› 1hjt

X-ray diffraction
1.7Å resolution

SPERM WHALE MYOGLOBIN (FERROUS, NITRIC OXIDE BOUND)

Released:
DOI: 10.2210/pdb1hjt/pdb
PDB entry 1hjt coloured by chain, front view.
PDB entry 1hjt coloured by chain, side view.
PDB entry 1hjt coloured by chain, top view.
Source organism: Physeter catodon
Primary publication:
Nitric oxide myoglobin: crystal structure and analysis of ligand geometry.
Brucker EA, Olson JS, Ikeda-Saito M, Phillips GN
Proteins 30 352-6 (1998)
PMID: 9533619

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
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 NO 1 x NO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SIEMENS
Spacegroup: P21
Unit cell:
a: 64.453Å b: 29.444Å c: 35.328Å
α: 90° β: 106.32° γ: 90°
R-values:
R R work R free
0.166 not available 0.252

Quick links

Citations

6 review citations

Interactions of multiple gas-transducing systems: hallmarks and uncertainties of CO, NO, and H2S gas biology.
Kajimura et al. (2010)
5 more

8 mentions without citation

Ambidentate H-bonding of NO and O2 in heme proteins.
Spiro et al. (2012)
7 more