eF-site ID 2phi-B PDB Code 2phi Chain B click to enlarge Title A LARGE CONFORMATIONAL CHANGE IS FOUND IN THE CRYSTAL STRUCTURE OF THE PORCINE PANCREATIC PHOSPHOLIPASE A2 POINT MUTANT F63V Classification HYDROLASE (CARBOXYLIC ESTER) Compound PHOSPHOLIPASE A2 Source Sus scrofa (Pig) (PA21B_PIG) Sequence B:  ALWQFRSMIKCAIPGSHPLMDFNNYGCYCGLGGSGTPVDE LDRCCETHDNCYRDAKNLDSCKVLVDNPYTESYSYSCSNT EITCNSKNNACEAFICNCDRNAAICFSKAPYNKEHKNLDT KKYC Description (1)  PHOSPHOLIPASE A2 (PHOSPHATIDE-2-ACYL-HYDROLASE) (E.C.3.1.1.4) MUTANT WITH PHE 63 REPLACED BY VAL (F63V) Functional site 1) chain B residue 71 type sequence E description BINDING SITE FOR RESIDUE CA B 125 source : AC2 2) chain B residue 72 type sequence S description BINDING SITE FOR RESIDUE CA B 125 source : AC2 3) chain B residue 92 type sequence E description BINDING SITE FOR RESIDUE CA B 125 source : AC2 4) chain B residue 28 type sequence Y description BINDING SITE FOR RESIDUE CA B 126 source : AC3 5) chain B residue 30 type sequence G description BINDING SITE FOR RESIDUE CA B 126 source : AC3 6) chain B residue 32 type sequence G description BINDING SITE FOR RESIDUE CA B 126 source : AC3 7) chain B residue 49 type sequence D description BINDING SITE FOR RESIDUE CA B 126 source : AC3 8) chain B residue 28 type catalytic sequence Y description 83 source MCSA : MCSA2 9) chain B residue 30 type catalytic sequence G description 83 source MCSA : MCSA2 10) chain B residue 32 type catalytic sequence G description 83 source MCSA : MCSA2 11) chain B residue 48 type catalytic sequence H description 83 source MCSA : MCSA2 12) chain B residue 49 type catalytic sequence D description 83 source MCSA : MCSA2 13) chain B residue 52 type catalytic sequence Y description 83 source MCSA : MCSA2 14) chain B residue 73 type catalytic sequence Y description 83 source MCSA : MCSA2 15) chain B residue 99 type catalytic sequence D description 83 source MCSA : MCSA2 16) chain B residue 28 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00593 source Swiss-Prot : SWS_FT_FI2 17) chain B residue 30 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P00593 source Swiss-Prot : SWS_FT_FI2 18) chain B residue 32 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P00593 source Swiss-Prot : SWS_FT_FI2 19) chain B residue 49 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P00593 source Swiss-Prot : SWS_FT_FI2 20) chain B residue 56 type LIPID sequence K description N6-palmitoyl lysine => ECO:0000269|PubMed:2498336 source Swiss-Prot : SWS_FT_FI3 21) chain B residue 48 type ACT_SITE sequence H description ACT_SITE => ECO:0000269|PubMed:6876174 source Swiss-Prot : SWS_FT_FI1 22) chain B residue 99 type ACT_SITE sequence D description ACT_SITE => ECO:0000269|PubMed:6876174 source Swiss-Prot : SWS_FT_FI1

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