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Structure of a self-inhibited N475A variant of the venezuelan equine encephalitis virus (veev) NSP2 cysteine protease
Analyse Structure of a self-inhibited N475A variant of the venezuelan equine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BCM
- Type
- protein
- Length
- 321 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protease NSP2
- UniProt
- A0A0M3T9D8
- Ligands
- NA
- Pockets
- 4 · best druggability 0.47
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protease NSP2 | protein | 321 | 29% helix, 20% strand | A0A0M3T9D8 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 132 | 0.47 | 0.78 | 21 | empty |
| 2 | 78 | 0.44 | 0.80 | 17 | empty |
| 3 | 83 | 0.40 | 0.78 | 19 | empty |
| 4 | 92 | 0.39 | 0.77 | 17 | empty |
Compared structures
- 6BCM · Structure of a Self-inhibited N475A variant of the Venezuelan Equine Encephalitis Virus… · 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 A0A0M3T9D8
- Elsewhere: RCSB PDB 6BCM · PDBe 6BCM · UniProt A0A0M3T9D8
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