eF-site ID 1i9a-A PDB Code 1i9a Chain A 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 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 A residue 25 type catalytic sequence H description 190 source MCSA : MCSA1 7) chain A residue 32 type catalytic sequence H description 190 source MCSA : MCSA1 8) chain A residue 67 type catalytic sequence C description 190 source MCSA : MCSA1 9) chain A residue 69 type catalytic sequence H description 190 source MCSA : MCSA1 10) chain A residue 87 type catalytic sequence E description 190 source MCSA : MCSA1 11) chain A residue 104 type catalytic sequence Y description 190 source MCSA : MCSA1 12) chain A residue 114 type catalytic sequence E description 190 source MCSA : MCSA1 13) chain A residue 116 type catalytic sequence E description 190 source MCSA : MCSA1 14) chain A residue 161 type catalytic sequence W description 190 source MCSA : MCSA1 15) chain A residue 21 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 16) chain A residue 51 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 17) chain A residue 55 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 18) chain A residue 67 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 19) chain A residue 69 type BINDING sequence H description source Swiss-Prot : SWS_FT_FI2 20) chain A residue 83 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 21) chain A residue 87 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI2 22) chain A residue 25 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12630859, ECO:0000269|PubMed:15643873 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 32 type BINDING sequence H description BINDING => ECO:0000269|PubMed:12630859, ECO:0000269|PubMed:15643873 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 114 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12630859, ECO:0000269|PubMed:15643873 source Swiss-Prot : SWS_FT_FI3 25) chain A residue 116 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12630859, ECO:0000269|PubMed:15643873 source Swiss-Prot : SWS_FT_FI3 26) chain A residue 104 type SITE sequence Y description Essential for catalytic activity source Swiss-Prot : SWS_FT_FI4 27) chain A residue 67 type ACT_SITE sequence C description source Swiss-Prot : SWS_FT_FI1 28) chain A residue 116 type ACT_SITE sequence E description source Swiss-Prot : SWS_FT_FI1

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