eF-site ID 3p2p-A PDB Code 3p2p Chain A click to enlarge Title ENHANCED ACTIVITY AND ALTERED SPECIFICITY OF PHOSPHOLIPASE A2 BY DELETION OF A SURFACE LOOP Classification HYDROLASE(CARBOXYL ESTER) Compound PHOSPHOLIPASE A2 Source null (PA21B_PIG) Sequence A:  ALWQFRSMIKCAIPGSHPLMDFNNYGCYCGLGGSGTPVDE LDRCCETHDNCYRDAKNLSGCYPYTESYSYSCSNTEITCN SKNNACEAFICNCDRNAAICFSKAPYNKEHKNLDTKKYC Description (1)  PHOSPHOLIPASE A2 (PHOSPHATIDE-2-ACYL-HYDROLASE) MUTANT WITH ASP 59 REPLACED BY SER, SER 60 REPLACED BY GLY, 62-66 DELETED, ASN 67 REPLACED BY TYR (D59S, S60G, DEL(62-66), N67Y) (E.C.3.1.1.4) Functional site 1) chain A residue 28 type sequence Y description BINDING SITE FOR RESIDUE CA A 125 source : AC1 2) chain A residue 30 type sequence G description BINDING SITE FOR RESIDUE CA A 125 source : AC1 3) chain A residue 32 type sequence G description BINDING SITE FOR RESIDUE CA A 125 source : AC1 4) chain A residue 49 type sequence D description BINDING SITE FOR RESIDUE CA A 125 source : AC1 5) chain A residue 71 type sequence E description BINDING SITE FOR RESIDUE CA B 126 source : AC3 6) chain A residue 72 type sequence S description BINDING SITE FOR RESIDUE CA B 126 source : AC3 7) chain A residue 92 type sequence E description BINDING SITE FOR RESIDUE CA B 126 source : AC3 8) chain A residue 44-51 type prosite sequence CCETHDNC description PA2_HIS Phospholipase A2 histidine active site. CCEtHDnC source prosite : PS00118 9) chain A residue 95-105 type prosite sequence ICNCDRNAAIC description PA2_ASP Phospholipase A2 aspartic acid active site. ICNCDRNAaIC source prosite : PS00119 10) chain A residue 48 type ACT_SITE sequence H description ACT_SITE => ECO:0000269|PubMed:6876174 source Swiss-Prot : SWS_FT_FI1 11) chain A residue 104 type ACT_SITE sequence I description ACT_SITE => ECO:0000269|PubMed:6876174 source Swiss-Prot : SWS_FT_FI1 12) chain A residue 30 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P00593 source Swiss-Prot : SWS_FT_FI2 13) chain A residue 32 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P00593 source Swiss-Prot : SWS_FT_FI2 14) chain A residue 49 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P00593 source Swiss-Prot : SWS_FT_FI2 15) chain A residue 28 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00593 source Swiss-Prot : SWS_FT_FI2 16) chain A residue 56 type LIPID sequence K description N6-palmitoyl lysine => ECO:0000269|PubMed:2498336 source Swiss-Prot : SWS_FT_FI3 17) chain A residue 30 type catalytic sequence G description 83 source MCSA : MCSA1 18) chain A residue 28 type catalytic sequence Y description 83 source MCSA : MCSA1 19) chain A residue 32 type catalytic sequence G description 83 source MCSA : MCSA1 20) chain A residue 48 type catalytic sequence H description 83 source MCSA : MCSA1 21) chain A residue 49 type catalytic sequence D description 83 source MCSA : MCSA1 22) chain A residue 52 type catalytic sequence Y description 83 source MCSA : MCSA1 23) chain A residue 78 type catalytic sequence S description 83 source MCSA : MCSA1 24) chain A residue 104 type catalytic sequence I description 83 source MCSA : MCSA1

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