› 1aby

X-ray diffraction
2.6Å resolution

CYANOMET RHB1.1 (RECOMBINANT HEMOGLOBIN)

Released:
DOI: 10.2210/pdb1aby/pdb
PDB entry 1aby coloured by chain, front view.
PDB entry 1aby coloured by chain, side view.
PDB entry 1aby coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of a hemoglobin-based blood substitute: insights into the function of allosteric proteins.
Kroeger KS, Kundrot CE
Structure 5 227-37 (1997)
PMID: 9032082

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159517 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Hemoglobin subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 283 amino acids
Theoretical weight: 30.37 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: 15.94 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 CYN 4 x CYN
Ligand HEM 4 x HEM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 102.54Å b: 115.17Å c: 56.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.175 0.278
Expression system: Not provided

Quick links

Citations

1 review citation

Hemoglobin-based oxygen carriers: development and clinical potential.
Ketcham et al. (1999)
18 other articles

1 mention without citation

Hemoglobin redux: combining neutron and X-ray diffraction with mass spectrometry to analyse the quaternary state of oxidized hemoglobins.
Mueser et al. (2010)