› 5iph

X-ray diffraction
1.3Å resolution

Xanthomonas campestris Peroxiredoxin Q - C84S mutant

Released:
DOI: 10.2210/pdb5iph/pdb
PDB entry 5iph coloured by chain, front view.
PDB entry 5iph coloured by chain, side view.
PDB entry 5iph coloured by chain, top view.
Source organism: Xanthomonas campestris pv. campestris str. ATCC 33913
Primary publication:
Peroxiredoxin Catalysis at Atomic Resolution.
Perkins A, Parsonage D, Nelson KJ, Ogba OM, Cheong PH, Poole LB, Karplus PA
Structure 24 1668-1678 (2016)
PMID: 27594682

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185726 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peroxiredoxin Bcp Chain: A
Molecule details ›
Chain: A
Length: 160 amino acids
Theoretical weight: 17.18 KDa
Source organism: Xanthomonas campestris pv. campestris str. ATCC 33913
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8P9V9 (Residues: 2-160; Coverage: 99%)
Gene names: XCC1738, bcp
Sequence domains: AhpC/TSA family
Structure domains: Glutaredoxin

Ligands and Environments

1 bound ligand:
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P21
Unit cell:
a: 35.304Å b: 50.797Å c: 39.486Å
α: 90° β: 103.59° γ: 90°
R-values:
R R work R free
0.17 0.168 0.206
Expression system: Escherichia coli

Quick links

Citations

4 review citations

ROS and RNS signalling: adaptive redox switches through oxidative/nitrosative protein modifications.
Moldogazieva et al. (2018)
3 more

1 mention without citation

Peroxiredoxins wear many hats: Factors that fashion their peroxide sensing personalities.
Bolduc et al. (2021)