Receptor
PDB id Resolution Class Description Source Keywords
3MMG 1.7 Å NON-ENZYME: TRANSCRIPT_TRANSLATE CRYSTAL STRUCTURE OF TOBACCO VEIN MOTTLING VIRUS PROTEASE TOBACCO VEIN MOTTLING VIRUS 3C-TYPE PROTEASE TEV TVMV VIRAL PROTEIN HYDROLASE
Ref.: STRUCTURAL DETERMINANTS OF TOBACCO VEIN MOTTLING VI PROTEASE SUBSTRATE SPECIFICITY. PROTEIN SCI. V. 19 2240 2010
Ligand
Ligand Chain:Residue Validity Ligand Warnings Binding Data NGL Viewer Molecular Weight (Da) Formula SMILES
FMT A:242;
Invalid;
none;
submit data
46.025 C H2 O2 C(=O)...
GLU THR VAL ARG PHE GLN SER ASP C:2;
D:2;
Valid;
Valid;
none;
none;
submit data
850.952 n/a O=C(N...
View in 3D viewer
90% Homology Family
Leader
PDB id Resolution Class Description Source Keywords
3MMG 1.7 Å NON-ENZYME: TRANSCRIPT_TRANSLATE CRYSTAL STRUCTURE OF TOBACCO VEIN MOTTLING VIRUS PROTEASE TOBACCO VEIN MOTTLING VIRUS 3C-TYPE PROTEASE TEV TVMV VIRAL PROTEIN HYDROLASE
Ref.: STRUCTURAL DETERMINANTS OF TOBACCO VEIN MOTTLING VI PROTEASE SUBSTRATE SPECIFICITY. PROTEIN SCI. V. 19 2240 2010
Members (1)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 309 families.
1 3MMG - GLU THR VAL ARG PHE GLN SER ASP n/a n/a
70% Homology Family (1)
No: PDB id Binding Data Representative ligand Formula Smiles
The Class containing this family consists of a total of 263 families.
1 3MMG - GLU THR VAL ARG PHE GLN SER ASP 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 221 families.
1 1LVB - THR GLU ASN LEU TYR PHE GLN SER GLY THR n/a n/a
2 1LVM - GLU ALA THR GLN LEU MET ASN n/a n/a
3 3MMG - GLU THR VAL ARG PHE GLN SER ASP n/a n/a
Polypharmacology
Similar Ligands
Ligand no: 1; Ligand: GLU THR VAL ARG PHE GLN SER ASP; Similar ligands found: 195
No: Ligand ECFP6 Tc MDL keys Tc
1 GLU THR VAL ARG PHE GLN SER ASP 1 1
2 GLY ARG PHE GLN VAL THR 0.593496 0.907407
3 VAL ALA PHE ARG SER 0.571429 0.90566
4 GLU GLU ASN LEU LEU ASP PHE VAL ARG PHE 0.565217 0.830508
5 GLN THR ALA ARG M3L SER 0.563492 0.742424
6 ARG ILE PHE SER 0.563025 0.854545
7 ALA THR ARG ASN PHE SER GLY 0.538462 0.910714
8 ALA THR VAL ARG THR TYR SER CYS 0.534351 0.896552
9 ASP ALA GLU PHE ARG HIS ASP 0.53125 0.886792
10 GLU GLN TYR LYS PHE TYR SER VAL 0.530303 0.783333
11 GLU ARG GLU SEP GLU PHE ASP ILE GLU ASP 0.527397 0.765625
12 ALA GLN ASP ILE TYR ARG ALA SER TYR 0.520548 0.852459
13 GLU ALA GLN THR ARG LEU 0.519685 0.907407
14 GLY ASP GLU VAL LYS VAL PHE ARG 0.517986 0.857143
15 ASP ALA GLU PHE ARG HIS ASP SER 0.517986 0.741935
16 GLU GLU PHE GLY ARG ALA PHE SER PHE 0.517986 0.892857
17 THR PHE GLN ALA PSA LEU ARG GLU 0.516779 0.881356
18 ALA GLN PHE SER ALA SER ALA SER ARG 0.515625 0.944444
19 SER GLU ILE GLU PHE ALA ARG LEU 0.510791 0.945455
20 ALA ARG THR GLU LEU TYR ARG SER LEU 0.510791 0.898305
21 SER SER ILE GLU PHE ALA ARG LEU 0.510638 0.928571
22 ARG ARG ARG GLU THR GLN VAL 0.508333 0.890909
23 GLU VAL TYR GLU SER 0.508333 0.767857
24 SER LEU ARG PHE LEU TYR GLU GLY 0.507246 0.883333
25 GLU THR PHE TYR VAL ASP GLY 0.503817 0.75
26 LEU PRO PHE GLU ARG ALA THR VAL MET 0.5 0.732394
27 ARG LEU GLN ARG ARG ARG GLU THR GLN VAL 0.496124 0.875
28 GLU GLU TYR LEU GLN ALA PHE THR TYR 0.485915 0.728814
29 SER ASP TYR GLN ARG LEU 0.484615 0.877193
30 SER SER LEU GLU ASN PHE ARG ALA TYR VAL 0.483871 0.868852
31 SER GLU ASP GLU PHE TYR ASP ALA LEU SER 0.482269 0.75
32 GLY ALA GLN THR PHE TYR VAL ASP GLY ALA 0.481752 0.75
33 ACE ALA ARG THR GLU VAL TYR NH2 0.481481 0.928571
34 ARG SEP PRO VAL PHE SER 0.48 0.680556
35 ACE GLN THR ALA ARG PRK SER THR 0.477612 0.827586
36 LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE 0.477124 0.819672
37 THR ARG ARG GLU THR GLN LEU 0.47619 0.875
38 ARG PRO GLY ASN PHE LEU GLN SER ARG LEU 0.47561 0.73913
39 LYS ILE LEU HIS ARG LEU LEU GLN ASP SER 0.474359 0.78125
40 ASP PHE M3L THR ASP 0.472868 0.681818
41 TYR GLU LEU ASP GLU LYS PHE ASP ARG LEU 0.469388 0.806452
42 ASP ASN ARG LEU GLY LEU VAL TYR GLN PHE 0.46875 0.661017
43 GLY ASN PHE LEU GLN SER ARG 0.467626 0.912281
44 PHQ LEU VAL ARG TYR 0.467153 0.790323
45 PHE ARG TYR LEU GLY 0.466165 0.816667
46 ALA PHE THR SER 0.464912 0.754717
47 VAL GLN GLN GLU SER SER PHE VAL MET 0.462687 0.762712
48 ALA ILE ARG SER 0.461538 0.8
49 ASN ALA LEU LEU ARG TYR LEU LEU ASP 0.456522 0.864407
50 GLY ILE LEU GLU PHE VAL PHE THR LEU 0.456522 0.789474
51 LEU GLU PHE GLN GLY 0.456 0.745455
52 ARG PRO GLY ASN PHE LEU GLN ASN ARG PRO 0.453901 0.839286
53 ACE GLN THR ALA ARG KCR SER THR 0.453237 0.842105
54 ARG ILE PRO SER TYR ARG TYR ARG TYR 0.452703 0.675676
55 GLU VAL ALA PRO PRO GLU TYR HIS ARG LYS 0.451977 0.662162
56 ARG GLY TYR VAL TYR GLN GLY LEU 0.451389 0.816667
57 PCA PHE ARG HIS ASP SER GLY TYR GLU VAL 0.450331 0.75
58 ARG PRO GLY ASN PHE PHE GLN SER ARG PRO 0.449664 0.75
59 ALA ARG THR M3L GLN THR ALA 2MR LYS 0.449612 0.727273
60 ALA ARG THR M3L GLN THR ALA 0.449612 0.727273
61 GLU ASP GLU ASP PHE GLU ILE LEU SER LEU 0.448276 0.789474
62 SER SER ARG LYS GLU TYR TYR ALA 0.447761 0.8
63 ALA ARG THR LYS GLN THR ALA ARG LYS 0.447761 0.839286
64 SAC ARG GLY THR GLN THR GLU 0.447761 0.875
65 LEU TYR LEU VAL CYS GLY GLU ARG VAL 0.447368 0.847458
66 GLY ALA ALA ARG ALA GLU VAL TYR LEU ARG 0.447368 0.816667
67 GLY ARG PRO ARG THR THR SER PHE ALA GLU 0.447205 0.776119
68 ALA ARG THR MLY GLN THR ALA ARG LYS SER 0.447154 0.87037
69 ASN PHE ASP ASN PRO VAL TYR ARG LYS THR 0.447059 0.712329
70 GLN THR ALA ARG M3L SER THR GLY 0.446809 0.742424
71 ALA ARG THR M3L GLN THR ALA ARG LYS SER 0.446154 0.727273
72 ALA ARG THR M3L GLN THR ALA ARG LYS 0.446154 0.727273
73 ALA ARG M3L SER 0.445378 0.681818
74 ALA PHE ARG ILE PRO LEU THR ARG 0.445161 0.73913
75 LEU TYR LEU VAL CYS GLY GLU ARG GLY 0.443709 0.847458
76 GLU ILE ILE ASN PHE GLU LYS LEU 0.443662 0.741379
77 ALA ASN SER ARG VAL GLN ASP SER ILE ILE 0.442857 0.844828
78 ALA ARG THR MLY GLN THR ALA 0.442748 0.75
79 ALA ARG THR MLY GLN THR ALA ARG LYS TYR 0.442748 0.75
80 SER LEU PHE ASN THR VAL ALA THR LEU TYR 0.442177 0.688525
81 ALA ARG THR MLY GLN THR ALA ARG TYR 0.441379 0.776119
82 LEU PRO PHE GLU ARG ALA THR ILE MET 0.440476 0.722222
83 ALA ARG THR MLY GLN THR ALA ARG LYS 0.439394 0.761905
84 ALA ARG THR ALY GLN THR ALA 0.438462 0.810345
85 PHE LEU ARG GLY ARG ALA TYR VAL LEU 0.437909 0.803279
86 THR LYS ASN TYR LYS GLN THR SER VAL 0.4375 0.783333
87 ALA ASN SER ARG TRP GLN ASP THR ARG LEU 0.4375 0.815385
88 ILE GLN GLN SER ILE GLU ARG ILE 0.43609 0.857143
89 ARG ARG ARG GLU ARG SER PRO THR ARG 0.435374 0.731343
90 ALA ARG THR MLZ GLN THR ALA ARG LYS 0.434783 0.770492
91 GLY VAL TYR ASP GLY ARG GLU HIS THR VAL 0.434783 0.787879
92 GLU LEU ARG ARG LYS MET MET TYR MET 0.434483 0.765625
93 GLY ALA GLU THR PHE TYR VAL ASP GLY ALA 0.434483 0.737705
94 ALA ARG THR MLY GLN THR ALA ARG MLY SER 0.434109 0.761905
95 ARG VAL ALA GLN LEU GLU GLN VAL TYR ILE 0.433333 0.844828
96 ARG ARG ILE TYR ASP LEU ILE GLU LEU 0.433333 0.833333
97 ALA ARG THR LYS GLN THR ALA ARG 0.433071 0.854545
98 THR LYS ASN TYR LYS GLN PHE SER VAL 0.432624 0.770492
99 ARG GLN PHE GLY PRO ASP PHE PRO THR ILE 0.431953 0.708333
100 ARG GLY PHE ALA LEU M3L SER THR HIS GLY 0.431138 0.693333
101 ACE ARG GLU PTR VAL ASN VAL 0.430556 0.757576
102 ALA ARG THR MLZ GLN THR ALA ARG LYS TYR 0.428571 0.783333
103 ARG ARG ARG VAL ARG 00S 0.425197 0.77193
104 ARG LEU TYR GLN ASN PRO THR THR TYR ILE 0.42515 0.68
105 LEU GLU LYS ALA ARG GLY SER THR TYR 0.425 0.868852
106 GLU LEU ARG SER ARG TYR TRP ALA ILE 0.424242 0.779412
107 LEU PRO PHE ASP ARG THR THR ILE MET 0.424242 0.712329
108 ARG ARG LEU PRO ILE PHE SER ARG LEU 0.424051 0.73913
109 SER ARG TYR TRP ALA ILE ARG THR ARG 0.423313 0.75
110 ARG THR PHE SER PRO THR TYR GLY LEU 0.423313 0.736111
111 ARG GLY PRO GLY ARG ALA PHE VAL THR ILE 0.422619 0.73913
112 PRO ALA THR ILE MET MET GLN ARG GLY ASN 0.422222 0.770492
113 GLU ASN PRO THR TYR LYS PHE PHE GLU GLN 0.422222 0.733333
114 THR TYR LYS PHE PHE GLU GLN 0.422222 0.733333
115 ACE GLU ALA GLN THR ARG LEU 0.422222 0.890909
116 GLU VAL ASN 1OL ALA GLU PHE 0.421769 0.75
117 GLU LEU ASP 1OL VAL GLU PHE 0.42069 0.745455
118 ALA GLU THR PHE TYR VAL ASP GLY 0.420635 0.655172
119 TYR HIS SEP VAL VAL ARG TYR ALA 0.420382 0.684932
120 PHE ALA GLY LEU ARG GLN ALA VAL THR GLN 0.42029 0.890909
121 GLU LEU LYS ARG LYS MET ILE TYR MET 0.419355 0.765625
122 GLU ASN GLN LYS GLU TYR PHE PHE 0.419118 0.688525
123 ALA ARG THR M3L GLN THR ALA ARG 0.419118 0.742424
124 SER LEU PHE ASN THR ILE ALA VAL LEU 0.418919 0.754386
125 ARG ARG ARG TRP ARG ARG LEU THR VAL 0.418919 0.796875
126 HIS LYS ILE LEU HIS ARG LEU LEU GLN GLU 0.41875 0.707692
127 SER TRP PHE GLN THR ASP LEU 0.418301 0.703125
128 GLU LEU LYS TPO GLU ARG TYR 0.418301 0.761194
129 CYS THR PHE LYS THR LYS THR ASN 0.41791 0.775862
130 SER ARG ILE ARG ILE ARG GLY TYR VAL ARG 0.417808 0.868852
131 LYS MET ASN THR GLN PHE THR ALA VAL 0.417219 0.741935
132 LEU PRO PHE GLU LYS SER THR VAL MET 0.417178 0.652778
133 CYS VAL ASN GLY SER CYS PHE THR VAL 0.416667 0.789474
134 THR ALA ARG M3L SER THR 0.416667 0.681818
135 PHE ARG SER LYS GLY GLU GLU LEU PHE THR 0.416667 0.857143
136 ALA ARG THR M3L GLN THR ALA DA2 LYS 0.416667 0.727273
137 LEU ASP GLU GLU THR GLY GLU PHE LEU 0.415493 0.821429
138 SER LEU PHE ASN THR VAL ALA THR LEU 0.415493 0.767857
139 ALA ARG THR MLY GLN 0.415385 0.777778
140 GLU ARG GLY SER GLY ARG 0.414062 0.821429
141 THR TYR PHE ALA VAL LEU MET VAL SER 0.413333 0.68254
142 ASP VAL GLN THR GLY ARG ARG PRO TYR GLU 0.413174 0.742857
143 GLU THR HPH TYR VAL ASP 0.412587 0.709677
144 ARG PRO GLY ASN PHE PHE GLN ASN ARG PRO 0.412214 0.65
145 SER PHE PHE GLU ASP ASN PHE VAL PRO GLU 0.412162 0.657143
146 ALA ILE PHE GLN SER SER MET THR LYS 0.412162 0.741935
147 GLN TYR PHE MET TPO GLU PTR VAL ALA 0.412121 0.616438
148 ARG PRO GLY ASN PHE LEU GLN SER ARG PRO 0.411765 0.71831
149 THR GLU ASN LEU TYR PHE GLN SER GLY THR 0.411765 0.758065
150 LEU PRO SER PHE GLU THR ALA LEU 0.411765 0.701493
151 ALA ASN SER ARG TRP GLN THR SER ILE ILE 0.411043 0.8
152 SER ILE ILE ASN PHE GLU LYS LEU 0.410959 0.793103
153 ARG ARG LEU ILE PHE NH2 0.410448 0.785714
154 GLY ILE LEU GLY PHE VAL PHE THR LEU 0.409722 0.741379
155 ALA LYS PHE ARG HIS ASP 0.409722 0.730159
156 GLY ALA GLU VAL PHE TYR VAL ASP GLY ALA 0.409722 0.716667
157 TYR SER THR CYS TYR PHE ILE MET 0.409722 0.646154
158 ASN TYR THR PRO GLY PRO GLY THR ARG PHE 0.409357 0.69863
159 GLU ASN LEU TYR PHE GLN 0.408759 0.7
160 ARG ABA VAL ILE PHE ALA ASN ILE 0.408163 0.875
161 GLU ALY ARG 0.408 0.736842
162 ASP PHE GLU GLU ILE 0.408 0.690909
163 ARG TYR GLY PHE VAL ALA ASN PHE 0.407895 0.85
164 ARG PRO GLY ASN PHE LEU GLN SER SER PRO 0.407895 0.725806
165 GLN PHE LYS ASP ASN VAL ILE LEU LEU 0.407895 0.728814
166 ILE LEU ALA LYS PHE LEU HIS ARG LEU 0.407643 0.676923
167 ILE GLY PRO GLY ARG ALA PHE TYR THR ILE 0.406977 0.708333
168 GLY ARG PHE ALA ALA ALA ILE ALA LYS 0.406897 0.793103
169 ALA ASN SER ARG TRP GLN VAL THR ARG VAL 0.406667 0.84127
170 ARG VAL LEU PHE GLU ALA MET 0.406667 0.783333
171 ILE THR ASP GLN VAL PRO PHE SER VAL 0.40625 0.691176
172 VAL MET ALA PRO ARG THR LEU PHE LEU 0.406061 0.708333
173 ALA ASN SER ARG PHE PRO THR SER ILE ILE 0.406061 0.753623
174 PHE TYR ARG ALA LEU MET 0.405405 0.761905
175 ALA GLU THR PHE 0.404959 0.773585
176 GLU LEU ASN ARG LYS MET ILE TYR MET 0.404908 0.784615
177 THR ILE MET MET GLN ARG GLY 0.404412 0.786885
178 GLU VAL PTR GLU SER PRO 0.40411 0.626667
179 SER GLU LEU GLU ILE LYS ARG TYR 0.403974 0.883333
180 GLU PHE SER PRO 0.403101 0.646154
181 DPN PRO DAR DTH NH2 0.402878 0.738462
182 LYS ALA ARG VAL LEU ALA GLU ALA MET 0.402778 0.758621
183 ALA ARG THR M3L GLN THR ALA ALA LYS ALA 0.402778 0.742424
184 LYS ALA ARG VAL LEU ALA GLU ALA MET SER 0.402778 0.758621
185 THR PHE ALY SER ILE MET LYS 0.402597 0.698413
186 PRO LEU GLU PSA ARG LEU 0.402597 0.852459
187 ILE ARG LYS ILE LEU PHE LEU ASP GLY ILE 0.402516 0.813559
188 THR PHE LYS LYS THR ASN 0.401515 0.789474
189 GLU ARG GLY MET THR 0.401515 0.779661
190 PHE GLU ASP LEU ARG VAL LEU SER PHE 0.401316 0.912281
191 GLY TYR GLU ASN PRO THR TYR LYS PHE PHE 0.401198 0.60274
192 THR ASN GLU PHE TYR ALA 0.4 0.683333
193 HY1 CIR VAL ARG 00S 0.4 0.762712
194 ACE GLN THR ALA ARG BTK SER THR 0.4 0.79661
195 LYS VAL ILE THR PHE ILE ASP LEU 0.4 0.807018
Similar Binding Sites (Proteins are less than 50% similar to leader)
Pocket No.: 1; Query (leader) PDB : 3MMG; Ligand: GLU THR VAL ARG PHE GLN SER ASP; 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: 3mmg.bio3) has 28 residues
No: Leader PDB Ligand Sequence Similarity
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