› 1hga

X-ray diffraction
2.1Å resolution

HIGH RESOLUTION CRYSTAL STRUCTURES AND COMPARISONS OF T STATE DEOXYHAEMOGLOBIN AND TWO LIGANDED T-STATE HAEMOGLOBINS: T(ALPHA-OXY)HAEMOGLOBIN AND T(MET)HAEMOGLOBIN

Released:
DOI: 10.2210/pdb1hga/pdb
PDB entry 1hga coloured by chain, front view.
PDB entry 1hga coloured by chain, side view.
PDB entry 1hga coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
High resolution crystal structures and comparisons of T-state deoxyhaemoglobin and two liganded T-state haemoglobins: T(alpha-oxy)haemoglobin and T(met)haemoglobin.
Liddington R, Derewenda Z, Dodson E, Hubbard R, Dodson G
J Mol Biol 228 551-79 (1992)
PMID: 1453464

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

1 bound ligand:
Ligand HEM 4 x HEM
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21212
Unit cell:
a: 95.78Å b: 97.78Å c: 65.49Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 not available not available
Expression system: Not provided

Quick links

Citations

4 review citations

The multiple functions of hemoglobin.
Giardina et al. (1995)
3 more

5 mentions without citation

New look at hemoglobin allostery.
Yuan et al. (2015)
4 more