Research workbench
X-ray structure of C15A arsenate reductase from PI258 complexed with arsenite
Analyse X-ray structure of C15A arsenate reductase from PI258 complexed with arsenite in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LJU
- Type
- protein
- Length
- 131 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arsenate reductase
- EC
- 1.97.1.5
- UniProt
- P0A006
- Ligands
- K
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arsenate reductase (EC 1.97.1.5) | protein | 131 | 34% helix, 17% strand | P0A006 |
Ligands and binding sites
- K · Potassium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 disulfide, 1 modified (disulfide, nonstandard).
Compared structures
- 1LJU · X-ray structure of C15A arsenate reductase from PI258 complexed with arsenite · the same entry in another collection · chain A against A, TM-score 1.00
- P0A006 · AlphaFold monomer V2.0 prediction for arsenate reductase (P0A006) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 1LJU · PDBe 1LJU · UniProt P0A006
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