Research workbench
Crystal structure of tobacco vein mottling virus protease
Analyse Crystal structure of tobacco vein mottling virus protease in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MMG
- Type
- protein
- Length
- 446 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nuclear inclusion protein a; Nuclear inclusion protein B fragment
- UniProt
- Q9J0W2
- Pockets
- 1 · best druggability 0.35
Structure
x-ray diffraction · 4 distinct chains · 10% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear inclusion protein a | protein | 217 | 10% helix, 43% strand | Q9J0W2 |
| B | Nuclear inclusion protein a | protein | 214 | 11% helix, 39% strand | Q9J0W2 |
| C | Nuclear inclusion protein B fragment | protein | 7 | 0% helix, 57% strand | — |
| D | Nuclear inclusion protein B fragment | protein | 8 | 0% helix, 50% strand | — |
Ligands and binding sites
- FMT · Formic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 84 | 0.35 | 0.75 | 23 | empty |
Interfaces
4 interfaces between chains.
- A–B · 1432 Ų buried · 42 hydrogen bonds · protein-protein
- B–D · 802 Ų buried · 23 hydrogen bonds · protein-protein
- A–C · 736 Ų buried · 20 hydrogen bonds · protein-protein
- A–D · 53 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 3MMG · Crystal structure of tobacco vein mottling virus protease · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9J0W2
- Elsewhere: RCSB PDB 3MMG · PDBe 3MMG · UniProt Q9J0W2
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