› 1mbo

X-ray diffraction
1.6Å resolution

Structure and refinement of oxymyoglobin at 1.6 angstroms resolution

Released:
DOI: 10.2210/pdb1mbo/pdb
PDB entry 1mbo coloured by chain, front view.
PDB entry 1mbo coloured by chain, side view.
PDB entry 1mbo coloured by chain, top view.
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:
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: 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

Hydrogen bonding in globular proteins.
Baker et al. (1984)
20 more

34 mentions without citation

Hydrogen sulfide and hemeproteins: knowledge and mysteries.
Pietri et al. (2011)
33 more