› 1hco

X-ray diffraction
2.7Å resolution

THE STRUCTURE OF HUMAN CARBONMONOXY HAEMOGLOBIN AT 2.7 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1hco/pdb
PDB entry 1hco coloured by chain, front view.
PDB entry 1hco coloured by chain, side view.
PDB entry 1hco coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The structure of human carbonmonoxy haemoglobin at 2.7 A resolution.
Baldwin JM
J Mol Biol 136 103-28 (1980)
PMID: 7373648

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 Chain: A
Molecule details ›
Chain: A
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 Chain: B
Molecule details ›
Chain: B
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

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

Experiments and Validation Details

Entry percentile scores
Spacegroup: P41212
Unit cell:
a: 53.7Å b: 53.7Å c: 193Å
α: 90° β: 90° γ: 90°
Expression system: Not provided

Quick links

Citations

2 review citations

Computer studies of interactions between macromolecules.
Wodak et al. (1987)
1 more

4 mentions without citation

The implementation of SOMO (SOlution MOdeller) in the UltraScan analytical ultracentrifugation data analysis suite: enhanced capabilities allow the reliable hydrodynamic modeling of virtually any kind of biomacromolecule.
Brookes et al. (2010)
3 more