› 1ofj

X-ray diffraction
1.8Å resolution

RECOMBINANT SPERM WHALE MYOGLOBIN L29H/H64L/D122N MUTANT (WITH INITIATOR MET)

Released:
DOI: 10.2210/pdb1ofj/pdb
PDB entry 1ofj coloured by chain, front view.
PDB entry 1ofj coloured by chain, side view.
PDB entry 1ofj coloured by chain, top view.
Source organism: Physeter catodon
Primary publication:
Effects of the location of distal histidine in the reaction of myoglobin with hydrogen peroxide.
Matsui T, Ozaki Si, Liong E, Phillips GN, Watanabe Y
J Biol Chem 274 2838-44 (1999)
PMID: 9915818

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: 17.37 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: SIEMENS
Spacegroup: P6
Unit cell:
a: 91.442Å b: 91.442Å c: 45.761Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.162 0.162 0.219
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Oxidative lipidomics of apoptosis: redox catalytic interactions of cytochrome c with cardiolipin and phosphatidylserine.
Kagan et al. (2004)
11 more

1 mention without citation

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