› 1yma

X-ray diffraction
2Å resolution

STRUCTURAL CHARACTERIZATION OF HEME LIGATION IN THE HIS64-->TYR VARIANT OF MYOGLOBIN

Released:
DOI: 10.2210/pdb1yma/pdb
PDB entry 1yma coloured by chain, front view.
PDB entry 1yma coloured by chain, side view.
PDB entry 1yma coloured by chain, top view.
Source organism: Equus caballus
Primary publication:
Structural characterization of heme ligation in the His64-->Tyr variant of myoglobin.
Maurus R, Bogumil R, Luo Y, Tang HL, Smith M, Mauk AG, Brayer GD
J Biol Chem 269 12606-10 (1994)
PMID: 8175669

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: A
Molecule details ›
Chain: A
Length: 153 amino acids
Theoretical weight: 17.01 KDa
Source organism: Equus caballus
Expression system: Not provided
UniProt:
  • Canonical: P68082 (Residues: 2-154; Coverage: 99%)
Gene name: MB
Sequence domains: Globin
Structure domains: Globins

Ligands and Environments

2 bound ligands:
Ligand SO4 1 x SO4
Ligand HEM 1 x HEM
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 63.7Å b: 28.8Å c: 35.7Å
α: 90° β: 106.6° γ: 90°
R-values:
R R work R free
0.169 not available not available
Expression system: Not provided

Quick links

Citations

8 citation in other articles

The microcontact imprinting of proteins: the effect of cross-linking monomers for lysozyme, ribonuclease A and myoglobin.
Lin et al. (2006)
7 more

1 mention without citation

Water stabilizes an alternate turn conformation in horse heart myoglobin.
Bronstein et al. (2023)