Research workbench
Arsenate reductase C12S mutant +0.4M arsenate from E. COLI
Analyse Arsenate reductase C12S mutant +0.4M arsenate 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
- 1SD9
- 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
- CS, SO4
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arsenate reductase (EC 1.20.4.1) | protein | 138 | 37% helix, 16% strand | P08692 |
Ligands and binding sites
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 P08692
- Elsewhere: RCSB PDB 1SD9 · PDBe 1SD9 · UniProt P08692
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