3dr9

X-ray diffraction
1.26Å resolution

Increased Distal Histidine Conformational Flexibility in the Deoxy Form of Dehaloperoxidase from Amphitrite ornata

Released:
Source organism: Amphitrite ornata
Primary publication:
Distal histidine conformational flexibility in dehaloperoxidase from Amphitrite ornata.
Acta Crystallogr D Biol Crystallogr 65 34-40 (2009)
PMID: 19153464

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
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: 15.55 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

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P212121
Unit cell:
a: 57.517Å b: 67.194Å c: 69.094Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.174 0.196
Expression system: Escherichia coli