eF-site ID 3cct-ABCD PDB Code 3cct 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 IVCGTVMAGELSLMAALAAGH B:  EPRPNEECLQILGNAEKGAKFLSDAEIIQLVNAKHIPAYK LETLIETHERGVSIRRQLLSKKLSEPSSLQYLPYRDYNYS LVMGACCENVIGYMPIPVGVAGPLCLDEKEFQVPMATTEG CLVASTNRGCRAIGLGGGASSRVLADGMTRGPVVRLPRAC DSAEVKAWLETSEGFAVIKEAFDSTSRFARLQKLHTSIAG RNLYIRFQSRSGDAMGMNMISKGTEKALSKLHEYFPEMQI LAVSGNYCTDKKPAAINWIEGRGKSVVCEAVIPAKVVREV LKTTTEAMIEVNINKNLVGSAMAGSIGGYNAHAANIVTAI YIACGQDAAQNVGSSNCITLMEASGPTNEDLYISCTMPSI EIGTVGGGTNLLPQQACLQMLGVQGACKDNPGENARQLAR IVCGTVMAGELSLMAALAAGH C:  PNEECLQILGNAEKGAKFLSDAEIIQLVNAKHIPAYKLET LIETHERGVSIRRQLLSKKLSEPSSLQYLPYRDYNYSLVM GACCENVIGYMPIPVGVAGPLCLDEKEFQVPMATTEGCLV ASTNRGCRAIGLGGGASSRVLADGMTRGPVVRLPRACDSA EVKAWLETSEGFAVIKEAFDSTSRFARLQKLHTSIAGRNL YIRFQSRSGDAMGMNMISKGTEKALSKLHEYFPEMQILAV SGNYCTDKKPAAINWIEGRGKSVVCEAVIPAKVVREVLKT TTEAMIEVNINKNLVGSAMAGSIGGYNAHAANIVTAIYIA CGQDAAQNVGSSNCITLMEASGPTNEDLYISCTMPSIEIG TVGGGTNLLPQQACLQMLGVQGACKDNPGENARQLARIVC GTVMAGELSLMAALAAG D:  GAKFLSDAEIIQLVNAKHLIETHERGVSIRRQLLSKKLSE PSSLQYLPYRDYNYSLVMGACCENVIGYMPIPVGVAGPLC LDEKEFQVPMATTEGCLVASTNRGCRAIGLGGGASSRVLA DGMTRGPVVRLPRACDSAEVKAWLETSEGFAVIKEAFDST SRFARLQKLHTSIAGRNLYIRFQSRSGDAMGMNMISKGTE KALSKLHEYFPEMQILAVSGNYCTDKKPAAINWIEGRGKS VVCEAVIPAKVVREVLKTTTEAMIEVNINKNLVGSAMAGS IGGYNAHAANIVTAIYIACGQDAAQNVGSSNCITLMEASG PTNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQMLGVQG ACKDNPGENARQLARIVCGTVMAGELSLMAALAA Description Functional site 1) chain A residue 559 type sequence E description BINDING SITE FOR RESIDUE 3HI B 1 source : AC1 2) chain A residue 560 type sequence G description BINDING SITE FOR RESIDUE 3HI B 1 source : AC1 3) chain A residue 562 type sequence L description BINDING SITE FOR RESIDUE 3HI B 1 source : AC1 4) chain A residue 565 type sequence S description BINDING SITE FOR RESIDUE 3HI B 1 source : AC1 5) chain A residue 568 type sequence R description BINDING SITE FOR RESIDUE 3HI B 1 source : AC1 6) chain A residue 735 type sequence K description BINDING SITE FOR RESIDUE 3HI B 1 source : AC1 7) chain A residue 751 type sequence A description BINDING SITE FOR RESIDUE 3HI B 1 source : AC1 8) chain A residue 752 type sequence H description BINDING SITE FOR RESIDUE 3HI B 1 source : AC1 9) chain A residue 755 type sequence N description BINDING SITE FOR RESIDUE 3HI B 1 source : AC1 10) chain A residue 853 type sequence L description BINDING SITE FOR RESIDUE 3HI B 1 source : AC1 11) chain A residue 856 type sequence A description BINDING SITE FOR RESIDUE 3HI B 1 source : AC1 12) chain A residue 857 type sequence L description BINDING SITE FOR RESIDUE 3HI B 1 source : AC1 13) chain B residue 590 type sequence R description BINDING SITE FOR RESIDUE 3HI B 1 source : AC1 14) chain B residue 657 type sequence M description BINDING SITE FOR RESIDUE 3HI B 1 source : AC1 15) chain B residue 661 type sequence S description BINDING SITE FOR RESIDUE 3HI B 1 source : AC1 16) chain B residue 684 type sequence S description BINDING SITE FOR RESIDUE 3HI B 1 source : AC1 17) chain B residue 690 type sequence D description BINDING SITE FOR RESIDUE 3HI B 1 source : AC1 18) chain B residue 691 type sequence K description BINDING SITE FOR RESIDUE 3HI B 1 source : AC1 19) chain B residue 692 type sequence K description BINDING SITE FOR RESIDUE 3HI B 1 source : AC1 20) chain A residue 590 type sequence R description BINDING SITE FOR RESIDUE 3HI B 2 source : AC2 21) chain A residue 657 type sequence M description BINDING SITE FOR RESIDUE 3HI B 2 source : AC2 22) chain A residue 661 type sequence S description BINDING SITE FOR RESIDUE 3HI B 2 source : AC2 23) chain A residue 684 type sequence S description BINDING SITE FOR RESIDUE 3HI B 2 source : AC2 24) chain A residue 690 type sequence D description BINDING SITE FOR RESIDUE 3HI B 2 source : AC2 25) chain A residue 691 type sequence K description BINDING SITE FOR RESIDUE 3HI B 2 source : AC2 26) chain A residue 692 type sequence K description BINDING SITE FOR RESIDUE 3HI B 2 source : AC2 27) chain B residue 559 type sequence E description BINDING SITE FOR RESIDUE 3HI B 2 source : AC2 28) chain B residue 561 type sequence C description BINDING SITE FOR RESIDUE 3HI B 2 source : AC2 29) chain B residue 562 type sequence L description BINDING SITE FOR RESIDUE 3HI B 2 source : AC2 30) chain B residue 565 type sequence S description BINDING SITE FOR RESIDUE 3HI B 2 source : AC2 31) chain B residue 568 type sequence R description BINDING SITE FOR RESIDUE 3HI B 2 source : AC2 32) chain B residue 735 type sequence K description BINDING SITE FOR RESIDUE 3HI B 2 source : AC2 33) chain B residue 751 type sequence A description BINDING SITE FOR RESIDUE 3HI B 2 source : AC2 34) chain B residue 752 type sequence H description BINDING SITE FOR RESIDUE 3HI B 2 source : AC2 35) chain B residue 755 type sequence N description BINDING SITE FOR RESIDUE 3HI B 2 source : AC2 36) chain B residue 853 type sequence L description BINDING SITE FOR RESIDUE 3HI B 2 source : AC2 37) chain B residue 856 type sequence A description BINDING SITE FOR RESIDUE 3HI B 2 source : AC2 38) chain C residue 559 type sequence E description BINDING SITE FOR RESIDUE 3HI D 3 source : AC3 39) chain C residue 560 type sequence G description BINDING SITE FOR RESIDUE 3HI D 3 source : AC3 40) chain C residue 561 type sequence C description BINDING SITE FOR RESIDUE 3HI D 3 source : AC3 41) chain C residue 565 type sequence S description BINDING SITE FOR RESIDUE 3HI D 3 source : AC3 42) chain C residue 568 type sequence R description BINDING SITE FOR RESIDUE 3HI D 3 source : AC3 43) chain C residue 735 type sequence K description BINDING SITE FOR RESIDUE 3HI D 3 source : AC3 44) chain C residue 751 type sequence A description BINDING SITE FOR RESIDUE 3HI D 3 source : AC3 45) chain C residue 752 type sequence H description BINDING SITE FOR RESIDUE 3HI D 3 source : AC3 46) chain C residue 755 type sequence N description BINDING SITE FOR RESIDUE 3HI D 3 source : AC3 47) chain C residue 853 type sequence L description BINDING SITE FOR RESIDUE 3HI D 3 source : AC3 48) chain C residue 856 type sequence A description BINDING SITE FOR RESIDUE 3HI D 3 source : AC3 49) chain D residue 590 type sequence R description BINDING SITE FOR RESIDUE 3HI D 3 source : AC3 50) chain D residue 661 type sequence S description BINDING SITE FOR RESIDUE 3HI D 3 source : AC3 51) chain D residue 684 type sequence S description BINDING SITE FOR RESIDUE 3HI D 3 source : AC3 52) chain D residue 686 type sequence N description BINDING SITE FOR RESIDUE 3HI D 3 source : AC3 53) chain D residue 690 type sequence D description BINDING SITE FOR RESIDUE 3HI D 3 source : AC3 54) chain D residue 691 type sequence K description BINDING SITE FOR RESIDUE 3HI D 3 source : AC3 55) chain D residue 692 type sequence K description BINDING SITE FOR RESIDUE 3HI D 3 source : AC3 56) chain C residue 590 type sequence R description BINDING SITE FOR RESIDUE 3HI C 4 source : AC4 57) chain C residue 661 type sequence S description BINDING SITE FOR RESIDUE 3HI C 4 source : AC4 58) chain C residue 684 type sequence S description BINDING SITE FOR RESIDUE 3HI C 4 source : AC4 59) chain C residue 686 type sequence N description BINDING SITE FOR RESIDUE 3HI C 4 source : AC4 60) chain C residue 690 type sequence D description BINDING SITE FOR RESIDUE 3HI C 4 source : AC4 61) chain C residue 691 type sequence K description BINDING SITE FOR RESIDUE 3HI C 4 source : AC4 62) chain C residue 692 type sequence K description BINDING SITE FOR RESIDUE 3HI C 4 source : AC4 63) chain D residue 559 type sequence E description BINDING SITE FOR RESIDUE 3HI C 4 source : AC4 64) chain D residue 560 type sequence G description BINDING SITE FOR RESIDUE 3HI C 4 source : AC4 65) chain D residue 561 type sequence C description BINDING SITE FOR RESIDUE 3HI C 4 source : AC4 66) chain D residue 562 type sequence L description BINDING SITE FOR RESIDUE 3HI C 4 source : AC4 67) chain D residue 565 type sequence S description BINDING SITE FOR RESIDUE 3HI C 4 source : AC4 68) chain D residue 568 type sequence R description BINDING SITE FOR RESIDUE 3HI C 4 source : AC4 69) chain D residue 735 type sequence K description BINDING SITE FOR RESIDUE 3HI C 4 source : AC4 70) chain D residue 751 type sequence A description BINDING SITE FOR RESIDUE 3HI C 4 source : AC4 71) chain D residue 752 type sequence H description BINDING SITE FOR RESIDUE 3HI C 4 source : AC4 72) chain D residue 755 type sequence N description BINDING SITE FOR RESIDUE 3HI C 4 source : AC4 73) chain D residue 853 type sequence L description BINDING SITE FOR RESIDUE 3HI C 4 source : AC4 74) chain D residue 856 type sequence A description BINDING SITE FOR RESIDUE 3HI C 4 source : AC4 75) chain A residue 559 type catalytic sequence E description 93 source MCSA : MCSA1 76) chain A residue 691 type catalytic sequence K description 93 source MCSA : MCSA1 77) chain A residue 767 type catalytic sequence D description 93 source MCSA : MCSA1 78) chain B residue 559 type catalytic sequence E description 93 source MCSA : MCSA2 79) chain B residue 691 type catalytic sequence K description 93 source MCSA : MCSA2 80) chain B residue 767 type catalytic sequence D description 93 source MCSA : MCSA2 81) chain C residue 559 type catalytic sequence E description 93 source MCSA : MCSA3 82) chain C residue 691 type catalytic sequence K description 93 source MCSA : MCSA3 83) chain C residue 767 type catalytic sequence D description 93 source MCSA : MCSA3 84) chain D residue 559 type catalytic sequence E description 93 source MCSA : MCSA4 85) chain D residue 691 type catalytic sequence K description 93 source MCSA : MCSA4 86) chain D residue 767 type catalytic sequence D description 93 source MCSA : MCSA4 87) chain A residue 646-660 type prosite sequence RFQSRSGDAMGMNMI description HMG_COA_REDUCTASE_1 Hydroxymethylglutaryl-coenzyme A reductases signature 1. RfQSrSGDaMGmNmI source prosite : PS00066 88) chain A residue 802-809 type prosite sequence IGTVGGGT description HMG_COA_REDUCTASE_2 Hydroxymethylglutaryl-coenzyme A reductases signature 2. IGtVGGGT source prosite : PS00318 89) 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 90) 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 91) 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 92) 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 93) 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 94) 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 95) 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 96) 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 97) 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 98) 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 99) 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 100) 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 101) chain A residue 565 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 102) chain B residue 720 type BINDING sequence V description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 103) chain C residue 565 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 104) chain C residue 626 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 105) chain C residue 653 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 106) chain C residue 720 type BINDING sequence V description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 107) chain D residue 565 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 108) chain A residue 626 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 109) chain D residue 626 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 110) chain D residue 653 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 111) chain D residue 720 type BINDING sequence V description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 112) chain A residue 653 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 113) chain A residue 720 type BINDING sequence V description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 114) chain B residue 565 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 115) chain B residue 626 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 116) chain B residue 653 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 117) chain A residue 504 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI4 118) chain B residue 504 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI4 119) chain C residue 504 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI4 120) 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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