› 1ajh

X-ray diffraction
1.69Å resolution

PHOTOPRODUCT OF CARBONMONOXY MYOGLOBIN AT 40 K

Released:
DOI: 10.2210/pdb1ajh/pdb
PDB entry 1ajh coloured by chain, front view.
PDB entry 1ajh coloured by chain, side view.
PDB entry 1ajh coloured by chain, top view.
Source organism: Physeter catodon
Primary publication:
Photolysis-induced structural changes in single crystals of carbonmonoxy myoglobin at 40 K.
Teng TY, Srajer V, Moffat K
Nat Struct Biol 1 701-5 (1994)
PMID: 7634074

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 2 x SO4
Ligand HEM 1 x HEM
Ligand CMO 1 x CMO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X26C
Spacegroup: P21
Unit cell:
a: 63.45Å b: 30.44Å c: 34.13Å
α: 90° β: 105.7° γ: 90°
R-values:
R R work R free
0.171 0.171 0.234

Quick links

Citations

6 review citations

Spectroscopic characterization of heme iron-nitrosyl species and their role in NO reductase mechanisms in diiron proteins.
Moënne-Loccoz P. (2007)
5 more

3 mentions without citation

The role of higher CO-multipole moments in understanding the dynamics of photodissociated carbonmonoxide in myoglobin.
Plattner et al. (2008)
2 more