› 1thb

X-ray diffraction
1.5Å resolution

REFINEMENT OF A PARTIALLY OXYGENATED T STATE HAEMOGLOBIN AT 1.5 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1thb/pdb
PDB entry 1thb coloured by chain, front view.
PDB entry 1thb coloured by chain, side view.
PDB entry 1thb coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Refinement of a partially oxygenated T state human haemoglobin at 1.5 A resolution.
Waller DA, Liddington RC
Acta Crystallogr B 46 ( Pt 3) 409-18 (1990)
PMID: 2383372

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

3 bound ligands:
Ligand HEM 4 x HEM
Ligand OXY 2 x OXY
Ligand IHP 1 x IHP
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21212
Unit cell:
a: 95.8Å b: 97.8Å c: 65.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 not available not available
Expression system: Not provided

Quick links

Citations

10 citation in other articles

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 et al. (1992)
9 more

5 mentions without citation

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