› 5kdq

X-ray diffraction
2.15Å resolution

Deoxyhemoglobin in Complex with an Aryloxyalkanoic acid

Released:
DOI: 10.2210/pdb5kdq/pdb
PDB entry 5kdq coloured by chain, front view.
PDB entry 5kdq coloured by chain, side view.
PDB entry 5kdq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Aryloxyalkanoic Acids as Non-Covalent Modifiers of the Allosteric Properties of Hemoglobin.
Omar AM, Mahran MA, Ghatge MS, Bamane FH, Ahmed MH, El-Araby ME, Abdulmalik O, Safo MK
Molecules 21 (2016)
PMID: 27529207

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
Expression system: 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: 146 amino acids
Theoretical weight: 15.89 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
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 PO4 2 x PO4
Ligand KOH 1 x KOH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: Cu FINE FOCUS
Spacegroup: P21
Unit cell:
a: 62.222Å b: 80.83Å c: 53.397Å
α: 90° β: 80.77° γ: 90°
R-values:
R R work R free
0.196 0.192 0.257
Expression system: Homo sapiens

Quick links

Citations

1 review citation

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

1 mention without citation

Aryloxyalkanoic Acids as Non-Covalent Modifiers of the Allosteric Properties of Hemoglobin.
Omar et al. (2016)