› 1a3n

X-ray diffraction
1.8Å resolution

DEOXY HUMAN HEMOGLOBIN

Released:
DOI: 10.2210/pdb1a3n/pdb
PDB 1a3n coloured by chain and viewed from the front.
PDB 1a3n coloured by chain and viewed from the side.
PDB 1a3n coloured by chain and viewed from the top.
Source organism: Homo sapiens
Entry authors: Tame J, Vallone B

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (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
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
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 4 x HEM
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 62.65Å b: 82.43Å c: 53.53Å
α: 90° β: 99.61° γ: 90°
R-values:
R R work R free
0.171 0.171 0.22

Quick links

Citations

2 review citations

Intrinsically disordered proteins: modes of binding with emphasis on disordered domains.
Morris et al. (2021)
1 more

25 mentions without citation

Intrinsic dynamics of enzymes in the unbound state and relation to allosteric regulation.
Bahar et al. (2007)
24 more