› 1fe5

X-ray diffraction
2.45Å resolution

SEQUENCE AND CRYSTAL STRUCTURE OF A BASIC PHOSPHOLIPASE A2 FROM COMMON KRAIT (BUNGARUS CAERULEUS) AT 2.4 RESOLUTION: IDENTIFICATION AND CHARACTERIZATION OF ITS PHARMACOLOGICAL SITES.

Released:
DOI: 10.2210/pdb1fe5/pdb
PDB entry 1fe5 coloured by chain, front view.
PDB entry 1fe5 coloured by chain, side view.
PDB entry 1fe5 coloured by chain, top view.
Source organism: Bungarus caeruleus
Primary publication:
Sequence and crystal structure determination of a basic phospholipase A2 from common krait (Bungarus caeruleus) at 2.4 A resolution: identification and characterization of its pharmacological sites.
Singh G, Gourinath S, Sharma S, Paramasivam M, Srinivasan A, Singh TP
J Mol Biol 307 1049-59 (2001)
PMID: 11286555

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190111 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Basic phospholipase A2 KPA2 Chain: A
Molecule details ›
Chain: A
Length: 118 amino acids
Theoretical weight: 12.99 KDa
Source organism: Bungarus caeruleus
UniProt:
  • Canonical: Q9DF52 (Residues: 28-145; Coverage: 94%)
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
X-ray source: RIGAKU RU200
Unit cell:
a: 57.98Å b: 57.98Å c: 57.98Å
α: 92.02° β: 92.02° γ: 92.02°
R-values:
R R work R free
0.217 0.201 0.271

Quick links

Citations

4 review citations

Structure-function relationships and mechanism of anticoagulant phospholipase A2 enzymes from snake venoms.
Kini RM. (2005)
3 more

6 mentions without citation

An algorithm for predicting protein-protein interaction sites: Abnormally exposed amino acid residues and secondary structure elements.
Hoskins et al. (2006)
5 more