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 (4)
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)....
4 6KU8 - AG7 C31 H41 F N4 O7 CCOC(=O)CC....
Polypharmacology
Similar Ligands (2D)
Ligand no: 1; Ligand: LYS PRO VAL LEU ARG THR ALA; Similar ligands found: 189
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 5JP PRO LYS ARG ILE ALA 0.595238 0.880597
6 GLY LEU LEU GLY SER PRO VAL ARG ALA 0.590909 0.923077
7 ALA MET ALA PRO ARG THR LEU LEU LEU 0.586466 0.926471
8 LYS ALA PRO ARG ALY GLN LEU ALA THR LYS 0.58042 0.954545
9 ARG PRO LYS PRO LEU VAL ASP PRO 0.568 0.861538
10 GLY LEU LEU GLY SEP PRO VAL ARG ALA 0.553191 0.819444
11 3BY PRO LYS ARG ILE ALA 0.540741 0.814286
12 PRO PRO LYS ARG ILE ALA 0.540741 0.876923
13 ARG PRO MET THR PHE LYS GLY ALA LEU 0.534591 0.887324
14 GLY GLU ARG THR ILE PRO ILE THR ARG GLU 0.532374 0.939394
15 ARG PRO MET THR TYR LYS GLY ALA LEU 0.53125 0.851351
16 ARG PRO ARG PRO ASP ASP LEU GLU ILE 0.528571 0.880597
17 ALA PHE ARG ILE PRO LEU THR ARG 0.527397 0.940298
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 ARG GLN PRO ALA LYS ALA PRO LEU LEU 0.51049 0.865672
25 VAL MET ALA PRO ARG THR LEU PHE LEU 0.509804 0.9
26 LYS LEU THR PRO LEU CYS VAL THR LEU 0.507353 0.876923
27 ASN ARG PRO ILE LEU SER LEU 0.50365 0.897059
28 SER ALA PRO ASP THR ARG PRO ALA 0.503597 0.897059
29 ALA ASN SER ARG VAL PRO THR SER ILE ILE 0.503597 0.939394
30 VAL PRO LEU ARG PRO MET THR TYR 0.503311 0.863014
31 LEU PRO PHE GLU ARG ALA THR VAL MET 0.503145 0.9
32 GLN VAL PRO LEU ARG PRO MET THR TYR LYS 0.497006 0.851351
33 TYR LEU GLU PRO ALA PRO VAL THR ALA 0.496504 0.788732
34 LYS PRO ILE VAL VAL LEU HIS GLY TYR 0.493671 0.753425
35 ALA LEU PRO HIS ALA ILE LEU ARG LEU 0.493421 0.852941
36 THR THR ALA PRO SER LEU SER GLY LYS 0.489362 0.850746
37 PRO LYS ARG PRO THR THR LEU ASN LEU PHE 0.487654 0.898551
38 ALA ASN SER ARG ALY PRO THR SER ILE ILE 0.487013 0.885714
39 ARG VAL ALA SER PRO THR SER GLY VAL 0.482269 0.924242
40 ASN LEU VAL PRO VAL VAL ALA THR VAL 0.481481 0.833333
41 DPN PRO DAR DTH NH2 0.480916 0.892308
42 PRO SER ILE ASP ARG SER THR LYS PRO 0.480263 0.911765
43 TYR LEU ALA PRO GLY PRO VAL THR ALA 0.479167 0.802817
44 GLU LEU PRO LEU VAL LYS ILE 0.478261 0.8
45 ARG LEU GLN ARG ARG ARG GLU THR GLN VAL 0.476923 0.769231
46 THR PRO ARG VAL THR GLY GLY GLY ALA MET 0.47651 0.9
47 ASN PRO ARG ALA MET GLN ALA LEU LEU 0.475862 0.869565
48 VAL MET ALA PRO ARG ALA LEU LEU LEU 0.475177 0.852941
49 ASP ARG VAL GLU LEU ASN ALA PRO ARG GLN 0.472222 0.909091
50 LEU PRO PHE ASP ARG THR THR ILE MET 0.471698 0.875
51 PHE PRO THR LYS ASP VAL ALA LEU 0.470199 0.850746
52 ARG PRO PRO ILE PHE ILE ARG ARG LEU 0.470199 0.852941
53 GLY ARG PRO ARG THR THR SER PHE ALA GLU 0.468354 0.897059
54 ILE LEU LYS GLU PRO VAL HIS GLY VAL 0.467949 0.768116
55 ILE SER PRO ARG THR LEU ASP ALA TRP 0.467836 0.863014
56 ALA ARG THR M3L GLN THR ALA ALA LYS ALA 0.467153 0.760563
57 THR PRO ARG ARG SER MLZ SER ALA 0.466667 0.884058
58 LEU PRO PRO VAL VAL ALA LYS GLU ILE 0.465753 0.776119
59 ASN LEU VAL PRO GLN VAL ALA THR VAL 0.464789 0.833333
60 LYS PRO LYS 0.464286 0.746032
61 TYR LEU GLU PRO GLY PRO VAL THR ALA 0.463576 0.814286
62 ASN LEU VAL PRO THR VAL ALA THR VAL 0.463235 0.833333
63 SER SER GLY LYS VAL PRO LEU SER 0.463235 0.848485
64 LEU SER SER PRO VAL THR LYS SER PHE 0.463087 0.835821
65 LEU PRO LYS MYK THR GLY GLY 0.463087 0.835821
66 ARG LEU TYR GLN ASN PRO THR THR TYR ILE 0.462963 0.837838
67 ASP LEU THR ARG PRO 0.462121 0.953846
68 LEU PRO PHE GLU ARG ALA THR ILE MET 0.460606 0.887324
69 ACE SER LEU ARG PRO ALA PRO LPD 0.460432 0.910448
70 MET ABA LEU ARG MET THR ALA VAL MET 0.460432 0.735294
71 PRO PRO LYS LYS LYS ARG LYS VAL 0.459259 0.859375
72 ARG ARG ARG GLU ARG SER PRO THR ARG 0.458333 0.909091
73 PRO VAL LYS ARG ARG LEU ASP LEU GLU 0.458333 0.815385
74 ILE PRO LEU THR GLU GLU ALA GLU LEU 0.456522 0.861538
75 PTR LEU ARG VAL ALA 0.455224 0.626667
76 THR LYS PRO ARG 0.454545 0.84127
77 ALA ASN SER ARG LEU PRO THR SER ILE ILE 0.454545 0.939394
78 TYR LEU LYS GLU PRO VAL HIS GLY VAL 0.453988 0.763889
79 ACE GLN GLU ARG GLU VAL PRO CYS 0.453237 0.863636
80 ARG THR PHE SER PRO THR TYR GLY LEU 0.45283 0.849315
81 ALA ASN SER ARG PHE PRO THR SER ILE ILE 0.45283 0.871429
82 SER SER GLY LYS VAL PRO LEU 0.451852 0.861538
83 ALA ALA LEU THR ARG ALA 0.451613 0.761905
84 ARG THR PRO SEP LEU PRO THR 49F 0.451389 0.847222
85 ARG THR PRO SEP LEU PRO THR 0.451389 0.847222
86 MET CYS LEU ARG MET THR ALA VAL MET 0.450704 0.735294
87 ALA ARG LYS LEU ASP 0.45 0.734375
88 ASN LEU VAL PRO SER VAL ALA THR VAL 0.45 0.835821
89 ALA ALA ARG KCR SER ALA PRO ALA 0.449664 0.909091
90 ARG ILE ILE PRO ARG HIS LEU GLN LEU 0.449367 0.828571
91 ASN LEU VAL PRO MET VAL ALA THR VAL 0.448276 0.785714
92 HIS HIS ALA SER PRO ARG LYS 0.448052 0.826087
93 LEU PRO PRO GLU GLU ARG LEU ILE 0.447552 0.878788
94 ARG VAL ALA SEP PRO THR SER GLY VAL 0.447368 0.847222
95 LEU PRO PHE GLU LYS SER THR VAL MET 0.446541 0.791667
96 LYS ARG ARG ARG HIS PRO SER 0.445205 0.797101
97 ARG ARG LEU PRO ILE PHE SER ARG LEU 0.445161 0.911765
98 ILE PRO ALA TYR GLY VAL LEU THR ILE 0.444444 0.8
99 SER HIS PRO ARG PRO ILE ARG VAL 0.444444 0.885714
100 LYS ARG ARG ARG HIS PRO SER GLY 0.442953 0.814286
101 LEU GLN ARG VAL LEU SEP ALA PRO PHE 0.441558 0.797297
102 MET CYS LEU ARG NLE THR ALA VAL MET 0.441379 0.724638
103 LYS LEU TYR GLN ASN PRO THR THR TYR ILE 0.440994 0.756757
104 ALA ARG THR LYS GLN THR ALA ARG LYS 0.440298 0.738462
105 ALA ASN SER ARG TYR PRO THR SER ILE ILE 0.43949 0.835616
106 LYS GLY PRO PRO ALA ALA LEU THR LEU 0.439189 0.863636
107 ALA ASN SER ARG TRP PRO THR THR ARG LEU 0.438272 0.863014
108 ARG PRO PRO LYS PRO ARG PRO ARG 0.437956 0.784615
109 GLN PRO PRO VAL PRO PRO GLN ARG PRO MET 0.437086 0.828571
110 DPN PRO DAR ILE NH2 0.437037 0.818182
111 ALA ARG THR LYS GLN THR ALA ARG 0.436508 0.75
112 ARG ILE PRO SER TYR ARG TYR ARG TYR 0.436242 0.835616
113 LYS ALA ARG VAL LEU ALA GLU ALA MET SER 0.435714 0.647059
114 ALA PRO ASP THR ARG PRO ALA PRO 0.435714 0.910448
115 ALA ASN SER ARG TRP PRO THR SER ALY ILE 0.434286 0.815789
116 ILE ARG TYR PRO LYS THR PHE GLY TRP 0.434066 0.837838
117 ACE ARG THR PRO SEP LEU PRO THR PIP 0.433333 0.802632
118 THR THR ALA PRO PHE LEU SER GLY LYS 0.433121 0.826087
119 SER THR GLY GLY VAL M3L LYS PRO HIS ARG 0.432584 0.815789
120 THR PRO THR ARG ASP VAL ALA THR SER PRO 0.432432 0.925373
121 GLU PRO VAL GLU THR THR ASP TYR 0.431507 0.771429
122 LEU PRO PHE ASP LYS THR THR ILE MET 0.43125 0.791667
123 LYS VAL PRO ARG ASN GLN ASP TRP LEU 0.431034 0.833333
124 SER ARG ASP HIS SER ARG THR PRO MET 0.430303 0.837838
125 ACE ALA ALA ARG LBZ SER ALA PRO ALA 0.428571 0.895522
126 LEU PRO PHE GLU LEU ARG GLY HIS LEU VAL 0.428571 0.828571
127 ARG PRO GLY ASN PHE LEU GLN SER ARG LEU 0.426035 0.884058
128 LEU PRO SER PHE GLU THR ALA LEU 0.423841 0.823529
129 PRO ARG ARG PRO VAL ILE MET ARG ARG 0.423841 0.8
130 ARG ARG ALA SEP ALA PRO LEU PRO 0.423841 0.808219
131 LYS PRO PHE PTR VAL ASN VAL NH2 0.423077 0.683544
132 ILE ARG ALA ALA PRO PRO PRO LEU PHE 0.423077 0.84058
133 ALA ILE MET PRO ALA ARG PHE TYR PRO LYS 0.422857 0.776316
134 ARG THR TYR SEP GLY PRO MET ASN LYS VAL 0.422222 0.768293
135 LYS LEU VAL GLN LEU LEU THR THR THR 0.421875 0.676923
136 ASN ARG LEU LEU LEU THR GLY 0.420635 0.742424
137 LYS GLY PRO PRO LEU PRO ARG PRO ARG VAL 0.42029 0.861538
138 LYS THR LYS LEU LEU 0.420168 0.714286
139 PHE ALA GLY LEU ARG GLN ALA VAL THR GLN 0.419118 0.78125
140 ARG SER LEU SEP ALA PRO GLY ASN 0.418919 0.821918
141 GLU GLU PRO THR VAL ILE LYS LYS TYR 0.41875 0.814286
142 VAL VAL ARG PRO GLY SER LEU ASP LEU PRO 0.41875 0.925373
143 ARG PHE PRO LEU THR PHE GLY TRP 0.418605 0.887324
144 LYS VAL ALA PRO PRO ILE PRO HIS ARG 0.418182 0.8
145 ARG ARG ARG GLU THR GLN VAL 0.417323 0.753846
146 ALA ASN SER ARG TRP PRO THR SER FAK ILE 0.416667 0.794872
147 ARG SEP PRO VAL PHE SER 0.416667 0.794521
148 TYR LEU GLU PRO GLY PRO VAL THR VAL 0.416667 0.814286
149 VAL PRO LEU THR GLU ASP ALA GLU LEU 0.416667 0.846154
150 DTY ILE ARG LEU LPD 0.416667 0.84058
151 ALA ARG LYS ILE ASP ASN LEU ASP 0.415493 0.705882
152 LYS ARG LYS SER ARG TRP ASP GLU THR PRO 0.414773 0.847222
153 ASN ARG PRO VAL TYR ILE PRO ARG PRO PRO 0.414013 0.842857
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 GLU PRO GLY GLY SER ARG 0.413043 0.892308
157 ALA ASN SER ARG TRP PRO THR SER 2KK ILE 0.413043 0.78481
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 GLU ALA GLN THR ARG LEU 0.411765 0.765625
162 ALA ARG THR M3L GLN THR ALA ARG 0.411765 0.760563
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 LYS PRO HIS SER ASP 0.408451 0.757143
170 LYS PRO PHE PTR VAL ASN VAL GLU PHE 0.407186 0.696203
171 ACE CSO ARG ALA THR LYS MET LEU 0.406897 0.671053
172 ASN LEU VAL PRO MET VAL ALA VAL VAL 0.406897 0.753623
173 ASN LEU VAL PRO MET VAL ALA ALA VAL 0.406897 0.753623
174 ALA ASN SER ARG TRP PRO THR SER 2KP ILE 0.406417 0.78481
175 LEU LEU PHE GLY LYS PRO VAL TYR VAL 0.40625 0.726027
176 LYS ARG ARG LYS SEP VAL 0.40625 0.676056
177 VAL ORN LEU DPN PRO VAL ORN LEU DPN PRO 0.405405 0.724638
178 DPN PRO DAR CYS NH2 0.404412 0.787879
179 HIS LYS LEU VAL GLN LEU LEU THR THR THR 0.402778 0.73913
180 ALA ARG THR GLU LEU TYR ARG SER LEU 0.402685 0.71831
181 MET SER LEU PRO GLY ARG TRP LYS PRO LYS 0.402174 0.815789
182 LEU LYS THR LYS LEU LEU 0.401639 0.714286
183 LEU GLU LYS ALA ARG GLY SER THR TYR 0.401235 0.746479
184 GLU LEU PRO PRO VAL LYS ILE HIS CYS 0.401163 0.746479
185 ASN ARG LEU MET LEU THR GLY 0.4 0.7
186 PRO SER ARG VAL 0.4 0.84375
187 VAL LEU ARG ASP ASP LEU LEU GLU ALA 0.4 0.681818
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
Similar Ligands (3D)
Ligand no: 1; Ligand: LYS PRO VAL LEU ARG THR ALA; Similar ligands found: 0
No: Ligand Similarity coefficient
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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