Structural highlights
Function
PA21B_PIG PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Porcine phospholipase A2 (Mr = 13,980), trigonal, P3(1)21, a = b = 69.4, c = 70.4 A, one molecule per asymmetric unit, lambda (Cu K alpha) = 1.54 A. Model incorporating 975 protein atoms and eight solvent molecules refined by restrained least-squares fit to a residual R = 0.21 for 6382 reflections from 5 to 2.4 A resolution.
An independent crystallographic refinement of porcine phospholipase A2 at 2.4 A resolution.,Finzel BC, Ohlendorf DH, Weber PC, Salemme FR Acta Crystallogr B. 1991 Aug 1;47 ( Pt 4):558-9. PMID:1930837[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Finzel BC, Ohlendorf DH, Weber PC, Salemme FR. An independent crystallographic refinement of porcine phospholipase A2 at 2.4 A resolution. Acta Crystallogr B. 1991 Aug 1;47 ( Pt 4):558-9. PMID:1930837
