› 3hvv

X-ray diffraction
1.75Å resolution

Escherichia coli Thiol peroxidase (Tpx) peroxidatic cysteine to serine mutant (C61S)

Released:
DOI: 10.2210/pdb3hvv/pdb
PDB entry 3hvv coloured by chain, front view.
PDB entry 3hvv coloured by chain, side view.
PDB entry 3hvv coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structural changes common to catalysis in the Tpx peroxiredoxin subfamily.
Hall A, Sankaran B, Poole LB, Karplus PA
J Mol Biol 393 867-81 (2009)
PMID: 19699750

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141668 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thiol peroxidase Chain: A
Molecule details ›
Chain: A
Length: 167 amino acids
Theoretical weight: 17.7 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A862 (Residues: 2-168; Coverage: 99%)
Gene names: JW1317, b1324, tpx, yzzJ
Sequence domains: Redoxin
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P3121
Unit cell:
a: 59.535Å b: 59.535Å c: 73.323Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.139 0.136 0.195
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Why do bacteria use so many enzymes to scavenge hydrogen peroxide?
Mishra et al. (2012)
8 more

9 mentions without citation

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