› 3emp

X-ray diffraction
4Å resolution

Crystal Structure of the S-acetanilide modified form of C165S AhpC

Released:
DOI: 10.2210/pdb3emp/pdb
PDB entry 3emp coloured by chain, front view.
PDB entry 3emp coloured by chain, side view.
PDB entry 3emp coloured by chain, top view.
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Primary publication:
Cysteine pK(a) values for the bacterial peroxiredoxin AhpC.
Nelson KJ, Parsonage D, Hall A, Karplus PA, Poole LB
Biochemistry 47 12860-8 (2008)
PMID: 18986167

Function and Biology Details

Reaction catalysed: 
NADH + ROOH + H(+) = NAD(+) + H(2)O + ROH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo decamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141051 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alkyl hydroperoxide reductase C Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 186 amino acids
Theoretical weight: 20.63 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A251 (Residues: 2-187; Coverage: 100%)
Gene names: STM0608, ahpC
Sequence domains:
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P3121
Unit cell:
a: 137.315Å b: 137.315Å c: 145.805Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.302 0.301 0.309
Expression system: Escherichia coli

Quick links

Citations

24 review citations

The basics of thiols and cysteines in redox biology and chemistry.
Poole LB. (2015)
23 more

5 mentions without citation

Structure-based insights into the catalytic power and conformational dexterity of peroxiredoxins.
Hall et al. (2011)
4 more