› 2o5q

X-ray diffraction
1.9Å resolution

Manganese horse heart myoglobin, nitric oxide modified

Released:
DOI: 10.2210/pdb2o5q/pdb
PDB entry 2o5q coloured by chain, front view.
PDB entry 2o5q coloured by chain, side view.
PDB entry 2o5q coloured by chain, top view.
Source organism: Equus caballus
Primary publication:
Crystal structures of manganese- and cobalt-substituted myoglobin in complex with NO and nitrite reveal unusual ligand conformations.
Zahran ZN, Chooback L, Copeland DM, West AH, Richter-Addo GB
J Inorg Biochem 102 216-33 (2008)
PMID: 17905436

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-159278 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Myoglobin Chain: X
Molecule details ›
Chain: X
Length: 153 amino acids
Theoretical weight: 16.98 KDa
Source organism: Equus caballus
UniProt:
  • Canonical: P68082 (Residues: 2-154; Coverage: 99%)
Gene name: MB
Sequence domains: Globin
Structure domains: Globins

Ligands and Environments

3 bound ligands:
Ligand SO4 2 x SO4
Ligand MNH 1 x MNH
Ligand NO 1 x NO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21
Unit cell:
a: 35.468Å b: 28.637Å c: 63.193Å
α: 90° β: 105.7° γ: 90°
R-values:
R R work R free
0.18 0.177 0.235

Quick links

Citations

2 review citations

Oxidation catalysis by iron and manganese porphyrins within enzyme-like cages.
Chino et al. (2018)
1 more

2 mentions without citation

Crystal structures of manganese- and cobalt-substituted myoglobin in complex with NO and nitrite reveal unusual ligand conformations.
Zahran et al. (2008)
1 more