› 2cmm

X-ray diffraction
1.8Å resolution

STRUCTURAL ANALYSIS OF THE MYOGLOBIN RECONSTITUTED WITH IRON PORPHINE

Released:
DOI: 10.2210/pdb2cmm/pdb
PDB entry 2cmm coloured by chain, front view.
PDB entry 2cmm coloured by chain, side view.
PDB entry 2cmm coloured by chain, top view.
Source organism: Physeter catodon
Primary publication:
Structural analysis of the myoglobin reconstituted with iron porphine.
Neya S, Funasaki N, Sato T, Igarashi N, Tanaka N
J Biol Chem 268 8935-42 (1993)
PMID: 8473336

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
Expression system: Not provided
UniProt:
  • Canonical: P02185 (Residues: 2-154; Coverage: 99%)
Gene name: MB
Sequence domains: Globin
Structure domains: Globins

Ligands and Environments

2 bound ligands:
Ligand CYN 1 x CYN
Ligand POR 1 x POR
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 57.62Å b: 76.23Å c: 33.26Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.187 not available
Expression system: Not provided

Quick links

Citations

2 review citations

Structures of a hemoglobin-based blood substitute: insights into the function of allosteric proteins.
Kroeger et al. (1997)
1 more

2 mentions without citation

Factors correlating with significant differences between X-ray structures of myoglobin.
Rashin et al. (2014)
1 more