› 1pmb

X-ray diffraction
2.5Å resolution

THE DETERMINATION OF THE CRYSTAL STRUCTURE OF RECOMBINANT PIG MYOGLOBIN BY MOLECULAR REPLACEMENT AND ITS REFINEMENT

Released:
DOI: 10.2210/pdb1pmb/pdb
PDB entry 1pmb coloured by chain, front view.
PDB entry 1pmb coloured by chain, side view.
PDB entry 1pmb coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Determination of the crystal structure of recombinant pig myoglobin by molecular replacement and its refinement.
Smerdon SJ, Oldfield TJ, Dodson EJ, Dodson GG, Hubbard RE, Wilkinson AJ
Acta Crystallogr B 46 ( Pt 3) 370-7 (1990)
PMID: 2383370

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-135413 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Myoglobin Chains: A, B
Molecule details ›
Chains: A, B
Length: 153 amino acids
Theoretical weight: 16.98 KDa
Source organism: Sus scrofa
Expression system: Not provided
UniProt:
  • Canonical: P02189 (Residues: 2-154; Coverage: 99%)
Gene name: MB
Sequence domains: Globin
Structure domains: Globins

Ligands and Environments

1 bound ligand:
Ligand HEM 2 x HEM
No modified residues

Experiments and Validation Details

Entry percentile scores
Unit cell:
a: 124.91Å b: 42.63Å c: 92.2Å
α: 90° β: 92.16° γ: 90°
R-values:
R R work R free
0.185 not available not available
Expression system: Not provided

Quick links

Citations

2 mentions without citation

Unfolding simulations of holomyoglobin from four mammals: identification of intermediates and β-sheet formation from partially unfolded states.
Dasmeh et al. (2013)
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