eF-site ID 5p2p-B PDB Code 5p2p Chain 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 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 B residue 28 type sequence Y description BINDING SITE FOR RESIDUE CA B 125 source : AC2 2) chain B residue 30 type sequence G description BINDING SITE FOR RESIDUE CA B 125 source : AC2 3) chain B residue 32 type sequence G description BINDING SITE FOR RESIDUE CA B 125 source : AC2 4) chain B residue 49 type sequence D description BINDING SITE FOR RESIDUE CA B 125 source : AC2 5) chain B residue 71 type sequence E description BINDING SITE FOR RESIDUE CA B 126 source : AC3 6) chain B residue 72 type sequence S description BINDING SITE FOR RESIDUE CA B 126 source : AC3 7) chain B residue 92 type sequence E description BINDING SITE FOR RESIDUE CA B 126 source : AC3 8) chain B residue 31 type sequence W description BINDING SITE FOR RESIDUE DHG A 126 source : AC4 9) chain B residue 32 type sequence G description BINDING SITE FOR RESIDUE DHG A 126 source : AC4 10) chain B residue 2 type sequence L description BINDING SITE FOR RESIDUE DHG B 127 source : AC5 11) chain B residue 6 type sequence R description BINDING SITE FOR RESIDUE DHG B 127 source : AC5 12) chain B residue 18 type sequence P description BINDING SITE FOR RESIDUE DHG B 127 source : AC5 13) chain B residue 28 type sequence Y description BINDING SITE FOR RESIDUE DHG B 127 source : AC5 14) chain B residue 30 type sequence G description BINDING SITE FOR RESIDUE DHG B 127 source : AC5 15) chain B residue 31 type sequence W description BINDING SITE FOR RESIDUE DHG B 127 source : AC5 16) chain B residue 32 type sequence G description BINDING SITE FOR RESIDUE DHG B 127 source : AC5 17) chain B residue 45 type sequence C description BINDING SITE FOR RESIDUE DHG B 127 source : AC5 18) chain B residue 48 type sequence H description BINDING SITE FOR RESIDUE DHG B 127 source : AC5 19) chain B residue 49 type sequence D description BINDING SITE FOR RESIDUE DHG B 127 source : AC5 20) chain B residue 52 type sequence Y description BINDING SITE FOR RESIDUE DHG B 127 source : AC5 21) chain B residue 53 type sequence R description BINDING SITE FOR RESIDUE DHG B 127 source : AC5 22) chain B residue 69 type sequence Y description BINDING SITE FOR RESIDUE DHG B 127 source : AC5 23) chain B residue 106 type sequence F description BINDING SITE FOR RESIDUE DHG B 127 source : AC5 24) chain B residue 28 type catalytic sequence Y description 83 source MCSA : MCSA2 25) chain B residue 30 type catalytic sequence G description 83 source MCSA : MCSA2 26) chain B residue 32 type catalytic sequence G description 83 source MCSA : MCSA2 27) chain B residue 48 type catalytic sequence H description 83 source MCSA : MCSA2 28) chain B residue 49 type catalytic sequence D description 83 source MCSA : MCSA2 29) chain B residue 52 type catalytic sequence Y description 83 source MCSA : MCSA2 30) chain B residue 78 type catalytic sequence S description 83 source MCSA : MCSA2 31) chain B residue 104 type catalytic sequence I description 83 source MCSA : MCSA2 32) chain B residue 48 type ACT_SITE sequence H description ACT_SITE => ECO:0000269|PubMed:6876174 source Swiss-Prot : SWS_FT_FI1 33) chain B residue 104 type ACT_SITE sequence I description ACT_SITE => ECO:0000269|PubMed:6876174 source Swiss-Prot : SWS_FT_FI1 34) chain B residue 28 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00593 source Swiss-Prot : SWS_FT_FI2 35) chain B residue 30 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P00593 source Swiss-Prot : SWS_FT_FI2 36) chain B residue 32 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P00593 source Swiss-Prot : SWS_FT_FI2 37) chain B residue 49 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P00593 source Swiss-Prot : SWS_FT_FI2 38) 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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