Receptor
PDB id Resolution Class Description Source Keywords
3SJ9 2.4 Å EC: 3.4.22.28 CRYSTAL STRUCTURE OF THE C147A MUTANT 3C OF CVA16 IN COMPLEX FAGLRQAVTQ PEPTIDE HUMAN COXSACKIEVIRUS A16 BINDING TO ITS SUBSTRATE-PEPTIDE CHYMOTRYPSIN-LIKE FOLD PRHYDROLASE
Ref.: ENTEROVIRUS 71 AND COXSACKIEVIRUS A16 3C PROTEASES: TO RUPINTRIVIR AND THEIR SUBSTRATES AND ANTI-HAND, MOUTH DISEASE VIRUS DRUG DESIGN. J.VIROL. V. 85 10319 2011
Ligand
Ligand Chain:Residue Validity Ligand Warnings Binding Data NGL Viewer Molecular Weight (Da) Formula SMILES
PHE ALA GLY LEU ARG GLN ALA VAL THR GLN B:1;
Valid;
none;
submit data
873.003 n/a O=C([...
View in 3D viewer
90% Homology Family
Leader
PDB id Resolution Class Description Source Keywords
3SJK 2.1 Å EC: 3.4.22.28 CRYSTAL STRUCTURE OF THE C147A MUTANT 3C FROM ENTEROVIRUS 71 HUMAN ENTEROVIRUS 71 CHYMOTRYPSIN-LIKE FOLD PROTEASE HYDROLASE
Ref.: ENTEROVIRUS 71 AND COXSACKIEVIRUS A16 3C PROTEASES: TO RUPINTRIVIR AND THEIR SUBSTRATES AND ANTI-HAND, MOUTH DISEASE VIRUS DRUG DESIGN. J.VIROL. V. 85 10319 2011
Members (2)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 3 families.
1 3SJK - LYS PRO VAL LEU ARG THR ALA n/a n/a
2 3SJ9 - PHE ALA GLY LEU ARG GLN ALA VAL THR GLN 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 3 families.
1 3SJK - LYS PRO VAL LEU ARG THR ALA n/a n/a
2 3SJ9 - PHE ALA GLY LEU ARG GLN ALA VAL THR GLN n/a n/a
50% Homology Family (3)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 2 families.
1 3SJK - LYS PRO VAL LEU ARG THR ALA n/a n/a
2 3SJ9 - PHE ALA GLY LEU ARG GLN ALA VAL THR GLN n/a n/a
3 2XYA Kd = 200 uM 7L4 C15 H11 N O c1ccc(cc1)....
Polypharmacology
Similar Ligands
Ligand no: 1; Ligand: PHE ALA GLY LEU ARG GLN ALA VAL THR GLN; Similar ligands found: 111
No: Ligand ECFP6 Tc MDL keys Tc
1 PHE ALA GLY LEU ARG GLN ALA VAL THR GLN 1 1
2 ARG LEU GLN ARG ARG ARG GLU THR GLN VAL 0.609091 0.943396
3 ACE GLU ALA GLN THR ARG LEU 0.6 0.961538
4 GLU ALA GLN THR ARG LEU 0.580357 0.980392
5 MET ABA LEU ARG MET THR ALA VAL MET 0.566667 0.859649
6 ALA ARG THR M3L GLN THR ALA ARG 0.566372 0.793651
7 THR ARG ARG GLU THR GLN LEU 0.559633 0.943396
8 ARG ARG ARG GLU THR GLN VAL 0.556604 0.924528
9 MET CYS LEU ARG MET THR ALA VAL MET 0.552846 0.859649
10 ALA ARG THR MLY GLN 0.541284 0.833333
11 MET CYS LEU ARG NLE THR ALA VAL MET 0.539683 0.844828
12 ALA PRO ALA LEU ARG VAL VAL LYS 0.527778 0.830189
13 ALA ARG THR M3L GLN THR ALA ALA LYS ALA 0.52459 0.793651
14 ACE CSO ARG ALA THR LYS MET LEU 0.512 0.769231
15 ALA ARG THR LYS GLN THR ALA ARG LYS 0.508475 0.87037
16 HIS GLY ALA ALA ARG ALA GLU VAL HIS LEU 0.504348 0.846154
17 GLY HIS LYS ILE LEU HIS ARG LEU LEU GLN 0.5 0.71875
18 ALA ARG THR MLY GLN THR ALA ARG TYR 0.496124 0.746269
19 SAC ARG GLY THR GLN THR GLU 0.495798 0.907407
20 GLY ASN PHE LEU GLN SER ARG 0.492063 0.877193
21 ALA ARG THR MLZ GLN THR ALA ARG LYS 0.491803 0.827586
22 GLY ARG PHE GLN VAL THR 0.487603 0.87037
23 ALA ALA LEU THR ARG ALA 0.486486 0.941176
24 GLN ARG ALA THR LYS MET NH2 0.483607 0.842105
25 LYS ALA ARG VAL LEU ALA GLU ALA MET SER 0.47619 0.818182
26 LYS ALA ARG VAL LEU ALA GLU ALA MET 0.47619 0.818182
27 ALA ARG THR MLZ GLN THR ALA ARG LYS TYR 0.474576 0.842105
28 ALA ARG THR MLY GLN THR ALA ARG LYS 0.474576 0.816667
29 ALA ARG THR M3L GLN THR ALA ARG LYS SER 0.470085 0.777778
30 ALA ARG THR M3L GLN THR ALA ARG LYS 0.470085 0.777778
31 ACE GLN THR ALA ARG PRK SER THR 0.467742 0.857143
32 ILE LYS LEU GLU THR LYS LYS THR LYS LEU 0.46729 0.818182
33 ALA ARG THR MLY GLN THR ALA 0.466102 0.803279
34 ALA ARG THR MLY GLN THR ALA ARG LYS TYR 0.466102 0.803279
35 ARG PRO GLY ASN PHE LEU GLN ASN ARG PRO 0.465116 0.836364
36 ALA GLN THR ALA ARG ALY SER THR 0.464 0.824561
37 ARG VAL ALA GLN LEU GLU GLN VAL TYR ILE 0.463235 0.810345
38 LEU GLY GLY ALA LYS GLN ARG GLY ASP VAL 0.46281 0.867925
39 ARG GLN ALA SEP LEU SER ILE SER VAL 0.462687 0.803279
40 LEU GLU LYS ALA ARG GLY SER THR TYR 0.462069 0.836066
41 ALA ARG THR M3L GLN THR ALA 2MR LYS 0.461538 0.777778
42 ALA ARG THR M3L GLN THR ALA 0.461538 0.777778
43 ALA ARG THR ALY GLN THR ALA 0.461538 0.839286
44 GLY ALA ALA ARG ALA GLU VAL TYR LEU ARG 0.457143 0.783333
45 VAL ALA ARG SER 0.456311 0.865385
46 ARG ARG ALA THR LYS MET NH2 0.454545 0.810345
47 LYS LEU VAL GLN LEU LEU THR THR THR 0.452174 0.830189
48 VAL LEU ARG ASP ASP LEU LEU GLU ALA 0.452174 0.867925
49 THR PHE GLN ALA PSA LEU ARG GLU 0.448276 0.87931
50 ALA ARG THR GLU LEU TYR ARG SER LEU 0.447761 0.833333
51 ACE GLN LEU VAL THR SER LEU 0.445455 0.777778
52 LEU PRO PHE GLU ARG ALA THR VAL MET 0.445161 0.728571
53 GLY LEU LEU GLY SER PRO VAL ARG ALA 0.444444 0.765625
54 LYS PRO VAL LEU ARG THR ALA 0.444444 0.78125
55 VAL ARG SER ARG ARG CYS LEU ARG LEU 0.443478 0.872727
56 ASN SER THR LEU GLN 0.440367 0.759259
57 ACE GLN THR ALA ARG BTK SER THR 0.44 0.890909
58 GLU ALA THR GLN LEU MET ASN 0.438017 0.763636
59 MET CYS PRO ARG MET THR ALA VAL MET 0.4375 0.724638
60 GLY ARG PRO ARG THR THR SER PHE ALA GLU 0.437086 0.720588
61 PHE LEU ARG GLY ARG ALA TYR VAL LEU 0.43662 0.8
62 GLN THR ALA ARG M3L SER 0.436508 0.765625
63 ALA ARG ALA ALA ALA ALA ALA ALA ALA 0.435644 0.823529
64 ALA GLN PHE SER ALA SER ALA SER ARG 0.435484 0.839286
65 GLN LEU ALA THR M3L ALA ALA ARG LYS SER 0.435484 0.761905
66 GLY ARG PHE ALA ALA ALA ILE ALA LYS 0.435115 0.789474
67 ALA DA2 THR M3L GLN THR ALA ARG ALA 0.432836 0.777778
68 ALA ARG LYS LEU ASP 0.432432 0.867925
69 ASN PRO ARG ALA MET GLN ALA LEU LEU 0.431655 0.695652
70 ACE GLN THR ALA ARG KCR SER THR 0.430769 0.839286
71 ALA ARG THR ALA ALA THR ALA ARG LYS SER 0.428571 0.884615
72 PTR LEU ARG VAL ALA 0.428571 0.692308
73 ARG ARG ALA ALA 0.427184 0.807692
74 ACE ALA ARG THR GLU VAL TYR NH2 0.426357 0.859649
75 ASN ARG LEU MET LEU THR GLY 0.42623 0.877193
76 GLY GLU ARG THR ILE PRO ILE THR ARG GLU 0.42446 0.757576
77 GLN THR ALA ARG M3L SER THR GLY 0.424242 0.765625
78 VAL ARG SER ARG ARG ABA LEU ARG LEU 0.423729 0.872727
79 ALA ARG THR M3L GLN THR ALA DA2 LYS 0.423611 0.777778
80 ILE GLN GLN SER ILE GLU ARG ILE 0.422764 0.888889
81 SER SER THR ARG GLY ILE SER GLN LEU TRP 0.422078 0.784615
82 ALA ARG THR MLY GLN THR ALA ARG LYS SER 0.421053 0.903846
83 GLU THR VAL ARG PHE GLN SER ASP 0.42029 0.890909
84 ALA ARG THR LYS GLN THR ALA ARG 0.418803 0.886792
85 ARG ARG ARG TRP ARG ARG LEU THR VAL 0.416058 0.765625
86 SER ASP TYR GLN ARG LEU 0.416 0.842105
87 ARG ASP ARG ALA ALA LYS LEU 0.415929 0.830189
88 ALA ARG 9AT 0.414141 0.901961
89 THR ARG SER GLY ALY VAL MET ARG ARG LEU 0.414062 0.745763
90 GLY ILE LEU GLU PHE VAL PHE THR LEU 0.412214 0.754386
91 THR ILE MET MET GLN ARG GLY 0.41129 0.877193
92 ASN ARG LEU LEU LEU THR GLY 0.410714 0.942308
93 GLY ALA ARG ALA HIS SER SER 0.409449 0.734375
94 ALA ASN SER ARG VAL GLN ASP SER ILE ILE 0.409091 0.875
95 GLU GLU ASN LEU LEU ASP PHE VAL ARG PHE 0.408451 0.79661
96 ALA ARG THR MLY GLN THR ALA ARG MLY SER 0.408333 0.816667
97 PRO ALA THR ILE MET MET GLN ARG GLY ASN 0.408 0.859649
98 ALA ASN SER ARG TRP GLN ASP THR ARG LEU 0.407895 0.757576
99 SER SER ILE GLU PHE ALA ARG LEU 0.407143 0.859649
100 THR PRO THR ARG ASP VAL ALA THR SER PRO 0.407143 0.746269
101 GLY LEU LEU GLY SEP PRO VAL ARG ALA 0.406897 0.676056
102 ARG GLU ASP GLN GLU THR ALA VAL 0.40678 0.769231
103 HIS LYS LEU VAL GLN LEU LEU THR THR THR 0.406015 0.714286
104 SER GLU ILE GLU PHE ALA ARG LEU 0.405797 0.875
105 LEU PRO PHE GLU ARG ALA THR ILE MET 0.403727 0.71831
106 PRO SER ARG VAL 0.403509 0.827586
107 GLU GLU TYR LEU GLN ALA PHE THR TYR 0.402878 0.694915
108 ARG VAL LEU PHE GLU ALA MET 0.402878 0.75
109 ACE ALA ARG THR LYS GLN 0.401709 0.867925
110 PHE TYR ARG ALA LEU MET 0.40146 0.730159
111 ALA MET ALA PRO ARG THR LEU LEU LEU 0.4 0.724638
Similar Binding Sites (Proteins are less than 50% similar to leader)
Pocket No.: 1; Query (leader) PDB : 3SJK; Ligand: LYS PRO VAL LEU ARG THR ALA; 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: 3sjk.bio1) has 12 residues
No: Leader PDB Ligand Sequence Similarity
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