eF-site ID 3cd5-ABCD PDB Code 3cd5 Chain A, B, C, D click to enlarge Title Thermodynamic and structure guided design of statin hmg-coa reductase inhibitors Classification OXIDOREDUCTASE Compound 3-hydroxy-3-methylglutaryl-coenzyme A reductase Source Homo sapiens (Human) (HMDH_HUMAN) Sequence A:  EPRPNEECLQILGNAEKGAKFLSDAEIIQLVNAKHIPAYK LETLIETHERGVSIRRQLLSKKLSEPSSLQYLPYRDYNYS LVMGACCENVIGYMPIPVGVAGPLCLDEKEFQVPMATTEG CLVASTNRGCRAIGLGGGASSRVLADGMTRGPVVRLPRAC DSAEVKAWLETSEGFAVIKEAFDSTSRFARLQKLHTSIAG RNLYIRFQSRSGDAMGMNMISKGTEKALSKLHEYFPEMQI LAVSGNYCTDKKPAAINWIEGRGKSVVCEAVIPAKVVREV LKTTTEAMIEVNINKNLVGSAMAGSIGGYNAHAANIVTAI YIACGQDAAQNVGSSNCITLMEASGPTNEDLYISCTMPSI EIGTVGGGTNLLPQQACLQMLGVQGACKDNPGENARQLAR IVCGTVMAGELSLMAALAAGHLVKS B:  EPRPNEECLQILGNAEKGAKFLSDAEIIQLVNAKHIPAYK LETLIETHERGVSIRRQLLSKKLSEPSSLQYLPYRDYNYS LVMGACCENVIGYMPIPVGVAGPLCLDEKEFQVPMATTEG CLVASTNRGCRAIGLGGGASSRVLADGMTRGPVVRLPRAC DSAEVKAWLETSEGFAVIKEAFDSTSRFARLQKLHTSIAG RNLYIRFQSRSGDAMGMNMISKGTEKALSKLHEYFPEMQI LAVSGNYCTDKKPAAINWIEGRGKSVVCEAVIPAKVVREV LKTTTEAMIEVNINKNLVGSAMAGSIGGYNAHAANIVTAI YIACGQDAAQNVGSSNCITLMEASGPTNEDLYISCTMPSI EIGTVGGGTNLLPQQACLQMLGVQGACKDNPGENARQLAR IVCGTVMAGELSLMAALAAGHLVKS C:  PNEECLQILGNGAKFLSDAEIIQLVNAKHIPAYKLETLIE THERGVSIRRQLLSKKLSEPSSLQYLPYRDYNYSLVMGAC CENVIGYMPIPVGVAGPLCLDEKEFQVPMATTEGCLVAST NRGCRAIGLGGGASSRVLADGMTRGPVVRLPRACDSAEVK AWLETSEGFAVIKEAFDSTSRFARLQKLHTSIAGRNLYIR FQSRSGDAMGMNMISKGTEKALSKLHEYFPEMQILAVSGN YCTDKKPAAINWIEGRGKSVVCEAVIPAKVVREVLKTTTE AMIEVNINKNLVGSAMAGSIGGYNAHAANIVTAIYIACGQ DAAQNVGSSNCITLMEASGPTNEDLYISCTMPSIEIGTVG GGTNLLPQQACLQMLGVQGACKDNPGENARQLARIVCGTV MAGELSLMAALAAGHLVK D:  PRPNEECLQGAKFLSDAEIIQLVNAKHIPAYKLETLIETH ERGVSIRRQLLSKKLSEPSSLQYLPYRDYNYSLVMGACCE NVIGYMPIPVGVAGPLCLDEKEFQVPMATTEGCLVASTNR GCRAIGLGGGASSRVLADGMTRGPVVRLPRACDSAEVKAW LETSEGFAVIKEAFDSTSRFARLQKLHTSIAGRNLYIRFQ SRSGDAMGMNMISKGTEKALSKLHEYFPEMQILAVSGNYC TDKKPAAINWIEGRGKSVVCEAVIPAKVVREVLKTTTEAM IEVNINKNLVGSAMAGSIGGYNAHAANIVTAIYIACGQDA AQNVGSSNCITLMEASGPTNEDLYISCTMPSIEIGTVGGG TNLLPQQACLQMLGVQGACKDNPGENARQLARIVCGTVMA GELSLMAALAAGHLVK Description Functional site 1) chain A residue 654 type sequence A description BINDING SITE FOR RESIDUE SO4 A 1 source : AC1 2) chain A residue 655 type sequence M description BINDING SITE FOR RESIDUE SO4 A 1 source : AC1 3) chain A residue 656 type sequence G description BINDING SITE FOR RESIDUE SO4 A 1 source : AC1 4) chain A residue 657 type sequence M description BINDING SITE FOR RESIDUE SO4 A 1 source : AC1 5) chain A residue 658 type sequence N description BINDING SITE FOR RESIDUE SO4 A 1 source : AC1 6) chain B residue 655 type sequence M description BINDING SITE FOR RESIDUE SO4 B 2 source : AC2 7) chain B residue 656 type sequence G description BINDING SITE FOR RESIDUE SO4 B 2 source : AC2 8) chain B residue 657 type sequence M description BINDING SITE FOR RESIDUE SO4 B 2 source : AC2 9) chain B residue 658 type sequence N description BINDING SITE FOR RESIDUE SO4 B 2 source : AC2 10) chain C residue 654 type sequence A description BINDING SITE FOR RESIDUE SO4 C 3 source : AC3 11) chain C residue 655 type sequence M description BINDING SITE FOR RESIDUE SO4 C 3 source : AC3 12) chain C residue 656 type sequence G description BINDING SITE FOR RESIDUE SO4 C 3 source : AC3 13) chain C residue 657 type sequence M description BINDING SITE FOR RESIDUE SO4 C 3 source : AC3 14) chain C residue 658 type sequence N description BINDING SITE FOR RESIDUE SO4 C 3 source : AC3 15) chain D residue 654 type sequence A description BINDING SITE FOR RESIDUE SO4 D 4 source : AC4 16) chain D residue 655 type sequence M description BINDING SITE FOR RESIDUE SO4 D 4 source : AC4 17) chain D residue 656 type sequence G description BINDING SITE FOR RESIDUE SO4 D 4 source : AC4 18) chain D residue 657 type sequence M description BINDING SITE FOR RESIDUE SO4 D 4 source : AC4 19) chain D residue 658 type sequence N description BINDING SITE FOR RESIDUE SO4 D 4 source : AC4 20) chain A residue 590 type sequence R description BINDING SITE FOR RESIDUE 7HI B 1 source : AC5 21) chain A residue 657 type sequence M description BINDING SITE FOR RESIDUE 7HI B 1 source : AC5 22) chain A residue 684 type sequence S description BINDING SITE FOR RESIDUE 7HI B 1 source : AC5 23) chain A residue 686 type sequence N description BINDING SITE FOR RESIDUE 7HI B 1 source : AC5 24) chain A residue 690 type sequence D description BINDING SITE FOR RESIDUE 7HI B 1 source : AC5 25) chain A residue 691 type sequence K description BINDING SITE FOR RESIDUE 7HI B 1 source : AC5 26) chain A residue 692 type sequence K description BINDING SITE FOR RESIDUE 7HI B 1 source : AC5 27) chain B residue 559 type sequence E description BINDING SITE FOR RESIDUE 7HI B 1 source : AC5 28) chain B residue 564 type sequence A description BINDING SITE FOR RESIDUE 7HI B 1 source : AC5 29) chain B residue 565 type sequence S description BINDING SITE FOR RESIDUE 7HI B 1 source : AC5 30) chain B residue 568 type sequence R description BINDING SITE FOR RESIDUE 7HI B 1 source : AC5 31) chain B residue 735 type sequence K description BINDING SITE FOR RESIDUE 7HI B 1 source : AC5 32) chain B residue 751 type sequence A description BINDING SITE FOR RESIDUE 7HI B 1 source : AC5 33) chain B residue 752 type sequence H description BINDING SITE FOR RESIDUE 7HI B 1 source : AC5 34) chain B residue 755 type sequence N description BINDING SITE FOR RESIDUE 7HI B 1 source : AC5 35) chain B residue 853 type sequence L description BINDING SITE FOR RESIDUE 7HI B 1 source : AC5 36) chain B residue 857 type sequence L description BINDING SITE FOR RESIDUE 7HI B 1 source : AC5 37) chain A residue 559 type sequence E description BINDING SITE FOR RESIDUE 7HI A 2 source : AC6 38) chain A residue 564 type sequence A description BINDING SITE FOR RESIDUE 7HI A 2 source : AC6 39) chain A residue 565 type sequence S description BINDING SITE FOR RESIDUE 7HI A 2 source : AC6 40) chain A residue 568 type sequence R description BINDING SITE FOR RESIDUE 7HI A 2 source : AC6 41) chain A residue 735 type sequence K description BINDING SITE FOR RESIDUE 7HI A 2 source : AC6 42) chain A residue 751 type sequence A description BINDING SITE FOR RESIDUE 7HI A 2 source : AC6 43) chain A residue 752 type sequence H description BINDING SITE FOR RESIDUE 7HI A 2 source : AC6 44) chain A residue 755 type sequence N description BINDING SITE FOR RESIDUE 7HI A 2 source : AC6 45) chain A residue 853 type sequence L description BINDING SITE FOR RESIDUE 7HI A 2 source : AC6 46) chain A residue 857 type sequence L description BINDING SITE FOR RESIDUE 7HI A 2 source : AC6 47) chain A residue 861 type sequence H description BINDING SITE FOR RESIDUE 7HI A 2 source : AC6 48) chain B residue 590 type sequence R description BINDING SITE FOR RESIDUE 7HI A 2 source : AC6 49) chain B residue 657 type sequence M description BINDING SITE FOR RESIDUE 7HI A 2 source : AC6 50) chain B residue 684 type sequence S description BINDING SITE FOR RESIDUE 7HI A 2 source : AC6 51) chain B residue 690 type sequence D description BINDING SITE FOR RESIDUE 7HI A 2 source : AC6 52) chain B residue 691 type sequence K description BINDING SITE FOR RESIDUE 7HI A 2 source : AC6 53) chain B residue 692 type sequence K description BINDING SITE FOR RESIDUE 7HI A 2 source : AC6 54) chain C residue 590 type sequence R description BINDING SITE FOR RESIDUE 7HI D 3 source : AC7 55) chain C residue 684 type sequence S description BINDING SITE FOR RESIDUE 7HI D 3 source : AC7 56) chain C residue 686 type sequence N description BINDING SITE FOR RESIDUE 7HI D 3 source : AC7 57) chain C residue 690 type sequence D description BINDING SITE FOR RESIDUE 7HI D 3 source : AC7 58) chain C residue 691 type sequence K description BINDING SITE FOR RESIDUE 7HI D 3 source : AC7 59) chain C residue 692 type sequence K description BINDING SITE FOR RESIDUE 7HI D 3 source : AC7 60) chain D residue 559 type sequence E description BINDING SITE FOR RESIDUE 7HI D 3 source : AC7 61) chain D residue 564 type sequence A description BINDING SITE FOR RESIDUE 7HI D 3 source : AC7 62) chain D residue 565 type sequence S description BINDING SITE FOR RESIDUE 7HI D 3 source : AC7 63) chain D residue 568 type sequence R description BINDING SITE FOR RESIDUE 7HI D 3 source : AC7 64) chain D residue 735 type sequence K description BINDING SITE FOR RESIDUE 7HI D 3 source : AC7 65) chain D residue 751 type sequence A description BINDING SITE FOR RESIDUE 7HI D 3 source : AC7 66) chain D residue 752 type sequence H description BINDING SITE FOR RESIDUE 7HI D 3 source : AC7 67) chain D residue 755 type sequence N description BINDING SITE FOR RESIDUE 7HI D 3 source : AC7 68) chain D residue 852 type sequence S description BINDING SITE FOR RESIDUE 7HI D 3 source : AC7 69) chain D residue 853 type sequence L description BINDING SITE FOR RESIDUE 7HI D 3 source : AC7 70) chain D residue 861 type sequence H description BINDING SITE FOR RESIDUE 7HI D 3 source : AC7 71) chain D residue 864 type sequence K description BINDING SITE FOR RESIDUE 7HI D 3 source : AC7 72) chain C residue 559 type sequence E description BINDING SITE FOR RESIDUE 7HI D 876 source : AC8 73) chain C residue 564 type sequence A description BINDING SITE FOR RESIDUE 7HI D 876 source : AC8 74) chain C residue 565 type sequence S description BINDING SITE FOR RESIDUE 7HI D 876 source : AC8 75) chain C residue 568 type sequence R description BINDING SITE FOR RESIDUE 7HI D 876 source : AC8 76) chain C residue 735 type sequence K description BINDING SITE FOR RESIDUE 7HI D 876 source : AC8 77) chain C residue 751 type sequence A description BINDING SITE FOR RESIDUE 7HI D 876 source : AC8 78) chain C residue 752 type sequence H description BINDING SITE FOR RESIDUE 7HI D 876 source : AC8 79) chain C residue 755 type sequence N description BINDING SITE FOR RESIDUE 7HI D 876 source : AC8 80) chain C residue 853 type sequence L description BINDING SITE FOR RESIDUE 7HI D 876 source : AC8 81) chain C residue 857 type sequence L description BINDING SITE FOR RESIDUE 7HI D 876 source : AC8 82) chain C residue 864 type sequence K description BINDING SITE FOR RESIDUE 7HI D 876 source : AC8 83) chain D residue 590 type sequence R description BINDING SITE FOR RESIDUE 7HI D 876 source : AC8 84) chain D residue 684 type sequence S description BINDING SITE FOR RESIDUE 7HI D 876 source : AC8 85) chain D residue 686 type sequence N description BINDING SITE FOR RESIDUE 7HI D 876 source : AC8 86) chain D residue 690 type sequence D description BINDING SITE FOR RESIDUE 7HI D 876 source : AC8 87) chain D residue 691 type sequence K description BINDING SITE FOR RESIDUE 7HI D 876 source : AC8 88) chain D residue 692 type sequence K description BINDING SITE FOR RESIDUE 7HI D 876 source : AC8 89) chain A residue 559 type catalytic sequence E description 93 source MCSA : MCSA1 90) chain A residue 691 type catalytic sequence K description 93 source MCSA : MCSA1 91) chain A residue 767 type catalytic sequence D description 93 source MCSA : MCSA1 92) chain B residue 559 type catalytic sequence E description 93 source MCSA : MCSA2 93) chain B residue 691 type catalytic sequence K description 93 source MCSA : MCSA2 94) chain B residue 767 type catalytic sequence D description 93 source MCSA : MCSA2 95) chain C residue 559 type catalytic sequence E description 93 source MCSA : MCSA3 96) chain C residue 691 type catalytic sequence K description 93 source MCSA : MCSA3 97) chain C residue 767 type catalytic sequence D description 93 source MCSA : MCSA3 98) chain D residue 559 type catalytic sequence E description 93 source MCSA : MCSA4 99) chain D residue 691 type catalytic sequence K description 93 source MCSA : MCSA4 100) chain D residue 767 type catalytic sequence D description 93 source MCSA : MCSA4 101) chain A residue 559 type ACT_SITE sequence E description Charge relay system => ECO:0000303|PubMed:10698924, ECO:0000303|PubMed:11349148 source Swiss-Prot : SWS_FT_FI1 102) chain D residue 559 type ACT_SITE sequence E description Charge relay system => ECO:0000303|PubMed:10698924, ECO:0000303|PubMed:11349148 source Swiss-Prot : SWS_FT_FI1 103) chain D residue 691 type ACT_SITE sequence K description Charge relay system => ECO:0000303|PubMed:10698924, ECO:0000303|PubMed:11349148 source Swiss-Prot : SWS_FT_FI1 104) chain D residue 767 type ACT_SITE sequence D description Charge relay system => ECO:0000303|PubMed:10698924, ECO:0000303|PubMed:11349148 source Swiss-Prot : SWS_FT_FI1 105) chain A residue 691 type ACT_SITE sequence K description Charge relay system => ECO:0000303|PubMed:10698924, ECO:0000303|PubMed:11349148 source Swiss-Prot : SWS_FT_FI1 106) chain A residue 767 type ACT_SITE sequence D description Charge relay system => ECO:0000303|PubMed:10698924, ECO:0000303|PubMed:11349148 source Swiss-Prot : SWS_FT_FI1 107) chain B residue 559 type ACT_SITE sequence E description Charge relay system => ECO:0000303|PubMed:10698924, ECO:0000303|PubMed:11349148 source Swiss-Prot : SWS_FT_FI1 108) chain B residue 691 type ACT_SITE sequence K description Charge relay system => ECO:0000303|PubMed:10698924, ECO:0000303|PubMed:11349148 source Swiss-Prot : SWS_FT_FI1 109) chain B residue 767 type ACT_SITE sequence D description Charge relay system => ECO:0000303|PubMed:10698924, ECO:0000303|PubMed:11349148 source Swiss-Prot : SWS_FT_FI1 110) chain C residue 559 type ACT_SITE sequence E description Charge relay system => ECO:0000303|PubMed:10698924, ECO:0000303|PubMed:11349148 source Swiss-Prot : SWS_FT_FI1 111) chain C residue 691 type ACT_SITE sequence K description Charge relay system => ECO:0000303|PubMed:10698924, ECO:0000303|PubMed:11349148 source Swiss-Prot : SWS_FT_FI1 112) chain C residue 767 type ACT_SITE sequence D description Charge relay system => ECO:0000303|PubMed:10698924, ECO:0000303|PubMed:11349148 source Swiss-Prot : SWS_FT_FI1 113) chain A residue 646-660 type prosite sequence RFQSRSGDAMGMNMI description HMG_COA_REDUCTASE_1 Hydroxymethylglutaryl-coenzyme A reductases signature 1. RfQSrSGDaMGmNmI source prosite : PS00066 114) chain A residue 802-809 type prosite sequence IGTVGGGT description HMG_COA_REDUCTASE_2 Hydroxymethylglutaryl-coenzyme A reductases signature 2. IGtVGGGT source prosite : PS00318 115) chain A residue 565 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 116) chain B residue 720 type BINDING sequence V description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 117) chain B residue 865 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 118) chain C residue 565 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 119) chain C residue 626 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 120) chain C residue 653 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 121) chain C residue 720 type BINDING sequence V description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 122) chain D residue 565 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 123) chain A residue 626 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 124) chain D residue 626 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 125) chain D residue 653 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 126) chain D residue 720 type BINDING sequence V description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 127) chain A residue 653 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 128) chain A residue 720 type BINDING sequence V description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 129) chain A residue 865 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 130) chain B residue 565 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 131) chain B residue 626 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 132) chain B residue 653 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 133) chain A residue 504 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI4 134) chain B residue 504 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI4 135) chain C residue 504 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI4 136) chain D residue 504 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI4

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