3s66

X-ray diffraction
1.4Å resolution

Structures and oxygen affinities of crystalline human hemoglobin C (beta6 Lys) in the R quaternary structures

Released:
Source organism: Homo sapiens
Entry authors: Shibayama N, Sugiyama K, Park SY

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Hemoglobin subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 141 amino acids
Theoretical weight: 15.15 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 Chain: B
Molecule details ›
Chain: B
Length: 146 amino acids
Theoretical weight: 15.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P68871 (Residues: 2-147; Coverage: 99%)
Gene name: HBB
Sequence domains: Globin
Structure domains: Globins

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P41212
Unit cell:
a: 53.097Å b: 53.097Å c: 191.526Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.208 0.233
Expression system: Escherichia coli