› 4hsx

X-ray diffraction
1.12Å resolution

Structure of the L100F mutant of dehaloperoxidase-hemoglobin A from Amphitrite ornata with 4-bromophenol

Released:
DOI: 10.2210/pdb4hsx/pdb
PDB entry 4hsx coloured by chain, front view.
PDB entry 4hsx coloured by chain, side view.
PDB entry 4hsx coloured by chain, top view.
Source organism: Amphitrite ornata
Primary publication:
Role of polarity of the distal pocket in the control of inhibitor binding in dehaloperoxidase-hemoglobin.
Plummer A, Thompson MK, Franzen S
Biochemistry 52 2218-27 (2013)
PMID: 23480794

Function and Biology Details

Reaction catalysed: 
2 phenolic donor + H(2)O(2) = 2 phenoxyl radical of the donor + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192412 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Globin domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 137 amino acids
Theoretical weight: 15.58 KDa
Source organism: Amphitrite ornata
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NAV8 (Residues: 2-138; Coverage: 99%)
Sequence domains: Globin
Structure domains: Globins

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
3 bound ligands:
Ligand SO4 4 x SO4
Ligand GOL 1 x GOL
Ligand BML 2 x BML
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P212121
Unit cell:
a: 58.241Å b: 67.441Å c: 69.338Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.127 0.126 0.15
Expression system: Escherichia coli

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Citations

3 citation in other articles

Influence of heme environment structure on dioxygen affinity for the dual function Amphitrite ornata hemoglobin/dehaloperoxidase. Insights into the evolutional structure-function adaptations.
Sun et al. (2014)
2 more