› 1lfq

X-ray diffraction
2.6Å resolution

OXY HEMOGLOBIN (93% RELATIVE HUMIDITY)

Released:
DOI: 10.2210/pdb1lfq/pdb
PDB entry 1lfq coloured by chain, front view.
PDB entry 1lfq coloured by chain, side view.
PDB entry 1lfq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of human oxy- and deoxyhaemoglobin at different levels of humidity: variability in the T state.
Biswal BK, Vijayan M
Acta Crystallogr D Biol Crystallogr 58 1155-61 (2002)
PMID: 12077435

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
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
UniProt:
  • Canonical: P68871 (Residues: 2-147; Coverage: 99%)
Gene name: HBB
Sequence domains: Globin
Structure domains: Globins

Ligands and Environments

1 bound ligand:
Ligand HEM 2 x HEM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P41212
Unit cell:
a: 54.2Å b: 54.2Å c: 195.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.197 0.258

Quick links

Citations

2 review citations

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