1ijl
From Proteopedia
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| , resolution 2.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Phospholipase A(2), with EC number 3.1.1.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of acidic phospholipase A2 from deinagkistrodon acutus
Overview
An acidic phospholipase A(2) was purified from Deinagkistrodon acutus (Agkistrodon acutus) which displays an inhibitory effect on platelet aggregation. The three-dimensional structure of the enzyme was determined by molecular replacement at 2.6 A resolution with a crystallographic R factor of 18.40% (R(free) = 22.50%) and reasonable stereochemistry. Two molecules in the asymmetric unit form a dimer and the dimer formation accompanies a significant conformational adaptation of segment 14-23, a constituent of the 'interface recognition site' (IRS). This probably reflects the inherent structural flexibility of the IRS. The possible expansion of the site for inhibiting platelet aggregation as proposed previously [Wang et al. (1996), J. Mol. Biol. 255, 669-676] is discussed.
About this Structure
1IJL is a Single protein structure of sequence from Deinagkistrodon acutus. Full crystallographic information is available from OCA.
Reference
Structure of an acidic phospholipase A2 from the venom of Deinagkistrodon acutus., Gu L, Zhang H, Song S, Zhou Y, Lin Z, Acta Crystallogr D Biol Crystallogr. 2002 Jan;58(Pt 1):104-10. Epub 2001, Dec 21. PMID:11752784
Page seeded by OCA on Thu Mar 20 11:51:11 2008
