› 1es9

X-ray diffraction
1.3Å resolution

X-RAY CRYSTAL STRUCTURE OF R22K MUTANT OF THE MAMMALIAN BRAIN PLATELET-ACTIVATING FACTOR ACETYLHYDROLASES (PAF-AH)

Released:
DOI: 10.2210/pdb1es9/pdb
PDB entry 1es9 coloured by chain, front view.
PDB entry 1es9 coloured by chain, side view.
PDB entry 1es9 coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
The functional implications of the dimerization of the catalytic subunits of the mammalian brain platelet-activating factor acetylhydrolase (Ib).
McMullen TW, Li J, Sheffield PJ, Aoki J, Martin TW, Arai H, Inoue K, Derewenda ZS
Protein Eng 13 865-71 (2000)
PMID: 11239086

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173350 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Platelet-activating factor acetylhydrolase IB subunit alpha1 Chain: A
Molecule details ›
Chain: A
Length: 232 amino acids
Theoretical weight: 25.88 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: Q29460 (Residues: 1-232; Coverage: 100%)
Gene names: PAFAH1B3, PAFAHG
Sequence domains: GDSL-like Lipase/Acylhydrolase family
Structure domains: SGNH hydrolase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9B
Spacegroup: P3121
Unit cell:
a: 81.049Å b: 81.049Å c: 72.662Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.192 0.192 0.217

Quick links

Citations

1 review citation

Regulation of the Golgi complex by phospholipid remodeling enzymes.
Ha et al. (2012)
5 other articles

6 mentions without citation

Overview of protein structural and functional folds.
Sun et al. (2004)
5 more