3vlk

X-ray diffraction
2Å resolution

Crystal Structure Analysis of the Ser305Ala variant of KatG from Haloarcula marismortui

Released:
Entry authors: Sato T, Higuchi W, Yoshimatsu K, Fujiwara T

Function and Biology Details

Reaction catalysed:
2 H(2)O(2) = O(2) + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129884 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Catalase-peroxidase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 737 amino acids
Theoretical weight: 82.27 KDa
Source organism: Haloarcula marismortui ATCC 43049
Expression system: Haloferax volcanii
UniProt:
  • Canonical: O59651 (Residues: 1-731; Coverage: 100%)
Gene names: Hmcp, katG2, rrnAC1171
Sequence domains: Peroxidase
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: C2
Unit cell:
a: 321.242Å b: 76.665Å c: 74.712Å
α: 90° β: 99.54° γ: 90°
R-values:
R R work R free
0.242 0.242 0.27
Expression system: Haloferax volcanii