› 1hda

X-ray diffraction
2.2Å resolution

A NOVEL ALLOSTERIC MECHANISM IN HAEMOGLOBIN. STRUCTURE OF BOVINE DEOXYHAEMOGLOBIN, ABSENCE OF SPECIFIC CHLORIDE-BINDING SITES AND ORIGIN OF THE CHLORIDE-LINKED BOHR EFFECT IN BOVINE AND HUMAN HAEMOGLOBIN

Released:
DOI: 10.2210/pdb1hda/pdb
PDB entry 1hda coloured by chain, front view.
PDB entry 1hda coloured by chain, side view.
PDB entry 1hda coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
A novel allosteric mechanism in haemoglobin. Structure of bovine deoxyhaemoglobin, absence of specific chloride-binding sites and origin of the chloride-linked Bohr effect in bovine and human haemoglobin.
Perutz MF, Fermi G, Poyart C, Pagnier J, Kister J
J Mol Biol 233 536-45 (1993)
PMID: 8411160

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-135382 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Hemoglobin subunit alpha Chains: A, C
Molecule details ›
Chains: A, C
Length: 141 amino acids
Theoretical weight: 15.08 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P01966 (Residues: 2-142; Coverage: 99%)
Gene name: HBA
Sequence domains: Globin
Structure domains: Globins
Hemoglobin subunit beta Chains: B, D
Molecule details ›
Chains: B, D
Length: 145 amino acids
Theoretical weight: 15.98 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P02070 (Residues: 1-145; Coverage: 100%)
Gene name: HBB
Sequence domains: Globin
Structure domains: Globins

Ligands and Environments

1 bound ligand:
Ligand HEM 4 x HEM
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 63.82Å b: 95.51Å c: 105.32Å
α: 90° β: 90° γ: 90°
Expression system: Not provided

Quick links

Citations

4 review citations

The stereochemical mechanism of the cooperative effects in hemoglobin revisited.
Perutz et al. (1998)
3 more

13 mentions without citation

Rationally selected basis proteins: a new approach to selecting proteins for spectroscopic secondary structure analysis.
Oberg et al. (2003)
12 more