MolNFT v1 · #138276 · protein
Structure of NS3 from HCV strain jfh-1 that is an unusually robust helicase that is primed to bind and unwind viral RNA
5WDX: “Structure of NS3 from HCV strain jfh-1 that is an unusually robust helicase that is primed to bind and unwind…”. X-ray diffraction, 2 ligands (MG, ZN). MolNFT v1 #138276 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5WDX
- Type
- protein
- Length
- 642 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- R9TEU1
- Ligands
- MG, ZN
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 642 | — | R9TEU1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5WDX · Structure of NS3 from HCV strain JFH-1 that is an unusually robust helicase that is… · 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 R9TEU1
- Elsewhere: RCSB PDB 5WDX · PDBe 5WDX · UniProt R9TEU1
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