Research workbench
PI258 arsenate reductase (arsc) triple mutant C10S/C15A/C82S
Analyse PI258 arsenate reductase (arsc) triple mutant C10S/C15A/C82S in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RXI
- Type
- protein
- Length
- 131 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arsenate reductase
- EC
- 1.20.4.1
- UniProt
- P0A006
- Ligands
- LCP, K, CL
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arsenate reductase (EC 1.20.4.1) | protein | 131 | 40% helix, 18% strand | P0A006 |
Ligands and binding sites
- LCP · Perchlorate ion · ligand · chains A
- K · Potassium ion · metal · chains A
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 P0A006
- Elsewhere: RCSB PDB 1RXI · PDBe 1RXI · UniProt P0A006
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