› 5e29

X-ray diffraction
1.85Å resolution

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

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
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: 145 amino acids
Theoretical weight: 15.79 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P68871 (Residues: 3-147; Coverage: 99%)
Gene name: HBB
Sequence domains: Globin
Structure domains: Globins

Ligands and Environments

6 bound ligands:
Ligand NO 2 x NO
Ligand HEM 4 x HEM
Ligand 5JN 1 x 5JN
Ligand RQ3 2 x RQ3
Ligand NO3 2 x NO3
Ligand CAC 1 x CAC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: Cu FINE FOCUS
Spacegroup: P21212
Unit cell:
a: 95.878Å b: 98.419Å c: 65.444Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.198 0.253

Quick links

Citations

2 review citations

Hemoglobin: Structure, Function and Allostery.
Ahmed et al. (2020)
1 more

1 mention without citation

Design, Synthesis, and Investigation of Novel Nitric Oxide (NO)-Releasing Prodrugs as Drug Candidates for the Treatment of Ischemic Disorders: Insights into NO-Releasing Prodrug Biotransformation and Hemoglobin-NO Biochemistry.
Xu et al. (2015)