Research workbench
Crystal structure of hepatitis C virus NS3.4A protease
Analyse Crystal structure of hepatitis C virus NS3.4A protease in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2P59
- Type
- protein
- Length
- 369 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A1Z093
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 151 | — | A1Z093 |
| B | — | protein | 181 | — | A1Z093 |
| C | — | protein | 16 | — | — |
| D | — | protein | 21 | — | — |
Compared structures
- 2P59 · Crystal Structure of Hepatitis C Virus NS3.4A protease · the same entry in another collection · chain C against C, 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 A1Z093
- Elsewhere: RCSB PDB 2P59 · PDBe 2P59 · UniProt A1Z093
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