Receptor
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
Ligand
Ligand Chain:Residue Validity Ligand Warnings Binding Data NGL Viewer Molecular Weight (Da) Formula SMILES
LYS PRO VAL LEU ARG THR ALA B:1;
Valid;
none;
submit data
785.989 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: LYS PRO VAL LEU ARG THR ALA; Similar ligands found: 193
No: Ligand ECFP6 Tc MDL keys Tc
1 LYS PRO VAL LEU ARG THR ALA 1 1
2 ARG PRO LYS ARG ILE ALA 0.691667 0.876923
3 SER PRO LYS ARG ILE ALA 0.628099 0.907692
4 TYR PRO LYS ARG ILE ALA 0.604478 0.855072
5 GLY LEU LEU GLY SER PRO VAL ARG ALA 0.590909 0.923077
6 ALA MET ALA PRO ARG THR LEU LEU LEU 0.586466 0.926471
7 THR LYS PRO ARG 0.585586 0.84127
8 ARG PRO LYS PRO LEU VAL ASP PRO 0.568 0.861538
9 GLY LEU LEU GLY SEP PRO VAL ARG ALA 0.553191 0.819444
10 3BY PRO LYS ARG ILE ALA 0.540741 0.814286
11 PRO PRO LYS ARG ILE ALA 0.540741 0.876923
12 ARG PRO MET THR PHE LYS GLY ALA LEU 0.534591 0.887324
13 GLY GLU ARG THR ILE PRO ILE THR ARG GLU 0.532374 0.939394
14 ARG PRO MET THR TYR LYS GLY ALA LEU 0.53125 0.851351
15 ARG PRO ARG PRO ASP ASP LEU GLU ILE 0.528571 0.880597
16 ALA PHE ARG ILE PRO LEU THR ARG 0.527397 0.940298
17 ALA PRO ALA LEU ARG VAL VAL LYS 0.525424 0.730159
18 ARG PRO GLN VAL PRO LEU ARG PRO MET 0.524476 0.828571
19 MET CYS PRO ARG MET THR ALA VAL MET 0.520548 0.926471
20 ARG LEU PRO ALA LYS ALA PRO LEU LEU 0.517986 0.878788
21 ALA ARG MLZ SER ALA PRO ALA THR 0.517986 0.898551
22 GLU ARG THR ILE PRO ILE THR ARG GLU 0.514925 0.938462
23 ALA ASN SER ARG ALA PRO THR SER ILE ILE 0.513889 0.884058
24 ALA ASN SER ARG VAL PRO THR SER ILE ILE 0.510791 0.939394
25 ARG GLN PRO ALA LYS ALA PRO LEU LEU 0.51049 0.865672
26 VAL MET ALA PRO ARG THR LEU PHE LEU 0.509804 0.9
27 LYS ALA PRO ARG ALY GLN LEU ALA THR LYS 0.507463 0.848485
28 LYS LEU THR PRO LEU CYS VAL THR LEU 0.507353 0.876923
29 5JP PRO LYS ARG ILE ALA 0.504 0.865672
30 ASN ARG PRO ILE LEU SER LEU 0.50365 0.897059
31 SER ALA PRO ASP THR ARG PRO ALA 0.503597 0.897059
32 VAL PRO LEU ARG PRO MET THR TYR 0.503311 0.863014
33 LEU PRO PHE GLU ARG ALA THR VAL MET 0.503145 0.9
34 ASP ARG VAL GLU LEU ASN ALA PRO ARG GLN 0.5 0.909091
35 ARG ARG ARG GLU ARG SER PRO THR ARG 0.5 0.909091
36 GLN VAL PRO LEU ARG PRO MET THR TYR LYS 0.497006 0.851351
37 TYR LEU GLU PRO ALA PRO VAL THR ALA 0.496504 0.788732
38 CYS THR PRO SER ARG 0.496124 0.893939
39 LYS PRO ILE VAL VAL LEU HIS GLY TYR 0.493671 0.753425
40 ALA LEU PRO HIS ALA ILE LEU ARG LEU 0.493421 0.852941
41 ALA ASN SER ARG LEU PRO THR SER ILE ILE 0.489209 0.939394
42 PRO LYS ARG PRO THR THR LEU ASN LEU PHE 0.487654 0.898551
43 ALA ASN SER ARG ALY PRO THR SER ILE ILE 0.487013 0.885714
44 ASN PHE ASP ASN PRO VAL TYR ARG LYS THR 0.484848 0.849315
45 ARG VAL ALA SER PRO THR SER GLY VAL 0.482269 0.924242
46 ASN LEU VAL PRO VAL VAL ALA THR VAL 0.481481 0.833333
47 DPN PRO DAR DTH NH2 0.480916 0.892308
48 PRO SER ILE ASP ARG SER THR LYS PRO 0.480263 0.911765
49 LEU GLN ARG VAL LEU SEP ALA PRO PHE 0.48 0.797297
50 TYR LEU ALA PRO GLY PRO VAL THR ALA 0.479167 0.802817
51 GLU LEU PRO LEU VAL LYS ILE 0.478261 0.8
52 ALA PRO ASP THR ARG PRO 0.477612 0.910448
53 ARG LEU GLN ARG ARG ARG GLU THR GLN VAL 0.476923 0.769231
54 ASN ARG PRO VAL TYR ILE PRO ARG PRO PRO 0.47651 0.842857
55 THR PRO ARG VAL THR GLY GLY GLY ALA MET 0.47651 0.9
56 ASN PRO ARG ALA MET GLN ALA LEU LEU 0.475862 0.869565
57 VAL MET ALA PRO ARG ALA LEU LEU LEU 0.475177 0.852941
58 SER LEU SER ARG THR PRO ALA ASP GLY ARG 0.473333 0.924242
59 LEU PRO PHE ASP ARG THR THR ILE MET 0.471698 0.875
60 SER SER GLY LYS VAL PRO LEU SER 0.470588 0.848485
61 PHE PRO THR LYS ASP VAL ALA LEU 0.470199 0.850746
62 ARG PRO PRO ILE PHE ILE ARG ARG LEU 0.470199 0.852941
63 GLY ARG PRO ARG THR THR SER PHE ALA GLU 0.468354 0.897059
64 ILE LEU LYS GLU PRO VAL HIS GLY VAL 0.467949 0.768116
65 ILE SER PRO ARG THR LEU ASP ALA TRP 0.467836 0.863014
66 ALA ARG THR M3L GLN THR ALA ALA LYS ALA 0.467153 0.760563
67 THR PRO ARG ARG SER MLZ SER ALA 0.466667 0.884058
68 LEU PRO PRO VAL VAL ALA LYS GLU ILE 0.465753 0.776119
69 ASN LEU VAL PRO GLN VAL ALA THR VAL 0.464789 0.833333
70 LYS PRO LYS 0.464286 0.746032
71 ALA PRO ASP THR ARG PRO ALA PRO 0.463768 0.910448
72 TYR LEU GLU PRO GLY PRO VAL THR ALA 0.463576 0.814286
73 ASN LEU VAL PRO THR VAL ALA THR VAL 0.463235 0.833333
74 LEU SER SER PRO VAL THR LYS SER PHE 0.463087 0.835821
75 LEU PRO LYS MYK THR GLY GLY 0.463087 0.835821
76 ARG LEU TYR GLN ASN PRO THR THR TYR ILE 0.462963 0.837838
77 ASP LEU THR ARG PRO 0.462121 0.953846
78 LEU PRO PHE GLU ARG ALA THR ILE MET 0.460606 0.887324
79 MET ABA LEU ARG MET THR ALA VAL MET 0.460432 0.735294
80 PRO VAL LYS ARG ARG LEU ASP LEU GLU 0.458333 0.815385
81 ILE PRO LEU THR GLU GLU ALA GLU LEU 0.456522 0.861538
82 PTR LEU ARG VAL ALA 0.455224 0.626667
83 ALA ASN SER ARG TRP PRO THR THR ARG LEU 0.453988 0.863014
84 TYR LEU LYS GLU PRO VAL HIS GLY VAL 0.453988 0.763889
85 ACE GLN GLU ARG GLU VAL PRO CYS 0.453237 0.863636
86 ARG THR PHE SER PRO THR TYR GLY LEU 0.45283 0.849315
87 ALA ASN SER ARG PHE PRO THR SER ILE ILE 0.45283 0.871429
88 ALA ASN SER ARG TYR PRO THR SER ILE ILE 0.452229 0.835616
89 SER SER GLY LYS VAL PRO LEU 0.451852 0.861538
90 ALA ALA LEU THR ARG ALA 0.451613 0.761905
91 ARG THR PRO SEP LEU PRO THR 0.451389 0.847222
92 MET CYS LEU ARG MET THR ALA VAL MET 0.450704 0.735294
93 ALA ARG LYS LEU ASP 0.45 0.734375
94 ASN LEU VAL PRO SER VAL ALA THR VAL 0.45 0.835821
95 ALA ALA ARG KCR SER ALA PRO ALA 0.449664 0.909091
96 ARG ILE ILE PRO ARG HIS LEU GLN LEU 0.449367 0.828571
97 ASN LEU VAL PRO MET VAL ALA THR VAL 0.448276 0.785714
98 HIS HIS ALA SER PRO ARG LYS 0.448052 0.826087
99 LEU PRO PRO GLU GLU ARG LEU ILE 0.447552 0.878788
100 ARG VAL ALA SEP PRO THR SER GLY VAL 0.447368 0.847222
101 LEU PRO PHE GLU LYS SER THR VAL MET 0.446541 0.791667
102 PRO ARG PRO ILE LEU LEU PRO TRP ARG NH2 0.446541 0.788732
103 LYS ARG ARG ARG HIS PRO SER 0.445205 0.797101
104 ARG ARG LEU PRO ILE PHE SER ARG LEU 0.445161 0.911765
105 SER HIS PRO ARG PRO ILE ARG VAL 0.444444 0.885714
106 ILE PRO ALA TYR GLY VAL LEU THR ILE 0.444444 0.8
107 GLN ARG SER THR SEP THR PRO ASN VAL HIS 0.444444 0.821918
108 PHE ALA GLY LEU ARG GLN ALA VAL THR GLN 0.444444 0.78125
109 LYS ARG ARG ARG HIS PRO SER GLY 0.442953 0.814286
110 MET CYS LEU ARG NLE THR ALA VAL MET 0.441379 0.724638
111 LYS LEU TYR GLN ASN PRO THR THR TYR ILE 0.440994 0.756757
112 ALA ARG THR LYS GLN THR ALA ARG LYS 0.440298 0.738462
113 LYS GLY PRO PRO ALA ALA LEU THR LEU 0.439189 0.863636
114 GLN PRO PRO VAL PRO PRO GLN ARG PRO MET 0.437086 0.828571
115 DPN PRO DAR ILE NH2 0.437037 0.818182
116 ALA ARG THR LYS GLN THR ALA ARG 0.436508 0.75
117 ARG ILE PRO SER TYR ARG TYR ARG TYR 0.436242 0.835616
118 LYS ALA ARG VAL LEU ALA GLU ALA MET 0.435714 0.647059
119 LYS ALA ARG VAL LEU ALA GLU ALA MET SER 0.435714 0.647059
120 SER PRO ARG LEU PRO LEU LEU GLU SER 0.434783 0.875
121 ALA ASN SER ARG TRP PRO THR SER ALY ILE 0.434286 0.815789
122 ILE ARG TYR PRO LYS THR PHE GLY TRP 0.434066 0.837838
123 ACE ARG THR PRO SEP LEU PRO THR PIP 0.433333 0.802632
124 SER THR GLY GLY VAL M3L LYS PRO HIS ARG 0.432584 0.815789
125 THR PRO THR ARG ASP VAL ALA THR SER PRO 0.432432 0.925373
126 LEU PRO PHE ASP LYS THR THR ILE MET 0.43125 0.791667
127 LYS VAL PRO ARG ASN GLN ASP TRP LEU 0.431034 0.833333
128 SER ARG ASP HIS SER ARG THR PRO MET 0.430303 0.837838
129 GLU VAL ALA PRO PRO GLU TYR HIS ARG LYS 0.430168 0.797297
130 ARG PRO GLY ASN PHE LEU GLN SER ARG LEU 0.426035 0.884058
131 ARG ARG ALA SEP ALA PRO LEU PRO 0.423841 0.808219
132 PRO ARG ARG PRO VAL ILE MET ARG ARG 0.423841 0.8
133 LEU PRO SER PHE GLU THR ALA LEU 0.423841 0.823529
134 LYS PRO PHE PTR VAL ASN VAL NH2 0.423077 0.683544
135 ILE ARG ALA ALA PRO PRO PRO LEU PHE 0.423077 0.84058
136 ALA ILE MET PRO ALA ARG PHE TYR PRO LYS 0.422857 0.776316
137 ARG THR TYR SEP GLY PRO MET ASN LYS VAL 0.422222 0.768293
138 ALA ASN SER ARG HIS PRO THR SER ILE ILE 0.422078 0.885714
139 LYS LEU VAL GLN LEU LEU THR THR THR 0.421875 0.676923
140 LEU PRO GLU THR GLY 0.421875 0.875
141 PRO ALA ALA LYS ARG VAL LYS LEU ASP 0.421488 0.68254
142 LYS GLY PRO PRO LEU PRO ARG PRO ARG VAL 0.42029 0.861538
143 LYS THR LYS LEU LEU 0.420168 0.714286
144 VAL VAL ARG PRO GLY SER LEU ASP LEU PRO 0.41875 0.925373
145 GLU GLU PRO THR VAL ILE LYS LYS TYR 0.41875 0.814286
146 ARG PHE PRO LEU THR PHE GLY TRP 0.418605 0.887324
147 ARG ARG ARG GLU THR GLN VAL 0.417323 0.753846
148 VAL PRO LEU THR GLU ASP ALA GLU LEU 0.416667 0.846154
149 DTY ILE ARG LEU LPD 0.416667 0.84058
150 TYR LEU GLU PRO GLY PRO VAL THR VAL 0.416667 0.814286
151 ARG SEP PRO VAL PHE SER 0.416667 0.794521
152 ALA ASN SER ARG TRP PRO THR SER FAK ILE 0.416667 0.794872
153 ALA ARG LYS ILE ASP ASN LEU ASP 0.415493 0.705882
154 LEU PRO PHE ASP LYS SER THR ILE MET 0.413174 0.780822
155 ALA PRO PRO PRO ARG PRO PRO LYS PRO 0.413043 0.787879
156 ALA ASN SER ARG TRP PRO THR SER 2KK ILE 0.413043 0.78481
157 GLU PRO GLY GLY SER ARG 0.413043 0.892308
158 SER SER TYR ARG ARG PRO VAL GLY ILE 0.4125 0.861111
159 THR ARG ARG GLU THR GLN LEU 0.412214 0.769231
160 ALA THR ALY ALA ALA ARG ALY SER ALA PRO 0.412162 0.895522
161 ALA ARG THR M3L GLN THR ALA ARG 0.411765 0.760563
162 GLU ALA GLN THR ARG LEU 0.411765 0.765625
163 DPN PRO ARG 0.410853 0.8
164 LEU ASP PRO ARG 0.410448 0.90625
165 ARG TYR PRO LEU THR PHE GLY TRP 0.410112 0.863014
166 PHE ASN ARG PRO VAL 0.409722 0.865672
167 LYS PRO ILE VAL GLN TYR ASP ASN PHE 0.409639 0.756757
168 ACE ALA ARG THR LYS GLN 0.409449 0.761905
169 SER SER ARG LYS GLU TYR TYR ALA 0.408759 0.661972
170 LYS PRO HIS SER ASP 0.408451 0.757143
171 ASP VAL GLN THR GLY ARG ARG PRO TYR GLU 0.407186 0.885714
172 LYS PRO PHE PTR VAL ASN VAL GLU PHE 0.407186 0.696203
173 ASN LEU VAL PRO MET VAL ALA ALA VAL 0.406897 0.753623
174 ACE CSO ARG ALA THR LYS MET LEU 0.406897 0.671053
175 ASN LEU VAL PRO MET VAL ALA VAL VAL 0.406897 0.753623
176 ALA ASN SER ARG TRP PRO THR SER 2KP ILE 0.406417 0.78481
177 LYS ARG ARG LYS SEP VAL 0.40625 0.676056
178 LEU LEU PHE GLY LYS PRO VAL TYR VAL 0.40625 0.726027
179 VAL ORN LEU DPN PRO VAL ORN LEU DPN PRO 0.405405 0.724638
180 DPN PRO DAR CYS NH2 0.404412 0.787879
181 HIS LYS LEU VAL GLN LEU LEU THR THR THR 0.402778 0.73913
182 ALA ARG THR GLU LEU TYR ARG SER LEU 0.402685 0.71831
183 MET SER LEU PRO GLY ARG TRP LYS PRO LYS 0.402174 0.815789
184 LEU LYS THR LYS LEU LEU 0.401639 0.714286
185 LEU GLU LYS ALA ARG GLY SER THR TYR 0.401235 0.746479
186 GLU LEU PRO PRO VAL LYS ILE HIS CYS 0.401163 0.746479
187 ASN ARG LEU MET LEU THR GLY 0.4 0.7
188 ALA ARG THR ALA ALA THR ALA ARG LYS SER 0.4 0.71875
189 SER LEU LYS LEU MET THR THR VAL 0.4 0.637681
190 ACE SER LEU ARG PRO ALA PRO LPD 0.4 0.910448
191 PRO SER ARG VAL 0.4 0.84375
192 ARG ASP ARG ALA ALA LYS LEU 0.4 0.730159
193 VAL LEU ARG ASP ASP LEU LEU GLU ALA 0.4 0.681818
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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