› 1y01

X-ray diffraction
2.8Å resolution

Crystal structure of AHSP bound to Fe(II) alpha-hemoglobin

Released:
DOI: 10.2210/pdb1y01/pdb
PDB entry 1y01 coloured by chain, front view.
PDB entry 1y01 coloured by chain, side view.
PDB entry 1y01 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular mechanism of AHSP-mediated stabilization of alpha-hemoglobin.
Feng L, Gell DA, Zhou S, Gu L, Kong Y, Li J, Hu M, Yan N, Lee C, Rich AM, Armstrong RS, Lay PA, Gow AJ, Weiss MJ, Mackay JP, Shi Y
Cell 119 629-40 (2004)
PMID: 15550245

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159684 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Alpha-hemoglobin-stabilizing protein Chain: A
Molecule details ›
Chain: A
Length: 102 amino acids
Theoretical weight: 11.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NZD4 (Residues: 1-102; Coverage: 100%)
Gene names: AHSP, EDRF, ERAF
Sequence domains: Alpha-haemoglobin stabilising protein
Structure domains: AHSP
Hemoglobin subunit alpha Chain: B
Molecule details ›
Chain: B
Length: 142 amino acids
Theoretical weight: 15.28 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P69905 (Residues: 1-142; Coverage: 100%)
Gene names: HBA1, HBA2
Sequence domains: Globin
Structure domains: Globins

Ligands and Environments

3 bound ligands:
Ligand HEM 1 x HEM
Ligand OXY 1 x OXY
Ligand CHK 1 x CHK
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25, null
Spacegroup: P41212
Unit cell:
a: 69.63Å b: 69.63Å c: 140.466Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.274 0.273 0.292
Expression system: Escherichia coli

Quick links

Citations

20 review citations

Oxidative stress in the regulation of normal and neoplastic hematopoiesis.
Ghaffari S. (2008)
19 more

9 mentions without citation

The role of alpha-hemoglobin stabilizing protein in redox chemistry, denaturation, and hemoglobin assembly.
Mollan et al. (2010)
8 more