Research workbench
Molecular mechanisms of viral and host-cell substrate recognition by HCV NS3/4A protease
Analyse Molecular mechanisms of viral and host-cell substrate recognition by HCV NS3/4A… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3RC4
- Type
- protein
- Length
- 205 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- D6MZ98
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 199 | — | D6MZ98 |
| B | — | protein | 6 | — | — |
Compared structures
- 3RC4 · Molecular mechanisms of viral and host-cell substrate recognition by HCV NS3/4A 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 D6MZ98
- Elsewhere: RCSB PDB 3RC4 · PDBe 3RC4 · UniProt D6MZ98
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