Research workbench
HCV NS3 protease DOMAIN:NS4A peptide complex
Analyse HCV NS3 protease DOMAIN:NS4A peptide complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1A1R
- Type
- protein
- Length
- 368 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P27958
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 152 | — | P27958 |
| B | — | protein | 179 | — | P27958 |
| C | — | protein | 16 | — | P27958 |
| D | — | protein | 21 | — | P27958 |
Compared structures
- 1A1R · HCV NS3 protease DOMAIN:NS4A peptide complex · 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 P27958
- Elsewhere: RCSB PDB 1A1R · PDBe 1A1R · UniProt P27958
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