› 1coh

X-ray diffraction
2.9Å resolution

STRUCTURE OF HAEMOGLOBIN IN THE DEOXY QUATERNARY STATE WITH LIGAND BOUND AT THE ALPHA HAEMS

Released:
DOI: 10.2210/pdb1coh/pdb
PDB entry 1coh coloured by chain, front view.
PDB entry 1coh coloured by chain, side view.
PDB entry 1coh coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of haemoglobin in the deoxy quaternary state with ligand bound at the alpha haems.
Luisi B, Shibayama N
J Mol Biol 206 723-36 (1989)
PMID: 2738915

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-159519 (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: 15.15 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P69905 (Residues: 2-142; Coverage: 99%)
Gene names: HBA1, HBA2
Sequence domains: Globin
Structure domains: Globins
Hemoglobin subunit beta Chains: B, D
Molecule details ›
Chains: B, D
Length: 146 amino acids
Theoretical weight: 15.89 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P68871 (Residues: 2-147; Coverage: 99%)
Gene name: HBB
Sequence domains: Globin
Structure domains: Globins

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 63.09Å b: 83.06Å c: 53.67Å
α: 90° β: 99.63° γ: 90°
Expression system: Not provided

Quick links

Citations

17 citation in other articles

1.25 A resolution crystal structures of human haemoglobin in the oxy, deoxy and carbonmonoxy forms.
Park et al. (2006)
16 more

5 mentions without citation

Advanced Glycation End-Products (AGEs): Formation, Chemistry, Classification, Receptors, and Diseases Related to AGEs.
Twarda-Clapa et al. (2022)
4 more