PDBe 1yex

X-ray diffraction
2.3Å resolution

Structural and biochemical analysis of the link between enzymatic activity and oligomerization in AhpC, a bacterial peroxiredoxin.

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo decamer (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: 20.66 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:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: C2221
Unit cell:
a: 127.12Å b: 170.95Å c: 135.38Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.19 0.234
Expression system: Escherichia coli