› 1ceh

X-ray diffraction
1.9Å resolution

STRUCTURE AND FUNCTION OF THE CATALYTIC SITE MUTANT ASP99ASN OF PHOSPHOLIPASE A2: ABSENCE OF CONSERVED STRUCTURAL WATER

Released:
DOI: 10.2210/pdb1ceh/pdb
PDB entry 1ceh coloured by chain, front view.
PDB entry 1ceh coloured by chain, side view.
PDB entry 1ceh coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Structure and function of the catalytic site mutant Asp 99 Asn of phospholipase A2: absence of the conserved structural water.
Kumar A, Sekharudu C, Ramakrishnan B, Dupureur CM, Zhu H, Tsai MD, Sundaralingam M
Protein Sci 3 2082-8 (1994)
PMID: 7703854

Function and Biology Details

Reaction catalysed: 
Phosphatidylcholine + H(2)O = 1-acylglycerophosphocholine + a carboxylate
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-132751 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phospholipase A2 Chain: A
Molecule details ›
Chain: A
Length: 123 amino acids
Theoretical weight: 13.81 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P00593 (Residues: 23-145; Coverage: 95%)
Gene name: PLA2G1B
Sequence domains: Phospholipase A2
Structure domains: Phospholipase A2 domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3121
Unit cell:
a: 46.11Å b: 46.11Å c: 102.1Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.185 0.185 not available
Expression system: Not provided

Quick links

Citations

3 review citations

Structural requirements of pyrroloquinoline quinone dependent enzymatic reactions.
Oubrie et al. (2000)
2 more

2 mentions without citation

Possible roles of S···O and S···N interactions in the functions and evolution of phospholipase A2.
Iwaoka et al. (2006)
1 more