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 308 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 266 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 220 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 (2D)
Ligand no: 1; Ligand: GLU THR VAL ARG PHE GLN SER ASP; Similar ligands found: 196
No: Ligand ECFP6 Tc MDL keys Tc
1 GLU THR VAL ARG PHE GLN SER ASP 1 1
2 VAL ALA PHE ARG SER 0.571429 0.90566
3 LEU ARG ASN GLN SER VAL PHE ASN PHE 0.567164 0.881356
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 ASP ALA GLU PHE ARG HIS ASP 0.53125 0.886792
9 GLU GLN TYR LYS PHE TYR SER VAL 0.530303 0.783333
10 GLU ARG GLU SEP GLU PHE ASP ILE GLU ASP 0.527397 0.765625
11 ALA GLN ASP ILE TYR ARG ALA SER TYR 0.520548 0.852459
12 GLU ALA GLN THR ARG LEU 0.519685 0.907407
13 ASP ALA GLU PHE ARG HIS ASP SER 0.517986 0.741935
14 GLY ASP GLU VAL LYS VAL PHE ARG 0.517986 0.857143
15 GLU GLU PHE GLY ARG ALA PHE SER PHE 0.517986 0.892857
16 THR PHE GLN ALA PSA LEU ARG GLU 0.516779 0.881356
17 PHE TYR ARG TYR GLY PHE VAL ALA ASN PHE 0.516393 0.758621
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 PHE GLU ASP LEU ARG VAL SER SER PHE 0.503497 0.912281
27 PHE GLU ASP LEU ARG VAL LEU SER PHE 0.503497 0.912281
28 ALA GLU THR PHE TYR VAL ASP GLY 0.5 0.711864
29 LEU PRO PHE GLU ARG ALA THR VAL MET 0.5 0.732394
30 ARG LEU GLN ARG ARG ARG GLU THR GLN VAL 0.496124 0.875
31 ARG ARG GLU VAL HIS THR TYR TYR 0.493243 0.787879
32 ARG LYS LYS ARG TYR THR VAL VAL GLY ASN 0.486301 0.836066
33 GLU GLU TYR LEU GLN ALA PHE THR TYR 0.485915 0.728814
34 SER SER LEU GLU ASN PHE ARG ALA TYR VAL 0.483871 0.868852
35 ACE ALA ARG THR GLU VAL TYR NH2 0.481481 0.928571
36 ARG SEP PRO VAL PHE SER 0.48 0.680556
37 ACE GLN THR ALA ARG PRK SER THR 0.477612 0.827586
38 LEU TYR LEU VAL CYS GLY GLU ARG GLY PHE 0.477124 0.819672
39 THR ARG ARG GLU THR GLN LEU 0.47619 0.875
40 ARG PRO GLY ASN PHE LEU GLN SER ARG LEU 0.47561 0.73913
41 LYS ILE LEU HIS ARG LEU LEU GLN ASP SER 0.474359 0.78125
42 ASP PHE M3L THR ASP 0.472868 0.681818
43 TYR GLU LEU ASP GLU LYS PHE ASP ARG LEU 0.469388 0.806452
44 GLY ASN PHE LEU GLN SER ARG 0.467626 0.912281
45 PHQ LEU VAL ARG TYR 0.467153 0.790323
46 PHE ARG TYR LEU GLY 0.466165 0.816667
47 ALA PHE THR SER 0.464912 0.754717
48 PHE GLU ASP LEU ARG LEU LEU SER PHE 0.464286 0.912281
49 VAL GLN GLN GLU SER SER PHE VAL MET 0.462687 0.762712
50 ALA ILE ARG SER 0.461538 0.8
51 GLY ALA GLN THR PHE TYR VAL ASP GLY ALA 0.460432 0.75
52 ALA ASN SER ARG TRP GLN VAL THR ARG VAL 0.459459 0.828125
53 HIS MET THR GLU VAL VAL ARG HIS CYS 0.457516 0.75
54 GLY ILE LEU GLU PHE VAL PHE THR LEU 0.456522 0.789474
55 ASN ALA LEU LEU ARG TYR LEU LEU ASP 0.456522 0.864407
56 HIS MET THR GLU VAL VAL ARG ARG CYS 0.456376 0.761194
57 LEU GLU PHE GLN GLY 0.456 0.745455
58 ALA VAL TYR ASP GLY ARG GLU HIS THR VAL 0.455696 0.787879
59 ARG PRO GLY ASN PHE LEU GLN ASN ARG PRO 0.453901 0.839286
60 ACE GLN THR ALA ARG KCR SER THR 0.453237 0.842105
61 ARG ILE PRO SER TYR ARG TYR ARG TYR 0.452703 0.675676
62 ARG GLY TYR VAL TYR GLN GLY LEU 0.451389 0.816667
63 ARG PRO GLY ASN PHE LEU GLN SER ARG PRO 0.450617 0.728571
64 SER ASP TYR GLN ARG LEU 0.450382 0.877193
65 PCA PHE ARG HIS ASP SER GLY TYR GLU VAL 0.450331 0.75
66 ARG PRO GLY ASN PHE PHE GLN SER ARG PRO 0.449664 0.75
67 ALA ARG THR M3L GLN THR ALA 2MR LYS 0.449612 0.727273
68 GLU ASP GLU ASP PHE GLU ILE LEU SER LEU 0.448276 0.789474
69 SAC ARG GLY THR GLN THR GLU 0.447761 0.875
70 ALA ARG THR LYS GLN THR ALA ARG LYS 0.447761 0.839286
71 GLY ALA ALA ARG ALA GLU VAL TYR LEU ARG 0.447368 0.816667
72 LEU TYR LEU VAL CYS GLY GLU ARG VAL 0.447368 0.847458
73 GLY ARG PRO ARG THR THR SER PHE ALA GLU 0.447205 0.776119
74 ALA ARG THR MLY GLN THR ALA ARG LYS SER 0.447154 0.87037
75 GLN THR ALA ARG M3L SER THR GLY 0.446809 0.742424
76 ALA ARG THR M3L GLN THR ALA ARG LYS SER 0.446154 0.727273
77 ALA ARG M3L SER 0.445378 0.681818
78 ALA PHE ARG ILE PRO LEU THR ARG 0.445161 0.73913
79 LEU TYR LEU VAL CYS GLY GLU ARG GLY 0.443709 0.847458
80 GLU ILE ILE ASN PHE GLU LYS LEU 0.443662 0.741379
81 SER GLY ILE PHE LEU GLU THR SER 0.443609 0.803571
82 ALA ARG THR MLY GLN THR ALA ARG LYS TYR 0.442748 0.75
83 SER LEU PHE ASN THR VAL ALA THR LEU TYR 0.442177 0.688525
84 LEU PRO PHE GLU ARG ALA THR ILE MET 0.440476 0.722222
85 ALA ARG THR MLY GLN THR ALA ARG LYS 0.439394 0.761905
86 ALA ARG THR ALY GLN THR ALA 0.438462 0.810345
87 PHE LEU ARG GLY ARG ALA TYR VAL LEU 0.437909 0.803279
88 ALA ASN SER ARG TRP GLN ASP THR ARG LEU 0.4375 0.815385
89 ILE GLN GLN SER ILE GLU ARG ILE 0.43609 0.857143
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 ASN CYS PHE SER LYS ARG ARG ALA ALA 0.434483 0.877193
94 ASP ARG VAL TYR ILE HIS PRO PHE 0.434211 0.757576
95 ALA ARG THR MLY GLN THR ALA ARG MLY SER 0.434109 0.761905
96 ARG ARG ILE TYR ASP LEU ILE GLU LEU 0.433333 0.833333
97 ARG VAL ALA GLN LEU GLU GLN VAL TYR ILE 0.433333 0.844828
98 ALA ARG THR LYS GLN THR ALA ARG 0.433071 0.854545
99 LYS ILE LEU HIS ARG LEU LEU GLN ASP 0.432258 0.734375
100 ARG GLN PHE GLY PRO ASP PHE PRO THR ILE 0.431953 0.708333
101 ARG GLY PHE ALA LEU M3L SER THR HIS GLY 0.431138 0.693333
102 ASP ASN ARG LEU GLY LEU VAL TYR GLN PHE 0.430769 0.661017
103 GLN ARG SER THR SEP THR 0.42963 0.803279
104 ALA ILE PHE GLN SER SER MET THR LYS 0.428571 0.741935
105 ALA ARG THR MLZ GLN THR ALA ARG LYS TYR 0.428571 0.783333
106 SER ILE ILE GLN PHE GLU HIS LEU 0.428571 0.71875
107 SER SER ARG LYS GLU TYR TYR ALA 0.426471 0.8
108 PHE ALA GLY LEU ARG GLN ALA VAL THR GLN 0.426471 0.890909
109 ARG ARG ARG VAL ARG 00S 0.425197 0.77193
110 ARG LEU TYR GLN ASN PRO THR THR TYR ILE 0.42515 0.68
111 LEU GLU LYS ALA ARG GLY SER THR TYR 0.425 0.868852
112 LEU PRO PHE ASP ARG THR THR ILE MET 0.424242 0.712329
113 GLU LEU ARG SER ARG TYR TRP ALA ILE 0.424242 0.779412
114 ARG ARG LEU PRO ILE PHE SER ARG LEU 0.424051 0.73913
115 SER ARG TYR TRP ALA ILE ARG THR ARG 0.423313 0.75
116 ARG THR PHE SER PRO THR TYR GLY LEU 0.423313 0.736111
117 ARG GLY PRO GLY ARG ALA PHE VAL THR ILE 0.422619 0.73913
118 ARG ARG ARG ARG TRP ARG GLU ARG GLN 0.422535 0.714286
119 ASP PHE GLN GLU SER ALA ASP SER PHE LEU 0.422535 0.775862
120 GLY ALA PHE THR PHE ASN GLU ASP PHE 0.422222 0.689655
121 ACE GLU ALA GLN THR ARG LEU 0.422222 0.890909
122 GLU VAL ASN 1OL ALA GLU PHE 0.421769 0.75
123 GLY ALA GLU THR PHE TYR VAL ASP GLY ALA 0.421769 0.737705
124 ALA ARG THR MLY GLN THR ALA ARG TYR 0.421769 0.776119
125 GLU LEU ASP 1OL VAL GLU PHE 0.42069 0.745455
126 TYR HIS SEP VAL VAL ARG TYR ALA 0.420382 0.684932
127 ALA THR PRO PHE GLN GLU 0.41958 0.661538
128 GLU LEU LYS ARG LYS MET ILE TYR MET 0.419355 0.765625
129 ALA ARG THR M3L GLN THR ALA ARG 0.419118 0.742424
130 SER LEU PHE ASN THR ILE ALA VAL LEU 0.418919 0.754386
131 ARG ARG ARG TRP ARG ARG LEU THR VAL 0.418919 0.796875
132 HIS LYS ILE LEU HIS ARG LEU LEU GLN GLU 0.41875 0.707692
133 ALA ASN SER ARG VAL GLN ASP SER ILE ILE 0.41844 0.844828
134 GLU LEU LYS TPO GLU ARG TYR 0.418301 0.761194
135 CYS THR PHE LYS THR LYS THR ASN 0.41791 0.775862
136 SER ARG ILE ARG ILE ARG GLY TYR VAL ARG 0.417808 0.868852
137 LYS MET ASN THR GLN PHE THR ALA VAL 0.417219 0.741935
138 LEU PRO PHE GLU LYS SER THR VAL MET 0.417178 0.652778
139 ALA ARG THR M3L GLN THR ALA DA2 LYS 0.416667 0.727273
140 CYS VAL ASN GLY SER CYS PHE THR VAL 0.416667 0.789474
141 PHE ARG SER LYS GLY GLU GLU LEU PHE THR 0.416667 0.857143
142 SER LEU PHE ASN THR VAL ALA THR LEU 0.415493 0.767857
143 LEU ASP GLU GLU THR GLY GLU PHE LEU 0.415493 0.821429
144 ALA ARG THR MLY GLN 0.415385 0.777778
145 GLU ARG GLY SER GLY ARG 0.414062 0.821429
146 GLU THR HPH TYR VAL ASP 0.412587 0.709677
147 THR LYS ASN TYR LYS GLN PHE SER VAL 0.412587 0.770492
148 SER PHE PHE GLU ASP ASN PHE VAL PRO GLU 0.412162 0.657143
149 GLN TYR PHE MET TPO GLU PTR VAL ALA 0.412121 0.616438
150 LEU PRO SER PHE GLU THR ALA LEU 0.411765 0.701493
151 THR GLU ASN LEU TYR PHE GLN SER GLY THR 0.411765 0.758065
152 ALA ASN SER ARG TRP GLN THR SER ILE ILE 0.411043 0.8
153 SER ILE ILE ASN PHE GLU LYS LEU 0.410959 0.793103
154 ARG ARG LEU ILE PHE NH2 0.410448 0.785714
155 GLY ILE LEU GLY PHE VAL PHE THR LEU 0.409722 0.741379
156 ALA LYS PHE ARG HIS ASP 0.409722 0.730159
157 SER GLU ASP GLU PHE TYR ASP ALA LEU SER 0.409396 0.75
158 ASN TYR THR PRO GLY PRO GLY THR ARG PHE 0.409357 0.69863
159 ASP PHE GLU LYS GLU GLY TYR SER LEU 0.409091 0.746032
160 GLU ASN LEU TYR PHE GLN 0.408759 0.7
161 ARG ABA VAL ILE PHE ALA ASN ILE 0.408163 0.875
162 ASP PHE GLU GLU ILE 0.408 0.690909
163 GLU ALY ARG 0.408 0.736842
164 ARG TYR GLY PHE VAL ALA ASN PHE 0.407895 0.85
165 ARG PRO GLY ASN PHE LEU GLN SER SER PRO 0.407895 0.725806
166 GLN PHE LYS ASP ASN VAL ILE LEU LEU 0.407895 0.728814
167 ILE LEU ALA LYS PHE LEU HIS ARG LEU 0.407643 0.676923
168 ILE GLY PRO GLY ARG ALA PHE TYR THR ILE 0.406977 0.708333
169 GLY ARG PHE ALA ALA ALA ILE ALA LYS 0.406897 0.793103
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 HIS LYS ILE LEU HIS ARG LEU LEU GLN ASP 0.40625 0.723077
173 VAL MET ALA PRO ARG THR LEU PHE LEU 0.406061 0.708333
174 ALA ASN SER ARG PHE PRO THR SER ILE ILE 0.406061 0.753623
175 PHE TYR ARG ALA LEU MET 0.405405 0.761905
176 ALA GLU THR PHE 0.404959 0.773585
177 GLU LEU ASN ARG LYS MET ILE TYR MET 0.404908 0.784615
178 THR ILE MET MET GLN ARG GLY 0.404412 0.786885
179 GLU VAL PTR GLU SER PRO 0.40411 0.626667
180 SER GLU LEU GLU ILE LYS ARG TYR 0.403974 0.883333
181 ASP VAL GLN THR GLY ARG ARG PRO TYR GLU 0.403614 0.742857
182 GLU PHE SER PRO 0.403101 0.646154
183 DPN PRO DAR DTH NH2 0.402878 0.738462
184 LYS ALA ARG VAL LEU ALA GLU ALA MET SER 0.402778 0.758621
185 ALA ARG THR M3L GLN THR ALA ALA LYS ALA 0.402778 0.742424
186 PRO LEU GLU PSA ARG LEU 0.402597 0.852459
187 THR PHE ALY SER ILE MET LYS 0.402597 0.698413
188 ILE ARG LYS ILE LEU PHE LEU ASP GLY ILE 0.402516 0.813559
189 THR PHE LYS LYS THR ASN 0.401515 0.789474
190 GLU ARG GLY MET THR 0.401515 0.779661
191 PRO ALA THR ILE MET MET GLN ARG GLY ASN 0.40146 0.770492
192 GLY TYR GLU ASN PRO THR TYR LYS PHE PHE 0.401198 0.60274
193 LYS VAL ILE THR PHE ILE ASP LEU 0.4 0.807018
194 THR ASN GLU PHE TYR ALA 0.4 0.683333
195 ACE GLN THR ALA ARG BTK SER THR 0.4 0.79661
196 HY1 CIR VAL ARG 00S 0.4 0.762712
Similar Ligands (3D)
Ligand no: 1; Ligand: GLU THR VAL ARG PHE GLN SER ASP; 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 : 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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