PDBe 1s5x

X-ray diffraction
2.4Å resolution

The crystal structure of Trematomus bernacchii hemoglobin oxidized by air

Released:
Source organism: Trematomus bernacchii
Primary publication:
The oxidation process of Antarctic fish hemoglobins.
Eur. J. Biochem. 271 1651-9 (2004)
PMID: 15096204

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:

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: 143 amino acids
Theoretical weight: 15.68 KDa
Source organism: Trematomus bernacchii
UniProt:
  • Canonical: P80043 (Residues: 1-142; 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: 16.15 KDa
Source organism: Trematomus bernacchii
UniProt:
  • Canonical: P80044 (Residues: 2-147; Coverage: 99%)
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: ENRAF-NONIUS
Spacegroup: C2
Unit cell:
a: 108.516Å b: 65.095Å c: 55.75Å
α: 90° β: 113.48° γ: 90°
R-values:
R R work R free
0.201 0.19 0.233