eF-site ID 1i9a-AB PDB Code 1i9a Chain A, B click to enlarge Title STRUCTURAL STUDIES OF CHOLESTEROL BIOSYNTHESIS: MEVALONATE 5-DIPHOSPHATE DECARBOXYLASE AND ISOPENTENYL DIPHOSPHATE ISOMERASE Classification ISOMERASE Compound ISOPENTENYL-DIPHOSPHATE DELTA-ISOMERASE Source (IDI_ECOLI) Sequence A:  EHVILLNAQGVPTGTLEKYAAHTADTRLHLAFSSWLFNAK GQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAVIRR CRYELGVEITPPESIYPDFRYRATDPSGIVENEVCPVFAA RTTSALQINDDEVXDYQWCDLADVLHGIDATPWAFSPWXV XQATNREARKRLSAFTQL B:  EHVILLNAQGVPTGTLEKYAAHTADTRLHLAFSSWLFNAK GQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAVIRR CRYELGVEITPPESIYPDFRYRATDPSGIVENEVCPVFAA RTTSALQINDDEVXDYQWCDLADVLHGIDATPWAFSPWXV XQATNREARKRLSAFTQL Description (1)  ISOPENTENYL DIPHOSPHATE: DIMETHYLALLYL DIPHOSPHATE DELTA ISOMERASE Functional site 1) chain A residue 25 type sequence H description BINDING SITE FOR RESIDUE MN A 1001 source : AC1 2) chain A residue 32 type sequence H description BINDING SITE FOR RESIDUE MN A 1001 source : AC1 3) chain A residue 69 type sequence H description BINDING SITE FOR RESIDUE MN A 1001 source : AC1 4) chain A residue 114 type sequence E description BINDING SITE FOR RESIDUE MN A 1001 source : AC1 5) chain A residue 116 type sequence E description BINDING SITE FOR RESIDUE MN A 1001 source : AC1 6) chain B residue 1025 type sequence H description BINDING SITE FOR RESIDUE MN B 2001 source : AC2 7) chain B residue 1032 type sequence H description BINDING SITE FOR RESIDUE MN B 2001 source : AC2 8) chain B residue 1069 type sequence H description BINDING SITE FOR RESIDUE MN B 2001 source : AC2 9) chain B residue 1114 type sequence E description BINDING SITE FOR RESIDUE MN B 2001 source : AC2 10) chain B residue 1116 type sequence E description BINDING SITE FOR RESIDUE MN B 2001 source : AC2 11) chain A residue 25 type catalytic sequence H description 190 source MCSA : MCSA1 12) chain A residue 32 type catalytic sequence H description 190 source MCSA : MCSA1 13) chain A residue 67 type catalytic sequence C description 190 source MCSA : MCSA1 14) chain A residue 69 type catalytic sequence H description 190 source MCSA : MCSA1 15) chain A residue 87 type catalytic sequence E description 190 source MCSA : MCSA1 16) chain A residue 104 type catalytic sequence Y description 190 source MCSA : MCSA1 17) chain A residue 114 type catalytic sequence E description 190 source MCSA : MCSA1 18) chain A residue 116 type catalytic sequence E description 190 source MCSA : MCSA1 19) chain A residue 161 type catalytic sequence W description 190 source MCSA : MCSA1 20) chain B residue 1025 type catalytic sequence H description 190 source MCSA : MCSA2 21) chain B residue 1032 type catalytic sequence H description 190 source MCSA : MCSA2 22) chain B residue 1067 type catalytic sequence C description 190 source MCSA : MCSA2 23) chain B residue 1069 type catalytic sequence H description 190 source MCSA : MCSA2 24) chain B residue 1087 type catalytic sequence E description 190 source MCSA : MCSA2 25) chain B residue 1104 type catalytic sequence Y description 190 source MCSA : MCSA2 26) chain B residue 1114 type catalytic sequence E description 190 source MCSA : MCSA2 27) chain B residue 1116 type catalytic sequence E description 190 source MCSA : MCSA2 28) chain B residue 1161 type catalytic sequence W description 190 source MCSA : MCSA2 29) chain A residue 21 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 30) chain B residue 1055 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 31) chain B residue 1067 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 32) chain B residue 1069 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 33) chain B residue 1083 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 34) chain B residue 1087 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 35) chain A residue 51 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 36) chain A residue 55 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 37) chain A residue 67 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 38) chain A residue 69 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 39) chain A residue 83 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 40) chain A residue 87 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 41) chain B residue 1021 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 42) chain B residue 1051 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 43) chain A residue 25 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12630859, ECO:0000269|PubMed:15643873 source Swiss-Prot : SWS_FT_FI3 44) chain A residue 32 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12630859, ECO:0000269|PubMed:15643873 source Swiss-Prot : SWS_FT_FI3 45) chain A residue 114 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12630859, ECO:0000269|PubMed:15643873 source Swiss-Prot : SWS_FT_FI3 46) chain A residue 116 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12630859, ECO:0000269|PubMed:15643873 source Swiss-Prot : SWS_FT_FI3 47) chain B residue 1025 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12630859, ECO:0000269|PubMed:15643873 source Swiss-Prot : SWS_FT_FI3 48) chain B residue 1032 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12630859, ECO:0000269|PubMed:15643873 source Swiss-Prot : SWS_FT_FI3 49) chain B residue 1114 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12630859, ECO:0000269|PubMed:15643873 source Swiss-Prot : SWS_FT_FI3 50) chain B residue 1116 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12630859, ECO:0000269|PubMed:15643873 source Swiss-Prot : SWS_FT_FI3 51) chain A residue 104 type SITE sequence Y description Essential for catalytic activity source Swiss-Prot : SWS_FT_FI4 52) chain B residue 1104 type SITE sequence Y description Essential for catalytic activity source Swiss-Prot : SWS_FT_FI4 53) chain A residue 67 type ACT_SITE sequence C description source Swiss-Prot : SWS_FT_FI1 54) chain A residue 116 type ACT_SITE sequence E description source Swiss-Prot : SWS_FT_FI1 55) chain B residue 1067 type ACT_SITE sequence C description source Swiss-Prot : SWS_FT_FI1 56) chain B residue 1116 type ACT_SITE sequence E description source Swiss-Prot : SWS_FT_FI1

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