eF-site ID 1ijl-AB PDB Code 1ijl Chain A, B click to enlarge Title Crystal structure of acidic phospholipase A2 from deinagkistrodon acutus Classification HYDROLASE Compound PHOSPHOLIPASE A2 Source ORGANISM_COMMON: Chinese moccasin; ORGANISM_SCIENTIFIC: Deinagkistrodon acutus; Sequence A:  SLIQFETLIMKVVKKSGMFWYSAYGCYCGWGGHGRPQDAT DRCCFVHDCCYGKVTGCDPKMDSYTYSEENGDIVCGGDDP CKREICECDRVAADCFRDNLDTYNSDTYWRYPRQDCEESP EPC B:  SLIQFETLIMKVVKKSGMFWYSAYGCYCGWGGHGRPQDAT DRCCFVHDCCYGKVTGCDPKMDSYTYSEENGDIVCGGDDP CKREICECDRVAADCFRDNLDTYNSDTYWRYPRQDCEESP EPC Description Functional site 1) chain A residue 33 type sequence H description BINDING SITE FOR RESIDUE ZN A 201 source : AC1 2) chain B residue 27 type sequence Y description BINDING SITE FOR RESIDUE CA B 202 source : AC2 3) chain B residue 29 type sequence G description BINDING SITE FOR RESIDUE CA B 202 source : AC2 4) chain B residue 31 type sequence G description BINDING SITE FOR RESIDUE CA B 202 source : AC2 5) chain B residue 48 type sequence D description BINDING SITE FOR RESIDUE CA B 202 source : AC2 6) chain A residue 27 type sequence Y description BINDING SITE FOR RESIDUE CA A 203 source : AC3 7) chain A residue 29 type sequence G description BINDING SITE FOR RESIDUE CA A 203 source : AC3 8) chain A residue 31 type sequence G description BINDING SITE FOR RESIDUE CA A 203 source : AC3 9) chain A residue 48 type sequence D description BINDING SITE FOR RESIDUE CA A 203 source : AC3 10) chain A residue 43-50 type prosite sequence CCFVHDCC description PA2_HIS Phospholipase A2 histidine active site. CCFvHDcC source prosite : PS00118 11) chain A residue 85-95 type prosite sequence ICECDRVAADC description PA2_ASP Phospholipase A2 aspartic acid active site. ICECDRVAaDC source prosite : PS00119 12) chain A residue 47 type ACT_SITE sequence H description ACT_SITE => ECO:0000250|UniProtKB:P00593 source Swiss-Prot : SWS_FT_FI1 13) chain A residue 89 type ACT_SITE sequence D description ACT_SITE => ECO:0000250|UniProtKB:P00593 source Swiss-Prot : SWS_FT_FI1 14) chain B residue 47 type ACT_SITE sequence H description ACT_SITE => ECO:0000250|UniProtKB:P00593 source Swiss-Prot : SWS_FT_FI1 15) chain B residue 89 type ACT_SITE sequence D description ACT_SITE => ECO:0000250|UniProtKB:P00593 source Swiss-Prot : SWS_FT_FI1 16) chain A residue 27 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:11752784, ECO:0007744|PDB:1IJL source Swiss-Prot : SWS_FT_FI2 17) chain A residue 29 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11752784, ECO:0007744|PDB:1IJL source Swiss-Prot : SWS_FT_FI2 18) chain A residue 31 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11752784, ECO:0007744|PDB:1IJL source Swiss-Prot : SWS_FT_FI2 19) chain B residue 27 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:11752784, ECO:0007744|PDB:1IJL source Swiss-Prot : SWS_FT_FI2 20) chain B residue 29 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11752784, ECO:0007744|PDB:1IJL source Swiss-Prot : SWS_FT_FI2 21) chain B residue 31 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11752784, ECO:0007744|PDB:1IJL source Swiss-Prot : SWS_FT_FI2 22) chain A residue 48 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11752784 source Swiss-Prot : SWS_FT_FI3 23) chain B residue 48 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11752784 source Swiss-Prot : SWS_FT_FI3

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