› 2l18

Solution NMR

An arsenate reductase in the phosphate binding state

Released:
DOI: 10.2210/pdb2l18/pdb
PDB entry 2l18 coloured by chain, ensemble of 20 models, front view.
PDB entry 2l18 coloured by chain, ensemble of 20 models, side view.
PDB entry 2l18 coloured by chain, ensemble of 20 models, top view.
Source organism: Synechocystis sp. PCC 6803
Primary publication:
1H, 13C and 15N resonance assignments of the arsenate reductase from Synechocystis sp. strain PCC 6803.
Yu C, Xia B, Jin C
Biomol NMR Assign 5 85-7 (2011)
PMID: 20960080

Function and Biology Details

Reactions catalysed: 
Arsenate + glutathione + glutaredoxin = arsenite + a glutaredoxin-glutathione disulfide + H(2)O
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159932 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutaredoxin arsenate reductase Chain: A
Molecule details ›
Chain: A
Length: 134 amino acids
Theoretical weight: 14.74 KDa
Source organism: Synechocystis sp. PCC 6803
Expression system: Escherichia coli
UniProt:
  • Canonical: P74313 (Residues: 1-131; Coverage: 100%)
Gene names: arsC, slr0946
Sequence domains: Low molecular weight phosphotyrosine protein phosphatase
Structure domains: Rossmann fold

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: molecular dynamics
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

Corynebacterium glutamicum survives arsenic stress with arsenate reductases coupled to two distinct redox mechanisms.
Villadangos et al. (2011)
1 more