eF-site ID 1i9a-B PDB Code 1i9a Chain 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 B:  EHVILLNAQGVPTGTLEKYAAHTADTRLHLAFSSWLFNAK GQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAVIRR CRYELGVEITPPESIYPDFRYRATDPSGIVENEVCPVFAA RTTSALQINDDEVXDYQWCDLADVLHGIDATPWAFSPWXV XQATNREARKRLSAFTQL Description (1)  ISOPENTENYL DIPHOSPHATE: DIMETHYLALLYL DIPHOSPHATE DELTA ISOMERASE Functional site 1) chain B residue 1025 type sequence H description BINDING SITE FOR RESIDUE MN B 2001 source : AC2 2) chain B residue 1032 type sequence H description BINDING SITE FOR RESIDUE MN B 2001 source : AC2 3) chain B residue 1069 type sequence H description BINDING SITE FOR RESIDUE MN B 2001 source : AC2 4) chain B residue 1114 type sequence E description BINDING SITE FOR RESIDUE MN B 2001 source : AC2 5) chain B residue 1116 type sequence E description BINDING SITE FOR RESIDUE MN B 2001 source : AC2 6) chain B residue 1025 type catalytic sequence H description 190 source MCSA : MCSA2 7) chain B residue 1032 type catalytic sequence H description 190 source MCSA : MCSA2 8) chain B residue 1067 type catalytic sequence C description 190 source MCSA : MCSA2 9) chain B residue 1069 type catalytic sequence H description 190 source MCSA : MCSA2 10) chain B residue 1087 type catalytic sequence E description 190 source MCSA : MCSA2 11) chain B residue 1104 type catalytic sequence Y description 190 source MCSA : MCSA2 12) chain B residue 1114 type catalytic sequence E description 190 source MCSA : MCSA2 13) chain B residue 1116 type catalytic sequence E description 190 source MCSA : MCSA2 14) chain B residue 1161 type catalytic sequence W description 190 source MCSA : MCSA2 15) chain B residue 1055 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 16) chain B residue 1067 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 17) chain B residue 1069 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 18) chain B residue 1083 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 19) chain B residue 1087 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 20) chain B residue 1021 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 21) chain B residue 1051 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 22) chain B residue 1025 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12630859, ECO:0000269|PubMed:15643873 source Swiss-Prot : SWS_FT_FI3 23) chain B residue 1032 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12630859, ECO:0000269|PubMed:15643873 source Swiss-Prot : SWS_FT_FI3 24) chain B residue 1114 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12630859, ECO:0000269|PubMed:15643873 source Swiss-Prot : SWS_FT_FI3 25) chain B residue 1116 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12630859, ECO:0000269|PubMed:15643873 source Swiss-Prot : SWS_FT_FI3 26) chain B residue 1104 type SITE sequence Y description Essential for catalytic activity source Swiss-Prot : SWS_FT_FI4 27) chain B residue 1067 type ACT_SITE sequence C description source Swiss-Prot : SWS_FT_FI1 28) chain B residue 1116 type ACT_SITE sequence E description source Swiss-Prot : SWS_FT_FI1

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