› 1cbm

X-ray diffraction
1.74Å resolution

THE 1.8 ANGSTROM STRUCTURE OF CARBONMONOXY-BETA4 HEMOGLOBIN: ANALYSIS OF A HOMOTETRAMER WITH THE R QUATERNARY STRUCTURE OF LIGANDED ALPHA2BETA2 HEMOGLOBIN

Released:
DOI: 10.2210/pdb1cbm/pdb
PDB entry 1cbm coloured by chain, front view.
PDB entry 1cbm coloured by chain, side view.
PDB entry 1cbm coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The 1.8 A structure of carbonmonoxy-beta 4 hemoglobin. Analysis of a homotetramer with the R quaternary structure of liganded alpha 2 beta 2 hemoglobin.
Borgstahl GE, Rogers PH, Arnone A
J Mol Biol 236 817-30 (1994)
PMID: 8114096

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159525 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hemoglobin subunit beta Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, 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 SO4 4 x SO4
Ligand HEM 4 x HEM
Ligand CMO 4 x CMO
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 63.3Å b: 82.4Å c: 53.7Å
α: 90° β: 90.1° γ: 90°
R-values:
R R work R free
0.177 not available not available
Expression system: Not provided

Quick links

Citations

3 review citations

Nature of the FeO2 bonding in myoglobin and hemoglobin: A new molecular paradigm.
Shikama K. (2006)
2 more

4 mentions without citation

The role of alpha-hemoglobin stabilizing protein in redox chemistry, denaturation, and hemoglobin assembly.
Mollan et al. (2010)
3 more