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3O4M

Crystal structure of porcine pancreatic phospholipase A2 in complex with 1,2-dihydroxybenzene

Summary for 3O4M
Entry DOI10.2210/pdb3o4m/pdb
Related2B00 2B03 2B04 3HSW 3L30 3L69
DescriptorPhospholipase A2, major isoenzyme, CALCIUM ION, CATECHOL, ... (4 entities in total)
Functional Keywordscatechol binding, pla2, pancreatic enzyme, disulfide bond, lipid degradation, lipoprotein, metal-binding, palmitate, pyrrolidone carboxylic acid, pancreas, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological sourceSus scrofa (Pig)
Cellular locationSecreted: P00592
Total number of polymer chains1
Total formula weight14199.98
Authors
Dileep, K.V.,Tintu, I.,Karthe, P.,Mandal, P.K.,Haridas, M.,Sadasivan, C. (deposition date: 2010-07-27, release date: 2010-08-25, Last modification date: 2024-10-30)
Primary citationDileep, K.V.,Tintu, I.,Mandal, P.K.,Karthe, P.,Haridas, M.,Sadasivan, C.
Binding to PLA(2) may contribute to the anti-inflammatory activity of catechol
Chem.Biol.Drug Des., 2011
Cited by
PubMed Abstract: Inhibiting PLA(2) activity should, in theory, be an effective approach to control the inflammation. Several naturally occurring polyphenolic compounds have been reported as inhibitors of PLA(2) . Among the naturally occurring polyphenols, catechol (1,2-dihydroxybenzene) possesses anti-inflammatory activity. Catechol can inhibit cyclooxygenase and lipo-oxygenase. By means of enzyme kinetic study, it was revealed that catechol can inhibit PLA(2) also. Crystal structure showed that catechol binds to PLA(2) at the opening of the active site cleft. This might stop the entry of substrate into the active site. Hence, catechol can be used as a lead compound for the development of novel anti-inflammatory drugs with PLA(2) as the target.
PubMed: 21995306
DOI: 10.1111/j.1747-0285.2011.01258.x
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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