eF-site ID 1kpm-AB PDB Code 1kpm Chain A, B click to enlarge Title First Structural Evidence of a Specific Inhibition of Phospholipase A2 by Vitamin E and its Implications in Inflammation: Crystal Structure of the Complex Formed between Phospholipase A2 and Vitamin E at 1.8 A Resolution. Classification HYDROLASE Compound Phospholipase A2 Source ORGANISM_SCIENTIFIC: Daboia russellii pulchella; Sequence A:  SLLEFGKMILEETGKLAIPSYSSYGCYCGWGGKGTPKDAT DRCCFVHDCCYGNLPDCNPKSDRYKYKRVNGAIVCEKGTS CENRICECDKAAAICFRQNLNTYSKKYMLYPDFLCKGELK C B:  SLLEFGKMILEETGKLAIPSYSSYGCYCGWGGKGTPKDAT DRCCFVHDCCYGNLPDCNPKSDRYKYKRVNGAIVCEKGTS CENRICECDKAAAICFRQNLNTYSKKYMLYPDFLCKGELK C Description Functional site 1) chain A residue 2 type sequence L description BINDING SITE FOR RESIDUE VIT A 401 source : AC1 2) chain A residue 3 type sequence L description BINDING SITE FOR RESIDUE VIT A 401 source : AC1 3) chain A residue 6 type sequence G description BINDING SITE FOR RESIDUE VIT A 401 source : AC1 4) chain A residue 7 type sequence K description BINDING SITE FOR RESIDUE VIT A 401 source : AC1 5) chain A residue 18 type sequence A description BINDING SITE FOR RESIDUE VIT A 401 source : AC1 6) chain A residue 19 type sequence I description BINDING SITE FOR RESIDUE VIT A 401 source : AC1 7) chain A residue 22 type sequence Y description BINDING SITE FOR RESIDUE VIT A 401 source : AC1 8) chain A residue 23 type sequence S description BINDING SITE FOR RESIDUE VIT A 401 source : AC1 9) chain A residue 28 type sequence Y description BINDING SITE FOR RESIDUE VIT A 401 source : AC1 10) chain A residue 45 type sequence C description BINDING SITE FOR RESIDUE VIT A 401 source : AC1 11) chain A residue 48 type sequence H description BINDING SITE FOR RESIDUE VIT A 401 source : AC1 12) chain A residue 49 type sequence D description BINDING SITE FOR RESIDUE VIT A 401 source : AC1 13) chain A residue 69 type sequence K description BINDING SITE FOR RESIDUE VIT A 401 source : AC1 14) chain B residue 54 type sequence N description BINDING SITE FOR RESIDUE VIT A 401 source : AC1 15) chain B residue 133 type sequence C description BINDING SITE FOR RESIDUE VIT A 401 source : AC1 16) chain A residue 121 type sequence P description BINDING SITE FOR RESIDUE ACY B 501 source : AC2 17) chain B residue 11 type sequence E description BINDING SITE FOR RESIDUE ACY B 501 source : AC2 18) chain B residue 77 type sequence R description BINDING SITE FOR RESIDUE ACY B 501 source : AC2 19) chain B residue 107 type sequence R description BINDING SITE FOR RESIDUE ACY B 501 source : AC2 20) chain A residue 121 type sequence P description BINDING SITE FOR RESIDUE ACY B 502 source : AC3 21) chain A residue 124 type sequence F description BINDING SITE FOR RESIDUE ACY B 502 source : AC3 22) chain B residue 107 type sequence R description BINDING SITE FOR RESIDUE ACY B 502 source : AC3 23) chain B residue 108 type sequence Q description BINDING SITE FOR RESIDUE ACY B 502 source : AC3 24) chain B residue 89 type sequence T description BINDING SITE FOR RESIDUE ACY B 503 source : AC4 25) chain B residue 90 type sequence S description BINDING SITE FOR RESIDUE ACY B 503 source : AC4 26) chain A residue 43 type sequence R description BINDING SITE FOR RESIDUE ACY A 504 source : AC5 27) chain A residue 48 type ACT_SITE sequence H description ACT_SITE => ECO:0000250|UniProtKB:P14418 source Swiss-Prot : SWS_FT_FI1 28) chain A residue 99 type ACT_SITE sequence D description ACT_SITE => ECO:0000250|UniProtKB:P14418 source Swiss-Prot : SWS_FT_FI1 29) chain B residue 48 type ACT_SITE sequence H description ACT_SITE => ECO:0000250|UniProtKB:P14418 source Swiss-Prot : SWS_FT_FI1 30) chain B residue 99 type ACT_SITE sequence D description ACT_SITE => ECO:0000250|UniProtKB:P14418 source Swiss-Prot : SWS_FT_FI1 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 44-51 type prosite sequence CCFVHDCC description PA2_HIS Phospholipase A2 histidine active site. CCFvHDcC source prosite : PS00118 40) chain A residue 95-105 type prosite sequence ICECDKAAAIC description PA2_ASP Phospholipase A2 aspartic acid active site. ICECDKAAaIC source prosite : PS00119

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