eF-site ID 5p2p-A PDB Code 5p2p Chain A click to enlarge Title X-RAY STRUCTURE OF PHOSPHOLIPASE A2 COMPLEXED WITH A SUBSTRATE-DERIVED INHIBITOR Classification HYDROLASE(CARBOXYLIC ESTER) Compound PHOSPHOLIPASE A2 Source Sus scrofa (Pig) (PA21B_PIG) Sequence A:  ALFQFRSMIKCAIPGSHPLMDFNNYGCYCGWGGSGTPVDE LDRCCETHDNCYRDAKNLSGCYPYTESYSYSCSNTEITCN SKNNACEAFICNCDRNAAICFSKAPYNKEHKNLDTKKYC Description (1)  PHOSPHOLIPASE A2 (PHOSPHATIDE-2-ACYL-HYDROLASE) MUTANT WITH TRP 3 REPLACED BY PHE, LEU 31 REPLACED BY TRP, ASP 59 REPLACED BY SER, SER 60 REPLACED BY GLY, 62-66 DELETED, ASN 67 REPLACED BY TYR (W3F, L31W ,D59S, S60G, DEL(62-66), N67Y) (E.C.3.1.1.4) COMPLEX WITH (R) 2-DODECANOYL-AMINO-1-HEXANOL-PHOSPHOGLYCOL 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 2 type sequence L description BINDING SITE FOR RESIDUE DHG A 126 source : AC4 9) chain A residue 18 type sequence P description BINDING SITE FOR RESIDUE DHG A 126 source : AC4 10) chain A residue 22 type sequence F description BINDING SITE FOR RESIDUE DHG A 126 source : AC4 11) chain A residue 28 type sequence Y description BINDING SITE FOR RESIDUE DHG A 126 source : AC4 12) chain A residue 30 type sequence G description BINDING SITE FOR RESIDUE DHG A 126 source : AC4 13) chain A residue 31 type sequence W description BINDING SITE FOR RESIDUE DHG A 126 source : AC4 14) chain A residue 32 type sequence G description BINDING SITE FOR RESIDUE DHG A 126 source : AC4 15) chain A residue 48 type sequence H description BINDING SITE FOR RESIDUE DHG A 126 source : AC4 16) chain A residue 49 type sequence D description BINDING SITE FOR RESIDUE DHG A 126 source : AC4 17) chain A residue 52 type sequence Y description BINDING SITE FOR RESIDUE DHG A 126 source : AC4 18) chain A residue 69 type sequence Y description BINDING SITE FOR RESIDUE DHG A 126 source : AC4 19) chain A residue 106 type sequence F description BINDING SITE FOR RESIDUE DHG A 126 source : AC4 20) chain A residue 31 type sequence W description BINDING SITE FOR RESIDUE DHG B 127 source : AC5 21) chain A residue 32 type sequence G description BINDING SITE FOR RESIDUE DHG B 127 source : AC5 22) chain A residue 28 type catalytic sequence Y description 83 source MCSA : MCSA1 23) chain A residue 30 type catalytic sequence G description 83 source MCSA : MCSA1 24) chain A residue 32 type catalytic sequence G description 83 source MCSA : MCSA1 25) chain A residue 48 type catalytic sequence H description 83 source MCSA : MCSA1 26) chain A residue 49 type catalytic sequence D description 83 source MCSA : MCSA1 27) chain A residue 52 type catalytic sequence Y description 83 source MCSA : MCSA1 28) chain A residue 78 type catalytic sequence S description 83 source MCSA : MCSA1 29) chain A residue 104 type catalytic sequence I description 83 source MCSA : MCSA1 30) chain A residue 48 type ACT_SITE sequence H description ACT_SITE => ECO:0000269|PubMed:6876174 source Swiss-Prot : SWS_FT_FI1 31) chain A residue 104 type ACT_SITE sequence I description ACT_SITE => ECO:0000269|PubMed:6876174 source Swiss-Prot : SWS_FT_FI1 32) chain A residue 44-51 type prosite sequence CCETHDNC description PA2_HIS Phospholipase A2 histidine active site. CCEtHDnC source prosite : PS00118 33) chain A residue 95-105 type prosite sequence ICNCDRNAAIC description PA2_ASP Phospholipase A2 aspartic acid active site. ICNCDRNAaIC source prosite : PS00119 34) chain A residue 28 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00593 source Swiss-Prot : SWS_FT_FI2 35) chain A residue 30 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P00593 source Swiss-Prot : SWS_FT_FI2 36) chain A residue 32 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P00593 source Swiss-Prot : SWS_FT_FI2 37) chain A residue 49 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P00593 source Swiss-Prot : SWS_FT_FI2 38) chain A residue 56 type LIPID sequence K description N6-palmitoyl lysine => ECO:0000269|PubMed:2498336 source Swiss-Prot : SWS_FT_FI3

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