eF-site ID 3o4m-A PDB Code 3o4m Chain A click to enlarge Title Crystal structure of porcine pancreatic phospholipase A2 in complex with 1,2-dihydroxybenzene Classification HYDROLASE/HYDROLASE INHIBITOR Compound Phospholipase A2, major isoenzyme Source ORGANISM_COMMON: Pig; ORGANISM_SCIENTIFIC: Sus scrofa; Sequence A:  ALWQFRSMIKCAIPGSHPLMDFNNYGCYCGLGGSGTPVDE LDRCCETHDNCYRDAKNLDSCKFLVDNPYTESYSYSCSNT EITCNSKNNACEAFICNCDRNAAICFSKAPYNKEHKNLDT KKYC Description (1)  Phospholipase A2, major isoenzyme (E.C.3.1.1.4) Functional site 1) chain A residue 71 type sequence E description BINDING SITE FOR RESIDUE CA A 125 source : AC1 2) chain A residue 71 type sequence E description BINDING SITE FOR RESIDUE CA A 125 source : AC1 3) chain A residue 72 type sequence S description BINDING SITE FOR RESIDUE CA A 125 source : AC1 4) chain A residue 72 type sequence S description BINDING SITE FOR RESIDUE CA A 125 source : AC1 5) chain A residue 92 type sequence E description BINDING SITE FOR RESIDUE CA A 125 source : AC1 6) chain A residue 92 type sequence E description BINDING SITE FOR RESIDUE CA A 125 source : AC1 7) chain A residue 28 type sequence Y description BINDING SITE FOR RESIDUE CA A 126 source : AC2 8) chain A residue 32 type sequence G description BINDING SITE FOR RESIDUE CA A 126 source : AC2 9) chain A residue 49 type sequence D description BINDING SITE FOR RESIDUE CA A 126 source : AC2 10) chain A residue 6 type sequence R description BINDING SITE FOR RESIDUE CAQ A 127 source : AC3 11) chain A residue 9 type sequence I description BINDING SITE FOR RESIDUE CAQ A 127 source : AC3 12) chain A residue 23 type sequence N description BINDING SITE FOR RESIDUE CAQ A 127 source : AC3 13) chain A residue 48 type ACT_SITE sequence H description ACT_SITE => ECO:0000269|PubMed:6876174 source Swiss-Prot : SWS_FT_FI1 14) chain A residue 99 type ACT_SITE sequence D description ACT_SITE => ECO:0000269|PubMed:6876174 source Swiss-Prot : SWS_FT_FI1 15) chain A residue 49 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P00593 source Swiss-Prot : SWS_FT_FI2 16) chain A residue 30 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P00593 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 32 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P00593 source Swiss-Prot : SWS_FT_FI2 18) chain A residue 28 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00593 source Swiss-Prot : SWS_FT_FI2 19) chain A residue 56 type LIPID sequence K description N6-palmitoyl lysine => ECO:0000269|PubMed:2498336 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 44-51 type prosite sequence CCETHDNC description PA2_HIS Phospholipase A2 histidine active site. CCEtHDnC source prosite : PS00118 21) chain A residue 95-105 type prosite sequence ICNCDRNAAIC description PA2_ASP Phospholipase A2 aspartic acid active site. ICNCDRNAaIC source prosite : PS00119 22) chain A residue 30 type catalytic sequence G description 83 source MCSA : MCSA1 23) chain A residue 49 type catalytic sequence D description 83 source MCSA : MCSA1 24) chain A residue 28 type catalytic sequence Y description 83 source MCSA : MCSA1 25) chain A residue 32 type catalytic sequence G description 83 source MCSA : MCSA1 26) chain A residue 48 type catalytic sequence H description 83 source MCSA : MCSA1 27) chain A residue 52 type catalytic sequence Y description 83 source MCSA : MCSA1 28) chain A residue 73 type catalytic sequence Y description 83 source MCSA : MCSA1 29) chain A residue 99 type catalytic sequence D description 83 source MCSA : MCSA1

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