1bp2 Summary



The structure was published by Dijkstra, B.W., Kalk, K.H., Hol, W.G., and Drenth, J., in 1981 in a paper entitled "Structure of bovine pancreatic phospholipase A2 at 1.7A resolution." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.7 Å and deposited in 1981.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of PHOSPHOLIPASE A2. This molecule has the UniProt identifier P00593 (PA21B_BOVIN)search. The sample contained 123 residues which is 95% of the natural sequence. Out of 123 residues 123 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A PHOSPHOLIPASE A2 P00593 (23-145) (PA21B_BOVIN)search Bos taurussearch 94% 123 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00593 (23 - 145) PHOSPHOLIPASE A2 Bos taurus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P00593) Vertebrate phospholipase A2search Phospholipase A2search PF00068: Phospholipase A2search

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A (P00593) phospholipid metabolic processsearch lipid catabolic processsearch lipid metabolic processsearch hydrolase activitysearch metal ion bindingsearch phospholipase A2 activitysearch calcium ion bindingsearch extracellular regionsearch

Chain InterPro annotation
A Phospholipase A2search Phospholipase A2, active sitesearch Phospholipase A2 domainsearch