Research workbench
Arsenate reductase R60K mutant +0.4M arsenite from E. COLI
Analyse Arsenate reductase R60K mutant +0.4M arsenite from E. COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SJZ
- Type
- protein
- Length
- 138 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arsenate reductase
- EC
- 1.20.4.1
- UniProt
- P08692
- Ligands
- TAS, CS, SO4
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arsenate reductase (EC 1.20.4.1) | protein | 138 | 36% helix, 16% strand | P08692 |
Ligands and binding sites
- TAS · Trihydroxyarsenite(iii) · ligand · chains A
- CS · Cesium ion · metal · 3 copies · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
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 P08692
- Elsewhere: RCSB PDB 1SJZ · PDBe 1SJZ · UniProt P08692
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