› 1m6m

X-ray diffraction
1.8Å resolution

V68N MET MYOGLOBIN

Released:
DOI: 10.2210/pdb1m6m/pdb
PDB entry 1m6m coloured by chain, front view.
PDB entry 1m6m coloured by chain, side view.
PDB entry 1m6m coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Stabilizing bound O2 in myoglobin by valine68 (E11) to asparagine substitution.
Krzywda S, Murshudov GN, Brzozowski AM, Jaskolski M, Scott EE, Klizas SA, Gibson QH, Olson JS, Wilkinson AJ
Biochemistry 37 15896-907 (1998)
PMID: 9843395

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: 17 KDa
Source organism: Sus scrofa
Expression system: Escherichia coli
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
X-ray source: RIGAKU RU200
Unit cell:
a: 122.3Å b: 41.91Å c: 91.54Å
α: 90° β: 92.55° γ: 90°
R-values:
R R work R free
0.212 0.212 0.265
Expression system: Escherichia coli

Quick links

Citations

15 citation in other articles

Hydration of protein-protein interfaces.
Rodier et al. (2005)
14 more

1 mention without citation

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