eF-site ID 1g2x-ABC PDB Code 1g2x Chain A, B, C click to enlarge Title Sequence induced trimerization of krait PLA2: crystal structure of the trimeric form of krait PLA2 Classification TOXIN Compound PHOSPHOLIPASE A2 Source ORGANISM_SCIENTIFIC: Bungarus caeruleus; Sequence A:  NLQQFKNMIQCAGTRTWTAYINYGCYCGKGGSGTPVDKLD RCCYTHDHCYNQADSIPGCNPNIKTYSYTCTQPNITCTRT ADACAKFLCDCDRTAAICFASAPYNINNIMISASNSCQ B:  NLQQFKNMIQCAGTRTWTAYINYGCYCGKGGSGTPVDKLD RCCYTHDHCYNQADSIPGCNPNIKTYSYTCTQPNITCTRT ADACAKFLCDCDRTAAICFASAPYNINNIMISASNSCQ C:  NLQQFKNMIQCAGTRTWTAYINYGCYCGKGGSGTPVDKLD RCCYTHDHCYNQADSIPGCNPNIKTYSYTCTQPNITCTRT ADACAKFLCDCDRTAAICFASAPYNINNIMISASNSCQ Description Functional site 1) chain A residue 44-51 type prosite sequence CCYTHDHC description PA2_HIS Phospholipase A2 histidine active site. CCYtHDhC source prosite : PS00118 2) chain A residue 90-100 type prosite sequence LCDCDRTAAIC description PA2_ASP Phospholipase A2 aspartic acid active site. LCDCDRTAaIC source prosite : PS00119 3) chain A residue 48 type ACT_SITE sequence H description ACT_SITE => ECO:0000250|UniProtKB:P14418 source Swiss-Prot : SWS_FT_FI1 4) chain A residue 94 type ACT_SITE sequence D description ACT_SITE => ECO:0000250|UniProtKB:P14418 source Swiss-Prot : SWS_FT_FI1 5) chain B residue 48 type ACT_SITE sequence H description ACT_SITE => ECO:0000250|UniProtKB:P14418 source Swiss-Prot : SWS_FT_FI1 6) chain B residue 94 type ACT_SITE sequence D description ACT_SITE => ECO:0000250|UniProtKB:P14418 source Swiss-Prot : SWS_FT_FI1 7) chain C residue 48 type ACT_SITE sequence H description ACT_SITE => ECO:0000250|UniProtKB:P14418 source Swiss-Prot : SWS_FT_FI1 8) chain C residue 94 type ACT_SITE sequence D description ACT_SITE => ECO:0000250|UniProtKB:P14418 source Swiss-Prot : SWS_FT_FI1 9) chain A residue 28 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P14418 source Swiss-Prot : SWS_FT_FI2 10) chain C residue 30 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P14418 source Swiss-Prot : SWS_FT_FI2 11) chain C residue 32 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P14418 source Swiss-Prot : SWS_FT_FI2 12) chain C residue 49 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P14418 source Swiss-Prot : SWS_FT_FI2 13) chain A residue 30 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P14418 source Swiss-Prot : SWS_FT_FI2 14) chain A residue 32 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P14418 source Swiss-Prot : SWS_FT_FI2 15) chain A residue 49 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P14418 source Swiss-Prot : SWS_FT_FI2 16) chain B residue 28 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P14418 source Swiss-Prot : SWS_FT_FI2 17) chain B residue 30 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P14418 source Swiss-Prot : SWS_FT_FI2 18) chain B residue 32 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P14418 source Swiss-Prot : SWS_FT_FI2 19) chain B residue 49 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P14418 source Swiss-Prot : SWS_FT_FI2 20) chain C residue 28 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P14418 source Swiss-Prot : SWS_FT_FI2

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