› 1fl2

X-ray diffraction
1.9Å resolution

CATALYTIC CORE COMPONENT OF THE ALKYLHYDROPEROXIDE REDUCTASE AHPF FROM E.COLI

Released:
DOI: 10.2210/pdb1fl2/pdb
PDB entry 1fl2 coloured by chain, front view.
PDB entry 1fl2 coloured by chain, side view.
PDB entry 1fl2 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of the catalytic core component of the alkylhydroperoxide reductase AhpF from Escherichia coli.
Bieger B, Essen LO
J Mol Biol 307 1-8 (2001)
PMID: 11243797

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-152888 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alkyl hydroperoxide reductase subunit F Chain: A
Molecule details ›
Chain: A
Length: 310 amino acids
Theoretical weight: 32.93 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P35340 (Residues: 212-521; Coverage: 60%)
Gene names: JW0599, ahpF, b0606
Sequence domains: Pyridine nucleotide-disulphide oxidoreductase
Structure domains: FAD/NAD(P)-binding domain

Ligands and Environments

2 bound ligands:
Ligand SO4 5 x SO4
Ligand FAD 1 x FAD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P3221
Unit cell:
a: 60.44Å b: 60.44Å c: 171.83Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.197 0.197 0.217
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Why do bacteria use so many enzymes to scavenge hydrogen peroxide?
Mishra et al. (2012)
5 other articles

6 mentions without citation

Cysteine reactivity and thiol-disulfide interchange pathways in AhpF and AhpC of the bacterial alkyl hydroperoxide reductase system.
Jönsson et al. (2007)
5 more