Receptor
PDB id Resolution Class Description Source Keywords
4X3I 1.8 Å NON-ENZYME: OTHER THE CRYSTAL STRUCTURE OF ARC N-LOBE COMPLEXED WITH CAMK2A FR RATTUS NORVEGICUS ENDOCYTOSIS MEDIATOR SIGNALING PROTEIN
Ref.: STRUCTURAL BASIS OF ARC BINDING TO SYNAPTIC PROTEIN IMPLICATIONS FOR COGNITIVE DISEASE. NEURON V. 86 490 2015
Ligand
Ligand Chain:Residue Validity Ligand Warnings Binding Data NGL Viewer Molecular Weight (Da) Formula SMILES
ALA THR ARG ASN PHE SER GLY B:309;
Valid;
Atoms found LESS than expected: % Diff = 0;
submit data
737.816 n/a O=C(N...
View in 3D viewer
90% Homology Family
Leader
PDB id Resolution Class Description Source Keywords
4X3H 2.4 Å NON-ENZYME: OTHER CRYSTAL STRUCTURE OF ARC N-LOBE COMPLEXED WITH STARGAZIN PEP RATTUS NORVEGICUS ENDOCYTOSIS MEDIATOR SIGNALING PROTEIN
Ref.: STRUCTURAL BASIS OF ARC BINDING TO SYNAPTIC PROTEIN IMPLICATIONS FOR COGNITIVE DISEASE. NEURON V. 86 490 2015
Members (2)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 1443 families.
1 4X3H Ki = 96 uM ARG ILE PRO SER TYR ARG TYR ARG TYR n/a n/a
2 4X3I - ALA THR ARG ASN PHE SER GLY n/a n/a
70% Homology Family (2)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 1205 families.
1 4X3H Ki = 96 uM ARG ILE PRO SER TYR ARG TYR ARG TYR n/a n/a
2 4X3I - ALA THR ARG ASN PHE SER GLY n/a n/a
50% Homology Family (2)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 1039 families.
1 4X3H Ki = 96 uM ARG ILE PRO SER TYR ARG TYR ARG TYR n/a n/a
2 4X3I - ALA THR ARG ASN PHE SER GLY n/a n/a
Polypharmacology
Similar Ligands
Ligand no: 1; Ligand: ALA THR ARG ASN PHE SER GLY; Similar ligands found: 115
No: Ligand ECFP6 Tc MDL keys Tc
1 ALA THR ARG ASN PHE SER GLY 1 1
2 GLU THR VAL ARG PHE GLN SER ASP 0.538462 0.910714
3 ALA THR VAL ARG THR TYR SER CYS 0.536585 0.85
4 PHE ARG SER LYS GLY GLU GLU LEU PHE THR 0.535088 0.875
5 ARG GLN VAL ASN PHE LEU GLY LYS ILE ASN 0.521368 0.714286
6 ALA GLN PHE SER ALA SER ALA SER ARG 0.516667 0.927273
7 GLY ARG PHE GLN VAL THR 0.508197 0.890909
8 SER LEU ARG PHE LEU TYR GLU GLY 0.507692 0.83871
9 ALA ASN SER ARG PHE PRO THR SER ILE ILE 0.506849 0.794118
10 GLY ALA GLN THR PHE TYR VAL ASP GLY ALA 0.503937 0.737705
11 ALA ASN SER ARG TRP GLN ASP THR ARG LEU 0.503448 0.80303
12 ARG GLN ALA ASN PHE LEU GLY LYS ILE ASN 0.5 0.714286
13 GLY ASN PHE LEU GLN SER ARG 0.5 0.929825
14 VAL ALA PHE ARG SER 0.495726 0.854545
15 GLU GLU ASN LEU LEU ASP PHE VAL ARG PHE 0.489051 0.816667
16 ALA ARG THR GLU LEU TYR ARG SER LEU 0.488722 0.852459
17 PRO ALA THR ILE MET MET GLN ARG GLY ASN 0.487603 0.786885
18 ALA ASN SER ARG TRP ALY THR SER ILE ILE 0.486667 0.779412
19 ALA ASN SER ARG TRP GLN THR SER ILE ILE 0.482993 0.815385
20 ARG ILE PHE SER 0.474576 0.839286
21 SER PHE ALA ASN GLY 0.473214 0.814815
22 SER SER LEU GLU ASN PHE ARG ALA TYR VAL 0.472973 0.854839
23 ALA VAL TYR ASN PHE ALA THR MET 0.462121 0.636364
24 THR LYS ASN TYR LYS GLN PHE SER VAL 0.461538 0.758065
25 ASP ALA GLU PHE ARG HIS ASP 0.460317 0.836364
26 ALA ARG THR M3L GLN THR ALA 2MR LYS 0.458333 0.716418
27 ALA ARG THR M3L GLN THR ALA 0.458333 0.716418
28 ALA GLN ASP ILE TYR ARG ALA SER TYR 0.458333 0.83871
29 ALA LYS PHE ARG HIS ASP 0.458015 0.71875
30 ILE ASN PHE ASP PHE ASN THR ILE 0.453782 0.683333
31 ARG PRO GLY ASN PHE PHE GLN ASN ARG PRO 0.453782 0.724138
32 THR PHE LYS LYS THR ASN 0.453782 0.807018
33 GLU GLU PHE GLY ARG ALA PHE SER PHE 0.452555 0.877193
34 ALA GLU THR PHE TYR VAL ASP GLY 0.452174 0.616667
35 ALA ARG THR 4WQ GLN THR ALA ARG LYS SER 0.452174 0.741935
36 ALA ARG THR MLY GLN THR ALA ARG LYS TYR 0.45082 0.738462
37 ALA ARG THR MLY GLN THR ALA 0.45082 0.738462
38 ALA PHE THR SER 0.448598 0.740741
39 LYS GLN THR ALA ARG M3L SER THR GLY 0.448 0.731343
40 ARG PRO GLY ASN PHE PHE GLN SER ARG PRO 0.446809 0.822581
41 ARG PRO GLY ASN PHE LEU GLN SER ARG LEU 0.446541 0.779412
42 ALA ARG THR ALY GLN THR ALA 0.446281 0.827586
43 SER SER ILE GLU PHE ALA ARG LEU 0.446043 0.87931
44 ARG ABA PHE ILE PHE ALA ASN ILE 0.443609 0.813559
45 GLN THR ALA ARG M3L SER THR GLY 0.443609 0.731343
46 ALA PHE ARG ILE PRO LEU THR ARG 0.442177 0.728571
47 PHE ARG TYR LEU GLY 0.440945 0.774194
48 ARG PRO GLY ASN PHE LEU GLN ASN ARG PRO 0.440298 0.857143
49 SER LEU PHE ASN THR VAL ALA THR LEU TYR 0.438849 0.704918
50 LYS ALA VAL PHE ASN PHE ALA THR MET 0.437956 0.71875
51 CYS THR PHE LYS THR LYS THR ASN 0.435484 0.793103
52 GLU ARG GLU SEP GLU PHE ASP ILE GLU ASP 0.435374 0.753846
53 SER GLU ILE GLU PHE ALA ARG LEU 0.434783 0.862069
54 ALA SER ASN SER ILE ALA SER GLY 0.434783 0.75
55 ARG PRO GLY ASN PHE LEU GLN SER ARG PRO 0.433962 0.757143
56 ARG ABA VAL ILE PHE ALA ASN ILE 0.433824 0.827586
57 ARG TYR GLY PHE VAL ALA ASN PHE 0.432624 0.836066
58 ALA ALA LEU THR ARG ALA 0.432203 0.821429
59 SER LEU PHE ASN THR VAL ALA THR LEU 0.431818 0.754386
60 ALA ARG THR M3L GLN THR ALA ARG LYS 0.430894 0.716418
61 ALA ARG THR M3L GLN THR ALA ARG LYS SER 0.430894 0.716418
62 ILE LYS ARG SER LYS LYS ASN SER LEU ALA 0.428571 0.803571
63 ALA ARG THR MLY GLN THR ALA ARG TYR 0.427536 0.73913
64 SER ARG ARG TRP ARG ARG TRP ASN ARG 0.427481 0.769231
65 ARG ARG LEU ILE PHE NH2 0.427419 0.77193
66 THR GLU ASN LEU TYR PHE GLN SER GLY THR 0.426573 0.774194
67 ALA ARG THR ALA ALA THR ALA ARG LYS SER 0.426087 0.87037
68 ALA ARG 9AT 0.425743 0.851852
69 ALA THR ALY ALA ALA ARG ALY SER ALA PRO 0.42446 0.735294
70 ALA ILE PHE GLN SER SER MET THR LYS 0.42446 0.730159
71 VAL VAL SER HIS PHE ASN ASP 0.424242 0.6875
72 ALA ARG THR MLY GLN THR ALA ARG LYS 0.424 0.723077
73 ALA ARG THR MLZ GLN THR ALA ARG LYS TYR 0.424 0.770492
74 THR LYS ASN TYR LYS GLN THR SER VAL 0.423358 0.770492
75 LYS MET ASN THR GLN PHE THR ALA VAL 0.422535 0.730159
76 ILE LYS ARG SER MLZ LYS ASN SER LEU ALA 0.422414 0.754098
77 CYS VAL ASN GLY SER CYS PHE THR VAL 0.422222 0.807018
78 ALA ARG THR MLY GLN 0.421488 0.712121
79 VAL SER PHE ASN FRD PRO GLN ILE THR ALA 0.421053 0.676056
80 LEU PRO PHE ASP ARG THR THR ILE MET 0.420382 0.702703
81 ARG ARG ARG GLU THR GLN VAL 0.420168 0.842105
82 ALA ILE ARG SER 0.419643 0.785714
83 ALA ARG THR MLY GLN THR ALA ARG LYS SER 0.418803 0.854545
84 ARG GLY PHE ALA LEU M3L SER THR HIS GLY 0.41875 0.72973
85 ALA ARG THR MLY GLN THR ALA ARG MLY SER 0.418033 0.723077
86 ALA ARG THR LYS GLN THR ALA ARG 0.416667 0.839286
87 GLY ARG PRO ARG THR THR SER PHE ALA GLU 0.416667 0.791045
88 LEU GLU PHE GLN GLY 0.416667 0.701754
89 ILE ARG LYS ILE LEU PHE LEU ASP GLY ILE 0.416107 0.770492
90 SER LEU PHE ASN THR ILE ALA VAL LEU 0.414286 0.77193
91 LYS ALA VAL TYR ASN PHE ALA THR MET 0.413793 0.686567
92 ASN TYR THR PRO GLY PRO GLY THR ARG PHE 0.41358 0.736111
93 ASP PHE M3L THR ASP 0.412698 0.647059
94 GLY ASP GLU VAL LYS VAL PHE ARG 0.411348 0.810345
95 MET PHE SER ILE ASP ASN ILE LEU ALA 0.411348 0.698413
96 ASP ALA GLU PHE ARG HIS ASP SER 0.411348 0.730159
97 PRO LYS ARG PRO THR THR LEU ASN LEU PHE 0.411043 0.768116
98 ARG ARG LEU PRO ILE PHE SER ARG LEU 0.410596 0.728571
99 GLU THR LEU LEU ASP LEU ASP PHE ASP PRO 0.410448 0.652174
100 VAL MET ALA PRO ARG THR LEU PHE LEU 0.410256 0.675676
101 SER ARG TYR TRP ALA ILE ARG THR ARG 0.410256 0.73913
102 ASN PHE ASP ASN PRO VAL TYR ARG LYS THR 0.409639 0.726027
103 1IP CYS PHE SER LYS PRO ARG 0.407895 0.753623
104 DPN PRO DAR DTH NH2 0.407692 0.753846
105 TYR GLU LEU ASP GLU LYS PHE ASP ARG LEU 0.406897 0.765625
106 ACE ARG ARG LEU ASN FCL NH2 0.40625 0.774194
107 TRP ASN TRP PHE ASP ILE THR ASN LYS 0.405405 0.61194
108 HY1 CIR VAL ARG 00S 0.404762 0.779661
109 ARG ARG PHE AIB ALA MET LEU ALA 0.404255 0.730159
110 ARG THR PHE SER PRO THR TYR GLY LEU 0.401274 0.726027
111 ARG GLY PRO GLY ARG ALA PHE VAL THR ILE 0.401235 0.753623
112 ALA ARG THR LYS GLN THR ALA ARG LYS 0.4 0.857143
113 ASN ALA LEU LEU ARG TYR LEU LEU ASP 0.4 0.85
114 ARG ILE PRO SER TYR ARG TYR ARG TYR 0.4 0.712329
115 TYR GLN GLU SER THR ASP PHE THR PHE LEU 0.4 0.661017
Similar Binding Sites (Proteins are less than 50% similar to leader)
Pocket No.: 1; Query (leader) PDB : 4X3H; Ligand: ARG ILE PRO SER TYR ARG TYR ARG TYR; 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: 4x3h.bio1) has 22 residues
No: Leader PDB Ligand Sequence Similarity
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