG ASP HIS SER ARG THR PRO MET 0.449198 0.835443
91 ASP PHE GLU GLU ILE PRO GLY GLU TYR LEU 0.448649 0.837838
92 TYR PRO ASN VAL ASN ILE HIS ASN PHE 0.448087 0.866667
93 PHE LEU PRO SER ASP PHE PHE PRO SER VAL 0.447059 0.837838
94 GLU THR VAL ARG PHE GLN SER ASP 0.447059 0.712329
95 ILE THR ASP GLN VAL PRO PHE SER VAL 0.446927 0.786667
96 ARG TYR PRO LEU THR LEU GLY TRP CYS PHE 0.446602 0.934211
97 ALA GLN ASP ILE TYR ARG ALA SER TYR 0.446328 0.76
98 GLN MET PRO THR GLU ASP GLU TYR 0.446328 0.792208
99 GLU ASN GLN LYS GLU TYR PHE PHE 0.44586 0.694444
100 ARG PHE PRO LEU THR PHE GLY TRP 0.445596 0.906667
101 ILE GLY PRO GLY ARG ALA PHE TYR THR ILE 0.445026 0.918919
102 ILE SER PRO ARG THR LEU ASP ALA TRP 0.444444 0.883117
103 PRO SER ILE ASP ARG SER THR LYS PRO 0.444444 0.853333
104 GLU TYR LEU GLY LEU ASP VAL PRO VAL 0.443182 0.808219
105 SER SER ARG LYS GLU TYR TYR ALA 0.443038 0.763889
106 ARG PRO LYS ARG ILE ALA 0.442424 0.77027
107 ARG PRO GLY ASN PHE LEU GLN SER ARG PRO 0.442105 0.88
108 TYR LEU GLY GLY PRO ASP PHE PRO THR ILE 0.441489 0.878378
109 GLY GLN VAL PRO PHE SER LYS GLU GLU CYS 0.441341 0.786667
110 DPN PRO DAR ILE NH2 0.440252 0.743243
111 GLN LEU SER PRO PHE PRO PHE ASP LEU 0.44 0.824324
112 THR ASN GLU TYR LYS VAL 0.43871 0.694444
113 SER PHE PHE GLU ASP ASN PHE VAL PRO GLU 0.43787 0.849315
114 ALA ASN SER ARG TRP PRO THR SER ALY ILE 0.437186 0.860759
115 ILE MET ASP GLN VAL PRO PHE SER VAL 0.437158 0.734177
116 GLU GLU ASN LEU LEU ASP PHE VAL ARG PHE 0.436782 0.739726
117 SER ASP TYR GLN ARG LEU 0.436709 0.726027
118 ARG PRO PRO GLY PHE SER PRO PHE ALA 0.436464 0.876712
119 ARG HIS ARG MLZ VAL LEU ARG ASP ASN TYR 0.43617 0.807692
120 ASP PHE GLU GLU ILE PRO GLU GLU TYS 0.435754 0.693182
121 GLN ASN GLY PTR VAL ASN PRO THR TYR 0.435028 0.846154
122 ARG ARG ARG GLU ARG SER PRO THR ARG 0.432749 0.849315
123 GLN ASN TYR PRO ILE VAL GLN 0.432749 0.810811
124 ALA ASN SER ARG TRP PRO THR SER 2KK ILE 0.432039 0.851852
125 ARG LEU TYR HIS SEP LEU PRO ALA 0.431579 0.839506
126 PHE ARG TYR LEU GLY 0.43125 0.753425
127 DPN PRO DAR CYS NH2 0.43038 0.739726
128 THR LYS ASN TYR LYS GLN PHE SER VAL 0.430303 0.739726
129 SER ASP ILE LEU PHE PRO ALA ASP SER 0.430233 0.773333
130 PHE TYR ALA PRO GLU PRO ILE THR SER LEU 0.430108 0.855263
131 VAL ORN LEU DPN PRO VAL ORN LEU DPN PRO 0.429412 0.753425
132 ARG GLY PRO GLY ARG ALA PHE VAL THR ILE 0.429319 0.878378
133 ALA ASN SER ARG TRP PRO THR SER FAK ILE 0.428571 0.839506
134 SER ILE TYR PHE TPO PRO GLU LEU TYR ASP 0.427835 0.802469
135 LEU GLN ARG VAL LEU SEP ALA PRO PHE 0.427778 0.753086
136 LEU ASN PHE PRO ILE SER PRO 0.427711 0.813333
137 ALA LYS PHE ARG HIS ASP 0.427711 0.753425
138 ILE LEU LYS GLU PRO VAL HIS GLY VAL 0.427027 0.746667
139 LYS ALA VAL TYR ASN PHE ALA THR MET 0.426136 0.701299
140 ALA ASN SER ARG TRP PRO THR SER 2KP ILE 0.425837 0.851852
141 HIS HIS ALA SER PRO ARG LYS 0.425414 0.824324
142 LYS THR PHE PRO PRO THR GLU PRO LYS 0.424581 0.833333
143 PHE ASN PHE PRO GLN ILE THR 0.424419 0.810811
144 ARG PHE PRO LEU THR PHE GLY TRP CYS PHE 0.42439 0.907895
145 SER LEU ARG PHE LEU TYR GLU GLY 0.423529 0.783784
146 GLU LEU ARG ARG LYS MET MET TYR MET 0.423529 0.714286
147 ALA ASN SER ARG TRP PRO ALY SER ILE ILE 0.422886 0.848101
148 LYS ARG ARG ARG HIS PRO SER 0.421965 0.797297
149 GLU GLN TYR LYS PHE TYR SER VAL 0.421687 0.726027
150 SER THR GLY GLY VAL M3L LYS PRO HIS ARG 0.421569 0.814815
151 LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE 0.420765 0.756757
152 ILE ARG LYS ILE LEU PHE LEU ASP GLY ILE 0.41989 0.68
153 ASP ALA GLU PHE ARG HIS ASP 0.419753 0.652778
154 GLY PHE ARG PRO 0.419355 0.777778
155 GLU LEU LYS ARG LYS MET ILE TYR MET 0.418994 0.692308
156 DPN PRO ARG 0.418301 0.75
157 ARG GLN PHE GLY PRO ASP TRP ILE VAL ALA 0.418269 0.842105
158 TRP GLU TYR ILE PRO ASN VAL 0.417989 0.828947
159 ARG PRO LYS PRO LEU VAL ASP PRO 0.417178 0.780822
160 GLU SER ASP PRO ILE VAL ALA GLN TYR 0.416216 0.826667
161 PRO VAL LYS ARG ARG LEU ASP LEU GLU 0.416185 0.739726
162 GLY LEU LEU GLY SER PRO VAL ARG ALA 0.416185 0.810811
163 ARG ARG ILE TYR ASP LEU ILE GLU LEU 0.414773 0.743243
164 DTY ILE ARG LEU LPD 0.414201 0.837838
165 DVA DPR GLY DSN DGN DHI DTY DAS DSN 0.413978 0.891892
166 MET VAL TRP GLY PRO ASP PRO LEU TYR VAL 0.413793 0.797468
167 PHE ALA PRO GLY ASN TYR PRO ALA LEU 0.413043 0.878378
168 ASP PHE GLU ASP TYR GLU PHE ASP 0.412903 0.608108
169 LYS ARG ARG ARG HIS PRO SER GLY 0.412429 0.837838
170 THR PRO ARG ARG SER MLZ SER ALA 0.412121 0.782051
171 ALA PRO ASP THR ARG PRO 0.412121 0.876712
172 GLU ARG GLU SEP GLU PHE ASP ILE GLU ASP 0.412088 0.62963
173 ALA ASN SER ARG ALY PRO THR SER ILE ILE 0.411765 0.831169
174 LYS PRO ILE VAL VAL LEU HIS GLY TYR 0.411458 0.826667
175 5JP PRO LYS ARG ILE ALA 0.411392 0.763158
176 PHE GLN PRO GLN ASN GLY GLN PHE ILE 0.411111 0.783784
177 ALA PRO ASP THR ARG PRO ALA PRO 0.410714 0.876712
178 ARG THR PRO SEP LEU PRO THR 0.410405 0.775
179 SER ALA PRO ASP THR ARG PRO ALA 0.410405 0.864865
180 ALA THR ARG ASN PHE SER GLY 0.409639 0.726027
181 GLY VAL TYR ASP GLY ARG GLU HIS THR VAL 0.409574 0.876712
182 ASN ARG PRO ILE LEU SER LEU 0.409357 0.84
183 THR LYS ASN TYR LYS GLN THR SER VAL 0.409357 0.726027
184 TYR PRO PHE PHE NH2 0.409091 0.75
185 GLN PHE LYS ASP ASN VAL ILE LEU LEU 0.409091 0.635135
186 GLY GLU ARG THR ILE PRO ILE THR ARG GLU 0.409091 0.851351
187 ARG TYR GLY PHE VAL ALA ASN PHE 0.409091 0.805556
188 LEU ASP PRO ARG 0.408805 0.794521
189 ARG HIS ARG MLY VAL LEU ARG ASP TYR 0.408602 0.833333
190 GLU THR PHE TYR VAL ASP GLY 0.408537 0.722222
191 ASP PHE GLU GLU ILE PRO GLY GLU PTR 0.408377 0.775
192 PHQ LEU VAL ARG TYR 0.407186 0.710526
193 PHE TYR ARG ALA LEU MET 0.406977 0.688312
194 ASP ILE ASN TYR TYR THR SER GLU PRO 0.405556 0.853333
195 DHI PRO PHE HIS LEU LEU VAL TYR 0.405263 0.824324
196 ILE ARG ALA ALA PRO PRO PRO LEU PHE 0.404372 0.813333
197 MET CYS PRO ARG MET THR ALA VAL MET 0.404372 0.818182
198 GLU TYR GLY PRO LYS TRP ASN LYS 0.404255 0.810811
199 GLU GLY PRO ARG ASN GLN ASP TRP LEU 0.40404 0.88
200 THR TYR LYS PHE PHE GLU GLN 0.403727 0.708333
201 GLU ASN PRO THR TYR LYS PHE PHE GLU GLN 0.403727 0.708333
202 ASP ILE ASN TYR TYR ALA SER GLU PRO 0.403315 0.853333
203 GLN ASN GLY PTR GLU ASN PRO THR TYR 0.403315 0.794872
204 PHE LEU ARG GLY ARG ALA TYR VAL LEU 0.403315 0.767123
205 GLY ALA GLN THR PHE TYR VAL ASP GLY ALA 0.402367 0.722222
206 PHE GLU ALA ILE PRO ALA GLU TYR LEU 0.402174 0.797297
207 PHE ALA PRO GLY PHE PHE PRO TYR LEU 0.401099 0.824324
208 LEU GLU LYS ALA ARG GLY SER THR TYR 0.40107 0.797297
209 HIS SER ILE THR TYR LEU LEU PRO VAL 0.4 0.855263
210 MAA LYS PRO PHE 0.4 0.684932
211 CYS THR PHE LYS THR LYS THR ASN 0.4 0.671233
Similar Binding Sites (Proteins are less than 50% similar to leader)
Pocket No.: 1; Query (leader) PDB : 1NTV; Ligand: ASN PHE ASP ASN PRO VAL TYR ARG LYS THR; 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: 1ntv.bio1) has 24 residues
No: Leader PDB Ligand Sequence Similarity
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