› 5lpc

X-ray diffraction
3.1Å resolution

Crystal structure of Vanadium-dependent Haloperoxidase from A. marina

Released:
DOI: 10.2210/pdb5lpc/pdb
PDB 5lpc coloured by chain and viewed from the front.
PDB 5lpc coloured by chain and viewed from the side.
PDB 5lpc coloured by chain and viewed from the top.
Source organism: Acaryochloris marina
Primary publication:
Characterization of a Cyanobacterial Haloperoxidase and Evaluation of its Biocatalytic Halogenation Potential.
Frank A, Seel CJ, Groll M, Gulder T
Chembiochem (2016)
PMID: 27542168

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dodecamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Vanadium-dependent bromoperoxidase, putative Chain: A
Molecule details ›
Chain: A
Length: 666 amino acids
Theoretical weight: 73.07 KDa
Source organism: Acaryochloris marina
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B0C4R0 (Residues: 1-639; Coverage: 100%)
Gene name: AM1_4975
Structure domains: Vanadium-containing Chloroperoxidase, domain 2

Ligands and Environments

1 bound ligand:
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: F4132
Unit cell:
a: 306.16Å b: 306.16Å c: 306.16Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.207 0.249
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Biocatalytic Oxidation Reactions: A Chemist's Perspective.
Dong et al. (2018)
2 other articles