eF-site ID 1jq9-ABP PDB Code 1jq9 Chain A, B, P click to enlarge Title Crystal structure of a complex formed between phospholipase A2 from Daboia russelli pulchella and a designed pentapeptide Phe-Leu-Ser-Tyr-Lys at 1.8 resolution Classification HYDROLASE/HYDROLASE INHIBITOR Compound Phospholipase A2 Source ORGANISM_SCIENTIFIC: Daboia russellii pulchella; Sequence A:  SLLEFGKMILEETGKLAIPSYSSYGCYCGWGGKGTPKDAT DRCCFVHDCCYGNLPDCNPKSDRYKYKRVNGAIVCEKGTS CENRICECDKAAAICFRQNLNTYSKKYMLYPDFLCKGELK C B:  SLLEFGKMILEETGKLAIPSYSSYGCYCGWGGKGTPKDAT DRCCFVHDCCYGNLPDCNPKSDRYKYKRVNGAIVCEKGTS CENRICECDKAAAICFRQNLNTYSKKYMLYPDFLCKGELK C P:  FLSYK Description Functional site 1) chain A residue 116 type sequence K description BINDING SITE FOR RESIDUE ACY A 301 source : AC1 2) chain B residue 11 type sequence E description BINDING SITE FOR RESIDUE ACY A 301 source : AC1 3) chain A residue 121 type sequence P description BINDING SITE FOR RESIDUE ACY A 302 source : AC2 4) chain A residue 124 type sequence F description BINDING SITE FOR RESIDUE ACY A 302 source : AC2 5) chain B residue 107 type sequence R description BINDING SITE FOR RESIDUE ACY A 302 source : AC2 6) chain B residue 90 type sequence S description BINDING SITE FOR RESIDUE ACY B 303 source : AC3 7) chain A residue 43 type sequence R description BINDING SITE FOR RESIDUE ACY A 304 source : AC4 8) chain A residue 2 type sequence L description BINDING SITE FOR CHAIN P OF PEPTIDE INHIBITOR source : AC5 9) chain A residue 3 type sequence L description BINDING SITE FOR CHAIN P OF PEPTIDE INHIBITOR source : AC5 10) chain A residue 5 type sequence F description BINDING SITE FOR CHAIN P OF PEPTIDE INHIBITOR source : AC5 11) chain A residue 6 type sequence G description BINDING SITE FOR CHAIN P OF PEPTIDE INHIBITOR source : AC5 12) chain A residue 7 type sequence K description BINDING SITE FOR CHAIN P OF PEPTIDE INHIBITOR source : AC5 13) chain A residue 9 type sequence I description BINDING SITE FOR CHAIN P OF PEPTIDE INHIBITOR source : AC5 14) chain A residue 18 type sequence A description BINDING SITE FOR CHAIN P OF PEPTIDE INHIBITOR source : AC5 15) chain A residue 19 type sequence I description BINDING SITE FOR CHAIN P OF PEPTIDE INHIBITOR source : AC5 16) chain A residue 28 type sequence Y description BINDING SITE FOR CHAIN P OF PEPTIDE INHIBITOR source : AC5 17) chain A residue 29 type sequence C description BINDING SITE FOR CHAIN P OF PEPTIDE INHIBITOR source : AC5 18) chain A residue 30 type sequence G description BINDING SITE FOR CHAIN P OF PEPTIDE INHIBITOR source : AC5 19) chain A residue 31 type sequence W description BINDING SITE FOR CHAIN P OF PEPTIDE INHIBITOR source : AC5 20) chain A residue 32 type sequence G description BINDING SITE FOR CHAIN P OF PEPTIDE INHIBITOR source : AC5 21) chain A residue 48 type sequence H description BINDING SITE FOR CHAIN P OF PEPTIDE INHIBITOR source : AC5 22) chain A residue 49 type sequence D description BINDING SITE FOR CHAIN P OF PEPTIDE INHIBITOR source : AC5 23) chain A residue 69 type sequence K description BINDING SITE FOR CHAIN P OF PEPTIDE INHIBITOR source : AC5 24) chain B residue 43 type sequence R description BINDING SITE FOR CHAIN P OF PEPTIDE INHIBITOR source : AC5 25) chain B residue 46 type sequence F description BINDING SITE FOR CHAIN P OF PEPTIDE INHIBITOR source : AC5 26) chain B residue 47 type sequence V description BINDING SITE FOR CHAIN P OF PEPTIDE INHIBITOR source : AC5 27) chain B residue 54 type sequence N description BINDING SITE FOR CHAIN P OF PEPTIDE INHIBITOR source : AC5 28) chain B residue 133 type sequence C description BINDING SITE FOR CHAIN P OF PEPTIDE INHIBITOR source : AC5 29) chain A residue 44-51 type prosite sequence CCFVHDCC description PA2_HIS Phospholipase A2 histidine active site. CCFvHDcC source prosite : PS00118 30) chain A residue 95-105 type prosite sequence ICECDKAAAIC description PA2_ASP Phospholipase A2 aspartic acid active site. ICECDKAAaIC source prosite : PS00119 31) chain A residue 28 type BINDING sequence Y description BINDING => ECO:0000269|Ref.12, ECO:0007744|PDB:1TGM source Swiss-Prot : SWS_FT_FI2 32) chain A residue 30 type BINDING sequence G description BINDING => ECO:0000269|Ref.12, ECO:0007744|PDB:1TGM source Swiss-Prot : SWS_FT_FI2 33) chain A residue 32 type BINDING sequence G description BINDING => ECO:0000269|Ref.12, ECO:0007744|PDB:1TGM source Swiss-Prot : SWS_FT_FI2 34) chain A residue 49 type BINDING sequence D description BINDING => ECO:0000269|Ref.12, ECO:0007744|PDB:1TGM source Swiss-Prot : SWS_FT_FI2 35) chain B residue 28 type BINDING sequence Y description BINDING => ECO:0000269|Ref.12, ECO:0007744|PDB:1TGM source Swiss-Prot : SWS_FT_FI2 36) chain B residue 30 type BINDING sequence G description BINDING => ECO:0000269|Ref.12, ECO:0007744|PDB:1TGM source Swiss-Prot : SWS_FT_FI2 37) chain B residue 32 type BINDING sequence G description BINDING => ECO:0000269|Ref.12, ECO:0007744|PDB:1TGM source Swiss-Prot : SWS_FT_FI2 38) chain B residue 49 type BINDING sequence D description BINDING => ECO:0000269|Ref.12, ECO:0007744|PDB:1TGM source Swiss-Prot : SWS_FT_FI2 39) chain A residue 48 type ACT_SITE sequence H description ACT_SITE => ECO:0000250|UniProtKB:P14418 source Swiss-Prot : SWS_FT_FI1 40) chain A residue 99 type ACT_SITE sequence D description ACT_SITE => ECO:0000250|UniProtKB:P14418 source Swiss-Prot : SWS_FT_FI1 41) chain B residue 48 type ACT_SITE sequence H description ACT_SITE => ECO:0000250|UniProtKB:P14418 source Swiss-Prot : SWS_FT_FI1 42) chain B residue 99 type ACT_SITE sequence D description ACT_SITE => ECO:0000250|UniProtKB:P14418 source Swiss-Prot : SWS_FT_FI1

Display surface Download Links