› 1xye

X-ray diffraction
2.13Å resolution

T-to-THigh Transitions in Human Hemoglobin: alpha Y42A deoxy low salt

Released:
DOI: 10.2210/pdb1xye/pdb
PDB entry 1xye coloured by chain, front view.
PDB entry 1xye coloured by chain, side view.
PDB entry 1xye coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Intersubunit interactions associated with Tyr42 alpha stabilize the quaternary-T tetramer but are not major quaternary constraints in deoxyhemoglobin.
Kavanaugh JS, Rogers PH, Arnone A, Hui HL, Wierzba A, DeYoung A, Kwiatkowski LD, Noble RW, Juszczak LJ, Peterson ES, Friedman JM
Biochemistry 44 3806-20 (2005)
PMID: 15751957

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: 15.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
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
X-ray source: RIGAKU RU200
Spacegroup: P21212
Unit cell:
a: 97Å b: 99.3Å c: 66.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.192 0.241
Expression system: Escherichia coli

Quick links

Citations

1 review citation

A role of heme side-chains of human hemoglobin in its function revealed by circular dichroism and resonance Raman spectroscopy.
Nagai et al. (2018)
3 other articles