› 1mbo

X-ray diffraction
1.6Å resolution

Structure and refinement of oxymyoglobin at 1.6 angstroms resolution

Released:
DOI: 10.2210/pdb1mbo/pdb
PDB 1mbo coloured by chain and viewed from the front.
PDB 1mbo coloured by chain and viewed from the side.
PDB 1mbo coloured by chain and viewed from the top.
Source organism: Physeter catodon
Primary publication:
Structure and refinement of oxymyoglobin at 1.6 A resolution.
Phillips SE
J. Mol. Biol. 142 531-54 (1980)
PMID: 7463482

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Myoglobin Chain: A
Molecule details ›
Chain: A
Length: 153 amino acids
Theoretical weight: 17.23 KDa
Source organism: Physeter catodon
Expression system: Not provided
UniProt:
  • Canonical: P02185 (Residues: 2-154; Coverage: 99%)
Gene name: MB
Sequence domains: Globin
Structure domains: Globins

Ligands and Environments

3 bound ligands:
Ligand SO4 1 x SO4
Ligand HEM 1 x HEM
Ligand OXY 1 x OXY
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 64.53Å b: 31.05Å c: 34.93Å
α: 90° β: 105.79° γ: 90°
Expression system: Not provided

Quick links

Citations

21 review citations

Oxygen Activation and Radical Transformations in Heme Proteins and Metalloporphyrins.
Huang et al. (2018)
20 more

23 mentions without citation

Resurrecting the Dead (Molecules).
Zaucha et al. (2017)
22 more