eF-site ID 3ccz-ABCD PDB Code 3ccz 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 IVCGTVMAGELSLMAALAAG B:  EPRPNEECLQILAKFLSDAEIIQLVNAKLIETHERGVSIR RQLLSKKLSEPSSLQYLPYRDYNYSLVMGACCENVIGYMP IPVGVAGPLCLDEKEFQVPMATTEGCLVASTNRGCRAIGL GGGASSRVLADGMTRGPVVRLPRACDSAEVKAWLETSEGF AVIKEAFDSTSRFARLQKLHTSIAGRNLYIRFQSRSGDAM GMNMISKGTEKALSKLHEYFPEMQILAVSGNYCTDKKPAA INWIEGRGKSVVCEAVIPAKVVREVLKTTTEAMIEVNINK NLVGSAMAGSIGGYNAHAANIVTAIYIACGQDAAQNVGSS NCITLMEASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQ ACLQMLGVQGACKDNPGENARQLARIVCGTVMAGELSLMA ALAAG C:  PNEECLQILGNGAKFLSDAEIIQLVETLIETHERGVSIRR QLLSKKLSEPSSLQYLPYRDYNYSLVMGACCENVIGYMPI PVGVAGPLCLDEKEFQVPMATTEGCLVASTNRGCRAIGLG GGASSRVLADGMTRGPVVRLPRACDSAEVKAWLETSEGFA VIKEAFDSTSRFARLQKLHTSIAGRNLYIRFQSRSGDAMG MNMISKGTEKALSKLHEYFPEMQILAVSGNYCTDKKPAAI NWIEGRGKSVVCEAVIPAKVVREVLKTTTEAMIEVNINKN LVGSAMAGSIGGYNAHAANIVTAIYIACGQDAAQNVGSSN CITLMEASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQA CLQMLGVQGACKDNPGENARQLARIVCGTVMAGELSLMAA LAAG D:  GAKFLSDAEIIQLVNETLIETHERGVSIRRQLLSKKLSEP SSLQYLPYRDYNYSLVMGACCENVIGYMPIPVGVAGPLCL DEKEFQVPMATTEGCLVASTNRGCRAIGLGGGASSRVLAD GMTRGPVVRLPRACDSAEVKAWLETSEGFAVIKEAFDSTS RFARLQKLHTSIAGRNLYIRFQSRSGDAMGMNMISKGTEK ALSKLHEYFPEMQILAVSGNYCTDKKPAAINWIEGRGKSV VCEAVIPAKVVREVLKTTTEAMIEVNINKNLVGSAMAGSI GGYNAHAANIVTAIYIACGQDAAQNVGSSNCITLMEASGP TNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQMLGVQGA CKDNPGENARQLARIVCGTVMAGELSLMAALAAG 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 654 type sequence A 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 5HI A 876 source : AC5 21) chain A residue 661 type sequence S description BINDING SITE FOR RESIDUE 5HI A 876 source : AC5 22) chain A residue 684 type sequence S description BINDING SITE FOR RESIDUE 5HI A 876 source : AC5 23) chain A residue 690 type sequence D description BINDING SITE FOR RESIDUE 5HI A 876 source : AC5 24) chain A residue 691 type sequence K description BINDING SITE FOR RESIDUE 5HI A 876 source : AC5 25) chain A residue 692 type sequence K description BINDING SITE FOR RESIDUE 5HI A 876 source : AC5 26) chain B residue 559 type sequence E description BINDING SITE FOR RESIDUE 5HI A 876 source : AC5 27) chain B residue 561 type sequence C description BINDING SITE FOR RESIDUE 5HI A 876 source : AC5 28) chain B residue 565 type sequence S description BINDING SITE FOR RESIDUE 5HI A 876 source : AC5 29) chain B residue 735 type sequence K description BINDING SITE FOR RESIDUE 5HI A 876 source : AC5 30) chain B residue 751 type sequence A description BINDING SITE FOR RESIDUE 5HI A 876 source : AC5 31) chain B residue 752 type sequence H description BINDING SITE FOR RESIDUE 5HI A 876 source : AC5 32) chain B residue 755 type sequence N description BINDING SITE FOR RESIDUE 5HI A 876 source : AC5 33) chain B residue 853 type sequence L description BINDING SITE FOR RESIDUE 5HI A 876 source : AC5 34) chain B residue 856 type sequence A description BINDING SITE FOR RESIDUE 5HI A 876 source : AC5 35) chain A residue 559 type sequence E description BINDING SITE FOR RESIDUE 5HI B 876 source : AC6 36) chain A residue 561 type sequence C description BINDING SITE FOR RESIDUE 5HI B 876 source : AC6 37) chain A residue 565 type sequence S description BINDING SITE FOR RESIDUE 5HI B 876 source : AC6 38) chain A residue 735 type sequence K description BINDING SITE FOR RESIDUE 5HI B 876 source : AC6 39) chain A residue 751 type sequence A description BINDING SITE FOR RESIDUE 5HI B 876 source : AC6 40) chain A residue 755 type sequence N description BINDING SITE FOR RESIDUE 5HI B 876 source : AC6 41) chain A residue 853 type sequence L description BINDING SITE FOR RESIDUE 5HI B 876 source : AC6 42) chain B residue 590 type sequence R description BINDING SITE FOR RESIDUE 5HI B 876 source : AC6 43) chain B residue 661 type sequence S description BINDING SITE FOR RESIDUE 5HI B 876 source : AC6 44) chain B residue 684 type sequence S description BINDING SITE FOR RESIDUE 5HI B 876 source : AC6 45) chain B residue 686 type sequence N description BINDING SITE FOR RESIDUE 5HI B 876 source : AC6 46) chain B residue 690 type sequence D description BINDING SITE FOR RESIDUE 5HI B 876 source : AC6 47) chain B residue 691 type sequence K description BINDING SITE FOR RESIDUE 5HI B 876 source : AC6 48) chain B residue 692 type sequence K description BINDING SITE FOR RESIDUE 5HI B 876 source : AC6 49) chain C residue 590 type sequence R description BINDING SITE FOR RESIDUE 5HI C 876 source : AC7 50) chain C residue 661 type sequence S description BINDING SITE FOR RESIDUE 5HI C 876 source : AC7 51) chain C residue 684 type sequence S description BINDING SITE FOR RESIDUE 5HI C 876 source : AC7 52) chain C residue 690 type sequence D description BINDING SITE FOR RESIDUE 5HI C 876 source : AC7 53) chain C residue 691 type sequence K description BINDING SITE FOR RESIDUE 5HI C 876 source : AC7 54) chain C residue 692 type sequence K description BINDING SITE FOR RESIDUE 5HI C 876 source : AC7 55) chain D residue 559 type sequence E description BINDING SITE FOR RESIDUE 5HI C 876 source : AC7 56) chain D residue 561 type sequence C description BINDING SITE FOR RESIDUE 5HI C 876 source : AC7 57) chain D residue 565 type sequence S description BINDING SITE FOR RESIDUE 5HI C 876 source : AC7 58) chain D residue 735 type sequence K description BINDING SITE FOR RESIDUE 5HI C 876 source : AC7 59) chain D residue 751 type sequence A description BINDING SITE FOR RESIDUE 5HI C 876 source : AC7 60) chain D residue 752 type sequence H description BINDING SITE FOR RESIDUE 5HI C 876 source : AC7 61) chain D residue 755 type sequence N description BINDING SITE FOR RESIDUE 5HI C 876 source : AC7 62) chain D residue 853 type sequence L description BINDING SITE FOR RESIDUE 5HI C 876 source : AC7 63) chain C residue 559 type sequence E description BINDING SITE FOR RESIDUE 5HI D 876 source : AC8 64) chain C residue 561 type sequence C description BINDING SITE FOR RESIDUE 5HI D 876 source : AC8 65) chain C residue 565 type sequence S description BINDING SITE FOR RESIDUE 5HI D 876 source : AC8 66) chain C residue 568 type sequence R description BINDING SITE FOR RESIDUE 5HI D 876 source : AC8 67) chain C residue 735 type sequence K description BINDING SITE FOR RESIDUE 5HI D 876 source : AC8 68) chain C residue 751 type sequence A description BINDING SITE FOR RESIDUE 5HI D 876 source : AC8 69) chain C residue 752 type sequence H description BINDING SITE FOR RESIDUE 5HI D 876 source : AC8 70) chain C residue 755 type sequence N description BINDING SITE FOR RESIDUE 5HI D 876 source : AC8 71) chain C residue 853 type sequence L description BINDING SITE FOR RESIDUE 5HI D 876 source : AC8 72) chain D residue 590 type sequence R description BINDING SITE FOR RESIDUE 5HI D 876 source : AC8 73) chain D residue 661 type sequence S description BINDING SITE FOR RESIDUE 5HI D 876 source : AC8 74) chain D residue 684 type sequence S description BINDING SITE FOR RESIDUE 5HI D 876 source : AC8 75) chain D residue 690 type sequence D description BINDING SITE FOR RESIDUE 5HI D 876 source : AC8 76) chain D residue 691 type sequence K description BINDING SITE FOR RESIDUE 5HI D 876 source : AC8 77) chain D residue 692 type sequence K description BINDING SITE FOR RESIDUE 5HI D 876 source : AC8 78) chain A residue 559 type catalytic sequence E description 93 source MCSA : MCSA1 79) chain A residue 691 type catalytic sequence K description 93 source MCSA : MCSA1 80) chain A residue 767 type catalytic sequence D description 93 source MCSA : MCSA1 81) chain B residue 559 type catalytic sequence E description 93 source MCSA : MCSA2 82) chain B residue 691 type catalytic sequence K description 93 source MCSA : MCSA2 83) chain B residue 767 type catalytic sequence D description 93 source MCSA : MCSA2 84) chain C residue 559 type catalytic sequence E description 93 source MCSA : MCSA3 85) chain C residue 691 type catalytic sequence K description 93 source MCSA : MCSA3 86) chain C residue 767 type catalytic sequence D description 93 source MCSA : MCSA3 87) chain D residue 559 type catalytic sequence E description 93 source MCSA : MCSA4 88) chain D residue 691 type catalytic sequence K description 93 source MCSA : MCSA4 89) chain D residue 767 type catalytic sequence D description 93 source MCSA : MCSA4 90) 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 91) 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 92) 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 93) 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 94) 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 95) 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 96) 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 97) 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 98) 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 99) 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 100) 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 101) 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 102) chain A residue 565 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 103) chain B residue 720 type BINDING sequence V description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 104) chain C residue 565 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 105) chain C residue 626 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 106) chain C residue 653 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 107) chain C residue 720 type BINDING sequence V description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 108) chain D residue 565 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 109) chain A 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 626 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 111) chain D residue 653 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 112) chain D residue 720 type BINDING sequence V description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 113) chain A residue 653 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 114) chain A residue 720 type BINDING sequence V description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 115) chain B 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 626 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 117) chain B residue 653 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 118) chain A residue 504 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI4 119) chain B residue 504 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI4 120) chain C residue 504 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI4 121) chain D residue 504 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI4 122) chain A residue 646-660 type prosite sequence RFQSRSGDAMGMNMI description HMG_COA_REDUCTASE_1 Hydroxymethylglutaryl-coenzyme A reductases signature 1. RfQSrSGDaMGmNmI source prosite : PS00066 123) chain A residue 802-809 type prosite sequence IGTVGGGT description HMG_COA_REDUCTASE_2 Hydroxymethylglutaryl-coenzyme A reductases signature 2. IGtVGGGT source prosite : PS00318

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