1poc
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| , resolution 2.0Å | |||||||
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| Ligands: | , | ||||||
| Activity: | Phospholipase A(2), with EC number 3.1.1.4 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF BEE-VENOM PHOSPHOLIPASE A2 IN A COMPLEX WITH A TRANSITION-STATE ANALOGUE
OverviewOverview
The 2.0 angstroms crystal structure of a complex containing bee-venom phospholipase A2 (PLA2) and a phosphonate transition-state analogue was solved by multiple isomorphous replacement. The electron-density map is sufficiently detailed to visualize the proximal sugars of the enzyme's N-linked carbohydrate and a single molecule of the transition-state analogue bound ot its active center. Although bee-venom PLA2 does not belong to the large homologous Class I/II family that encompasses most other well-studied PLA2s, there is segmental sequence similarity and conservation of many functional substructures. Comparison of the bee-venom enzyme with other phospholipase structures provides compelling evidence for a common catalytic mechanism.
About this StructureAbout this Structure
1POC is a Single protein structure of sequence from Apis mellifera. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of bee-venom phospholipase A2 in a complex with a transition-state analogue., Scott DL, Otwinowski Z, Gelb MH, Sigler PB, Science. 1990 Dec 14;250(4987):1563-6. PMID:2274788
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