3pel

X-ray diffraction
1.9Å resolution

Structure of Greyhound Hemoglobin: Origin of High Oxygen Affinity

Released:
Source organism: Canis lupus familiaris
Primary publication:
Structure of Greyhound hemoglobin: origin of high oxygen affinity.
Acta Crystallogr. D Biol. Crystallogr. 67 395-402 (2011)
PMID: 21543841

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Hemoglobin subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 141 amino acids
Theoretical weight: 15.24 KDa
Source organism: Canis lupus familiaris
UniProt:
  • Canonical: P60529 (Residues: 1-141; Coverage: 100%)
Gene name: HBA
Sequence domains: Globin
Structure domains: Globins
Hemoglobin subunit beta Chain: B
Molecule details ›
Chain: B
Length: 146 amino acids
Theoretical weight: 16.02 KDa
Source organism: Canis lupus familiaris
UniProt:
  • Canonical: P60524 (Residues: 1-146; Coverage: 100%)
Gene name: HBB
Sequence domains: Globin
Structure domains: Globins

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2
Unit cell:
a: 87.973Å b: 88.045Å c: 53.073Å
α: 90° β: 103.37° γ: 90°
R-values:
R R work R free
0.19 0.188 0.232