› 3hc9

X-ray diffraction
2Å resolution

Ferric Horse Heart Myoglobin; H64V mutant

Released:
DOI: 10.2210/pdb3hc9/pdb
PDB entry 3hc9 coloured by chain, front view.
PDB entry 3hc9 coloured by chain, side view.
PDB entry 3hc9 coloured by chain, top view.
Source organism: Equus caballus
Primary publication:
The distal pocket histidine residue in horse heart myoglobin directs the O-binding mode of nitrite to the heme iron.
Yi J, Heinecke J, Tan H, Ford PC, Richter-Addo GB
J Am Chem Soc 131 18119-28 (2009)
PMID: 19924902

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-549791 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Myoglobin Chain: A
Molecule details ›
Chain: A
Length: 153 amino acids
Theoretical weight: 16.94 KDa
Source organism: Equus caballus
Expression system: Escherichia coli
UniProt:
  • Canonical: P68082 (Residues: 2-154; Coverage: 99%)
Gene name: MB
Sequence domains: Globin
Structure domains: Globins

Ligands and Environments

3 bound ligands:
Ligand HEM 1 x HEM
Ligand PO4 1 x PO4
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P21212
Unit cell:
a: 30.639Å b: 119.236Å c: 56.677Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.186 0.237
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Small molecule signaling agents: the integrated chemistry and biochemistry of nitrogen oxides, oxides of carbon, dioxygen, hydrogen sulfide, and their derived species.
Fukuto et al. (2012)
4 more

3 mentions without citation

The distal pocket histidine residue in horse heart myoglobin directs the O-binding mode of nitrite to the heme iron.
Yi et al. (2009)
2 more