› 1nih

X-ray diffraction
2.6Å resolution

Structure of deoxy-quaternary haemoglobin with liganded beta subunits

Released:
DOI: 10.2210/pdb1nih/pdb
PDB entry 1nih coloured by chain, front view.
PDB entry 1nih coloured by chain, side view.
PDB entry 1nih coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of deoxy-quaternary haemoglobin with liganded beta subunits.
Luisi B, Liddington B, Fermi G, Shibayama N
J Mol Biol 214 7-14 (1990)
PMID: 2370669

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 Chains: A, C
Molecule details ›
Chains: A, C
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 Chains: B, D
Molecule details ›
Chains: B, 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

4 bound ligands:
Ligand HNI 2 x HNI
Ligand HEM 2 x HEM
Ligand CMO 2 x CMO
Ligand IHP 1 x IHP
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 63.18Å b: 82.26Å c: 55.06Å
α: 90° β: 98.42° γ: 90°
R-values:
R R work R free
0.214 0.214 not available
Expression system: Not provided

Quick links

Citations

24 citation in other articles

1.25 A resolution crystal structures of human haemoglobin in the oxy, deoxy and carbonmonoxy forms.
Park et al. (2006)
23 more

1 mention without citation

Native, sequential protein folding via anchored N and C protein termini.
Alberti S. (2016)