› 1o16

X-ray diffraction
1.95Å resolution

RECOMBINANT SPERM WHALE MYOGLOBIN H64D/V68S/D122N MUTANT (MET)

Released:
DOI: 10.2210/pdb1o16/pdb
PDB entry 1o16 coloured by chain, front view.
PDB entry 1o16 coloured by chain, side view.
PDB entry 1o16 coloured by chain, top view.
Source organism: Physeter catodon
Primary publication:
Molecular engineering of myoglobin: influence of residue 68 on the rate and the enantioselectivity of oxidation reactions catalyzed by H64D/V68X myoglobin.
Yang HJ, Matsui T, Ozaki S, Kato S, Ueno T, Phillips GN, Fukuzumi S, Watanabe Y
Biochemistry 42 10174-81 (2003)
PMID: 12939145

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-135409 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Myoglobin Chain: A
Molecule details ›
Chain: A
Length: 154 amino acids
Theoretical weight: 17.33 KDa
Source organism: Physeter catodon
Expression system: Escherichia coli
UniProt:
  • Canonical: P02185 (Residues: 1-154; Coverage: 100%)
Gene name: MB
Sequence domains: Globin
Structure domains: Globins

Ligands and Environments

2 bound ligands:
Ligand SO4 1 x SO4
Ligand HEM 1 x HEM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P6
Unit cell:
a: 91.2Å b: 91.2Å c: 45.85Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.16 0.16 0.19
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Peroxide-utilizing biocatalysts: structural and functional diversity of heme-containing enzymes.
Matsunaga et al. (2004)
3 more

1 mention without citation

Water stabilizes an alternate turn conformation in horse heart myoglobin.
Bronstein et al. (2023)