› 1fxw

X-ray diffraction
2.1Å resolution

CRYSTAL STRUCTURE OF THE RECOMBINANT ALPHA1/ALPHA2 CATALYTIC HETERODIMER OF BOVINE BRAIN PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE IB.

Released:
DOI: 10.2210/pdb1fxw/pdb
PDB entry 1fxw coloured by chain, front view.
PDB entry 1fxw coloured by chain, side view.
PDB entry 1fxw coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Preparation and crystal structure of the recombinant alpha(1)/alpha(2) catalytic heterodimer of bovine brain platelet-activating factor acetylhydrolase Ib.
Sheffield PJ, McMullen TW, Li J, Ho YS, Garrard SM, Derewenda U, Derewenda ZS
Protein Eng 14 513-9 (2001)
PMID: 11522926

Function and Biology Details

Reaction catalysed: 
1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H(2)O = 1-alkyl-sn-glycero-3-phosphocholine + acetate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159393 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Platelet-activating factor acetylhydrolase IB subunit alpha1 Chain: A
Molecule details ›
Chain: A
Length: 232 amino acids
Theoretical weight: 25.9 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q29460 (Residues: 1-232; Coverage: 100%)
Gene names: PAFAH1B3, PAFAHG
Sequence domains: GDSL-like Lipase/Acylhydrolase family
Structure domains: SGNH hydrolase
Platelet-activating factor acetylhydrolase IB subunit alpha2 Chain: F
Molecule details ›
Chain: F
Length: 229 amino acids
Theoretical weight: 25.6 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P68401 (Residues: 1-229; Coverage: 100%)
Gene names: PAFAH1B2P68402, PAFAHB
Sequence domains: GDSL-like Lipase/Acylhydrolase family
Structure domains: SGNH hydrolase

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 44.519Å b: 80.848Å c: 116.207Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.218 0.275
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Phospholipase A2 enzymes: physical structure, biological function, disease implication, chemical inhibition, and therapeutic intervention.
Dennis et al. (2011)
1 more

4 mentions without citation

Structural similarity enhances interaction propensity of proteins.
Lukatsky et al. (2007)
3 more