Research workbench
NSP4 proteinase from equine arteritis virus
Analyse NSP4 proteinase from equine arteritis virus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MBM
- Type
- protein
- Length
- 776 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chymotrypsin-like serine protease
- EC
- 3.4.21.-
- UniProt
- P19811
- Pockets
- 4 · best druggability 0.78
Structure
x-ray diffraction · 4 distinct chains · 10% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chymotrypsin-like serine protease (EC 3.4.21.-) | protein | 198 | 12% helix, 46% strand | P19811 |
| B | Chymotrypsin-like serine protease (EC 3.4.21.-) | protein | 192 | 8% helix, 47% strand | P19811 |
| C | Chymotrypsin-like serine protease (EC 3.4.21.-) | protein | 191 | 9% helix, 47% strand | P19811 |
| D | Chymotrypsin-like serine protease (EC 3.4.21.-) | protein | 195 | 10% helix, 47% strand | P19811 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 700 | 0.78 | 0.83 | 119 | empty |
| 2 | 55 | 0.50 | 0.87 | 18 | empty |
| 3 | 71 | 0.33 | 0.75 | 12 | empty |
| 4 | 79 | 0.33 | 0.74 | 18 | empty |
Interfaces
6 interfaces between chains.
- A–D · 529 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 468 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 413 Ų buried · 3 hydrogen bonds · protein-protein
- C–D · 390 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 367 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 1MBM · NSP4 proteinase from Equine Arteritis 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 P19811
- Elsewhere: RCSB PDB 1MBM · PDBe 1MBM · UniProt P19811
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