› 3mng

X-ray diffraction
1.45Å resolution

wild type human PrxV with DTT bound as a competitive inhibitor

Released:
DOI: 10.2210/pdb3mng/pdb
PDB entry 3mng coloured by chain, front view.
PDB entry 3mng coloured by chain, side view.
PDB entry 3mng coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural evidence that peroxiredoxin catalytic power is based on transition-state stabilization.
Hall A, Parsonage D, Poole LB, Karplus PA
J Mol Biol 402 194-209 (2010)
PMID: 20643143

Function and Biology Details

Reaction catalysed: 
Thioredoxin + ROOH = thioredoxin disulfide + H(2)O + ROH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151617 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peroxiredoxin-5, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 173 amino acids
Theoretical weight: 18.33 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P30044 (Residues: 54-214; Coverage: 75%)
Gene names: ACR1, PRDX5, SBBI10
Sequence domains: Redoxin
Structure domains: Glutaredoxin

Ligands and Environments

3 bound ligands:
Ligand D1D 1 x D1D
Ligand BR 8 x BR
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P41212
Unit cell:
a: 67.313Å b: 67.313Å c: 123.867Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.114 0.113 0.136
Expression system: Escherichia coli

Quick links

Citations

40 review citations

The thioredoxin antioxidant system.
Lu et al. (2014)
39 more

15 mentions without citation

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