› 3gkv

X-ray diffraction
1.4Å resolution

X-ray structure of an intermediate along the oxidation pathway of Trematomus bernacchii hemoglobin

Released:
DOI: 10.2210/pdb3gkv/pdb
PDB entry 3gkv coloured by chain, front view.
PDB entry 3gkv coloured by chain, side view.
PDB entry 3gkv coloured by chain, top view.
Source organism: Trematomus bernacchii
Primary publication:
Combined crystallographic and spectroscopic analysis of Trematomus bernacchii hemoglobin highlights analogies and differences in the peculiar oxidation pathway of Antarctic fish hemoglobins.
Merlino A, Vitagliano L, Howes BD, Verde C, di Prisco G, Smulevich G, Sica F, Vergara A
Biopolymers 91 1117-25 (2009)
PMID: 19373928

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160338 (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

2 bound ligands:
Ligand HEM 2 x HEM
Ligand CMO 2 x CMO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: C2
Unit cell:
a: 86.88Å b: 87.647Å c: 55.339Å
α: 90° β: 100.17° γ: 90°
R-values:
R R work R free
0.191 0.184 0.211

Quick links

Citations

1 review citation

Occurrence and formation of endogenous histidine hexa-coordination in cold-adapted hemoglobins.
Merlino et al. (2011)
9 other articles

1 mention without citation

Crystallization, preliminary X-ray diffraction studies and Raman microscopy of the major haemoglobin from the sub-Antarctic fish Eleginops maclovinus in the carbomonoxy form.
Merlino et al. (2010)