eF-site ID 5p2p-AB PDB Code 5p2p Chain A, B 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 B:  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 B residue 28 type sequence Y description BINDING SITE FOR RESIDUE CA B 125 source : AC2 6) chain B residue 30 type sequence G description BINDING SITE FOR RESIDUE CA B 125 source : AC2 7) chain B residue 32 type sequence G description BINDING SITE FOR RESIDUE CA B 125 source : AC2 8) chain B residue 49 type sequence D description BINDING SITE FOR RESIDUE CA B 125 source : AC2 9) chain A residue 71 type sequence E description BINDING SITE FOR RESIDUE CA B 126 source : AC3 10) chain A residue 72 type sequence S description BINDING SITE FOR RESIDUE CA B 126 source : AC3 11) chain A residue 92 type sequence E description BINDING SITE FOR RESIDUE CA B 126 source : AC3 12) chain B residue 71 type sequence E description BINDING SITE FOR RESIDUE CA B 126 source : AC3 13) chain B residue 72 type sequence S description BINDING SITE FOR RESIDUE CA B 126 source : AC3 14) chain B residue 92 type sequence E description BINDING SITE FOR RESIDUE CA B 126 source : AC3 15) chain A residue 2 type sequence L description BINDING SITE FOR RESIDUE DHG A 126 source : AC4 16) chain A residue 18 type sequence P description BINDING SITE FOR RESIDUE DHG A 126 source : AC4 17) chain A residue 22 type sequence F description BINDING SITE FOR RESIDUE DHG A 126 source : AC4 18) chain A residue 28 type sequence Y description BINDING SITE FOR RESIDUE DHG A 126 source : AC4 19) chain A residue 30 type sequence G description BINDING SITE FOR RESIDUE DHG A 126 source : AC4 20) chain A residue 31 type sequence W description BINDING SITE FOR RESIDUE DHG A 126 source : AC4 21) chain A residue 32 type sequence G description BINDING SITE FOR RESIDUE DHG A 126 source : AC4 22) chain A residue 48 type sequence H description BINDING SITE FOR RESIDUE DHG A 126 source : AC4 23) chain A residue 49 type sequence D description BINDING SITE FOR RESIDUE DHG A 126 source : AC4 24) chain A residue 52 type sequence Y description BINDING SITE FOR RESIDUE DHG A 126 source : AC4 25) chain A residue 69 type sequence Y description BINDING SITE FOR RESIDUE DHG A 126 source : AC4 26) chain A residue 106 type sequence F description BINDING SITE FOR RESIDUE DHG A 126 source : AC4 27) chain B residue 31 type sequence W description BINDING SITE FOR RESIDUE DHG A 126 source : AC4 28) chain B residue 32 type sequence G description BINDING SITE FOR RESIDUE DHG A 126 source : AC4 29) chain A residue 31 type sequence W description BINDING SITE FOR RESIDUE DHG B 127 source : AC5 30) chain A residue 32 type sequence G description BINDING SITE FOR RESIDUE DHG B 127 source : AC5 31) chain B residue 2 type sequence L description BINDING SITE FOR RESIDUE DHG B 127 source : AC5 32) chain B residue 6 type sequence R description BINDING SITE FOR RESIDUE DHG B 127 source : AC5 33) chain B residue 18 type sequence P description BINDING SITE FOR RESIDUE DHG B 127 source : AC5 34) chain B residue 28 type sequence Y description BINDING SITE FOR RESIDUE DHG B 127 source : AC5 35) chain B residue 30 type sequence G description BINDING SITE FOR RESIDUE DHG B 127 source : AC5 36) chain B residue 31 type sequence W description BINDING SITE FOR RESIDUE DHG B 127 source : AC5 37) chain B residue 32 type sequence G description BINDING SITE FOR RESIDUE DHG B 127 source : AC5 38) chain B residue 45 type sequence C description BINDING SITE FOR RESIDUE DHG B 127 source : AC5 39) chain B residue 48 type sequence H description BINDING SITE FOR RESIDUE DHG B 127 source : AC5 40) chain B residue 49 type sequence D description BINDING SITE FOR RESIDUE DHG B 127 source : AC5 41) chain B residue 52 type sequence Y description BINDING SITE FOR RESIDUE DHG B 127 source : AC5 42) chain B residue 53 type sequence R description BINDING SITE FOR RESIDUE DHG B 127 source : AC5 43) chain B residue 69 type sequence Y description BINDING SITE FOR RESIDUE DHG B 127 source : AC5 44) chain B residue 106 type sequence F description BINDING SITE FOR RESIDUE DHG B 127 source : AC5 45) chain A residue 44-51 type prosite sequence CCETHDNC description PA2_HIS Phospholipase A2 histidine active site. CCEtHDnC source prosite : PS00118 46) chain A residue 95-105 type prosite sequence ICNCDRNAAIC description PA2_ASP Phospholipase A2 aspartic acid active site. ICNCDRNAaIC source prosite : PS00119 47) chain A residue 30 type catalytic sequence G description 83 source MCSA : MCSA1 48) chain A residue 28 type catalytic sequence Y description 83 source MCSA : MCSA1 49) chain A residue 32 type catalytic sequence G description 83 source MCSA : MCSA1 50) chain A residue 48 type catalytic sequence H description 83 source MCSA : MCSA1 51) chain A residue 49 type catalytic sequence D description 83 source MCSA : MCSA1 52) chain A residue 52 type catalytic sequence Y description 83 source MCSA : MCSA1 53) chain A residue 78 type catalytic sequence S description 83 source MCSA : MCSA1 54) chain A residue 104 type catalytic sequence I description 83 source MCSA : MCSA1 55) chain B residue 30 type catalytic sequence G description 83 source MCSA : MCSA2 56) chain B residue 28 type catalytic sequence Y description 83 source MCSA : MCSA2 57) chain B residue 32 type catalytic sequence G description 83 source MCSA : MCSA2 58) chain B residue 48 type catalytic sequence H description 83 source MCSA : MCSA2 59) chain B residue 49 type catalytic sequence D description 83 source MCSA : MCSA2 60) chain B residue 52 type catalytic sequence Y description 83 source MCSA : MCSA2 61) chain B residue 78 type catalytic sequence S description 83 source MCSA : MCSA2 62) chain B residue 104 type catalytic sequence I description 83 source MCSA : MCSA2 63) chain B residue 48 type ACT_SITE sequence H description ACT_SITE => ECO:0000269|PubMed:6876174 source Swiss-Prot : SWS_FT_FI1 64) chain B residue 104 type ACT_SITE sequence I description ACT_SITE => ECO:0000269|PubMed:6876174 source Swiss-Prot : SWS_FT_FI1 65) chain A residue 48 type ACT_SITE sequence H description ACT_SITE => ECO:0000269|PubMed:6876174 source Swiss-Prot : SWS_FT_FI1 66) chain A residue 104 type ACT_SITE sequence I description ACT_SITE => ECO:0000269|PubMed:6876174 source Swiss-Prot : SWS_FT_FI1 67) chain B residue 32 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P00593 source Swiss-Prot : SWS_FT_FI2 68) chain B residue 49 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P00593 source Swiss-Prot : SWS_FT_FI2 69) chain A residue 30 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P00593 source Swiss-Prot : SWS_FT_FI2 70) chain A residue 32 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P00593 source Swiss-Prot : SWS_FT_FI2 71) chain A residue 49 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P00593 source Swiss-Prot : SWS_FT_FI2 72) chain B residue 28 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00593 source Swiss-Prot : SWS_FT_FI2 73) chain B residue 30 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P00593 source Swiss-Prot : SWS_FT_FI2 74) chain A residue 28 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00593 source Swiss-Prot : SWS_FT_FI2 75) chain A residue 56 type LIPID sequence K description N6-palmitoyl lysine => ECO:0000269|PubMed:2498336 source Swiss-Prot : SWS_FT_FI3 76) chain B residue 56 type LIPID sequence K description N6-palmitoyl lysine => ECO:0000269|PubMed:2498336 source Swiss-Prot : SWS_FT_FI3

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