eF-site ID 1dq9-ABCD PDB Code 1dq9 Chain A, B, C, D click to enlarge Title COMPLEX OF CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE WITH HMG-COA Classification OXIDOREDUCTASE Compound PROTEIN (HMG-COA REDUCTASE) Source Homo sapiens (Human) (HMDH_HUMAN) Sequence A:  FLSDAEIIQLVNAKHIPAYKLETLIETHERGVSIRRQLLS KKLSEPSSLQYLPYRDYNYSLVMGACCENVIGYMPIPVGV AGPLCLDEKEFQVPMATTEGCLVASTNRGCRAIGLGGGAS SRVLADGMTRGPVVRLPRACDSAEVKAWLETSEGFAVIKE AFDSTSRFARLQKLHTSIAGRNLYIRFQSRSGDAMGMNMI SKGTEKALSKLHEYFPEMQILAVSGNYCTDKKPAAINWIE GRGKSVVCEAVIPAKVVREVLKTTTEAMIEVNINKNLVGS AMAGSIGGYNAHAANIVTAIYIACGQDAAQNVGSSNCITL MEASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQM LGVQGACKDNPGENARQLARIVCGTVMAGELSLMAALAAG HLVKS B:  KFLSDAEIIQLVNAKHIPAYKLETLIETHERGVSIRRQLL SKKLSEPSSLQYLPYRDYNYSLVMGACCENVIGYMPIPVG VAGPLCLDEKEFQVPMATTEGCLVASTNRGCRAIGLGGGA SSRVLADGMTRGPVVRLPRACDSAEVKAWLETSEGFAVIK EAFDSTSRFARLQKLHTSIAGRNLYIRFQSRSGDAMGMNM ISKGTEKALSKLHEYFPEMQILAVSGNYCTDKKPAAINWI EGRGKSVVCEAVIPAKVVREVLKTTTEAMIEVNINKNLVG SAMAGSIGGYNAHAANIVTAIYIACGQDAAQNVGSSNCIT LMEASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQ MLGVQGACKDNPGENARQLARIVCGTVMAGELSLMAALAA GHLVK C:  KFLSDAEIIQLVNAKHIPAYKLETLIETHERGVSIRRQLL SKKLSEPSSLQYLPYRDYNYSLVMGACCENVIGYMPIPVG VAGPLCLDEKEFQVPMATTEGCLVASTNRGCRAIGLGGGA SSRVLADGMTRGPVVRLPRACDSAEVKAWLETSEGFAVIK EAFDSTSRFARLQKLHTSIAGRNLYIRFQSRSGDAMGMNM ISKGTEKALSKLHEYFPEMQILAVSGNYCTDKKPAAINWI EGRGKSVVCEAVIPAKVVREVLKTTTEAMIEVNINKNLVG SAMAGSIGGYNAHAANIVTAIYIACGQDAAQNVGSSNCIT LMEASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQ MLGVQGACKDNPGENARQLARIVCGTVMAGELSLMAALAA GHLVKSH D:  GNAEKGAKFLSDAEIIQLVNAKHIPAYKLETLIETHERGV SIRRQLLSKKLSEPSSLQYLPYRDYNYSLVMGACCENVIG YMPIPVGVAGPLCLDEKEFQVPMATTEGCLVASTNRGCRA IGLGGGASSRVLADGMTRGPVVRLPRACDSAEVKAWLETS EGFAVIKEAFDSTSRFARLQKLHTSIAGRNLYIRFQSRSG DAMGMNMISKGTEKALSKLHEYFPEMQILAVSGNYCTDKK PAAINWIEGRGKSVVCEAVIPAKVVREVLKTTTEAMIEVN INKNLVGSAMAGSIGGYNAHAANIVTAIYIACGQDAAQNV GSSNCITLMEASGPTNEDLYISCTMPSIEIGTVGGGTNLL PQQACLQMLGVQGACKDNPGENARQLARIVCGTVMAGELS LMAALAAGHLVKS Description Functional site 1) chain A residue 559 type sequence E description BINDING SITE FOR RESIDUE HMG A 101 source : AC1 2) chain A residue 564 type sequence A description BINDING SITE FOR RESIDUE HMG A 101 source : AC1 3) chain A residue 565 type sequence S description BINDING SITE FOR RESIDUE HMG A 101 source : AC1 4) chain A residue 567 type sequence N description BINDING SITE FOR RESIDUE HMG A 101 source : AC1 5) chain A residue 568 type sequence R description BINDING SITE FOR RESIDUE HMG A 101 source : AC1 6) chain A residue 571 type sequence R description BINDING SITE FOR RESIDUE HMG A 101 source : AC1 7) chain A residue 720 type sequence V description BINDING SITE FOR RESIDUE HMG A 101 source : AC1 8) chain A residue 722 type sequence K description BINDING SITE FOR RESIDUE HMG A 101 source : AC1 9) chain A residue 735 type sequence K description BINDING SITE FOR RESIDUE HMG A 101 source : AC1 10) chain A residue 751 type sequence A description BINDING SITE FOR RESIDUE HMG A 101 source : AC1 11) chain A residue 752 type sequence H description BINDING SITE FOR RESIDUE HMG A 101 source : AC1 12) chain A residue 852 type sequence S description BINDING SITE FOR RESIDUE HMG A 101 source : AC1 13) chain A residue 853 type sequence L description BINDING SITE FOR RESIDUE HMG A 101 source : AC1 14) chain A residue 856 type sequence A description BINDING SITE FOR RESIDUE HMG A 101 source : AC1 15) chain A residue 862 type sequence L description BINDING SITE FOR RESIDUE HMG A 101 source : AC1 16) chain A residue 865 type sequence S description BINDING SITE FOR RESIDUE HMG A 101 source : AC1 17) chain B residue 479 type sequence Y description BINDING SITE FOR RESIDUE HMG A 101 source : AC1 18) chain B residue 528 type sequence E description BINDING SITE FOR RESIDUE HMG A 101 source : AC1 19) chain B residue 590 type sequence R description BINDING SITE FOR RESIDUE HMG A 101 source : AC1 20) chain B residue 684 type sequence S description BINDING SITE FOR RESIDUE HMG A 101 source : AC1 21) chain B residue 690 type sequence D description BINDING SITE FOR RESIDUE HMG A 101 source : AC1 22) chain B residue 691 type sequence K description BINDING SITE FOR RESIDUE HMG A 101 source : AC1 23) chain B residue 692 type sequence K description BINDING SITE FOR RESIDUE HMG A 101 source : AC1 24) chain A residue 479 type sequence Y description BINDING SITE FOR RESIDUE HMG B 102 source : AC2 25) chain A residue 528 type sequence E description BINDING SITE FOR RESIDUE HMG B 102 source : AC2 26) chain A residue 590 type sequence R description BINDING SITE FOR RESIDUE HMG B 102 source : AC2 27) chain A residue 684 type sequence S description BINDING SITE FOR RESIDUE HMG B 102 source : AC2 28) chain A residue 690 type sequence D description BINDING SITE FOR RESIDUE HMG B 102 source : AC2 29) chain A residue 691 type sequence K description BINDING SITE FOR RESIDUE HMG B 102 source : AC2 30) chain A residue 692 type sequence K description BINDING SITE FOR RESIDUE HMG B 102 source : AC2 31) chain B residue 559 type sequence E description BINDING SITE FOR RESIDUE HMG B 102 source : AC2 32) chain B residue 564 type sequence A description BINDING SITE FOR RESIDUE HMG B 102 source : AC2 33) chain B residue 565 type sequence S description BINDING SITE FOR RESIDUE HMG B 102 source : AC2 34) chain B residue 567 type sequence N description BINDING SITE FOR RESIDUE HMG B 102 source : AC2 35) chain B residue 568 type sequence R description BINDING SITE FOR RESIDUE HMG B 102 source : AC2 36) chain B residue 571 type sequence R description BINDING SITE FOR RESIDUE HMG B 102 source : AC2 37) chain B residue 720 type sequence V description BINDING SITE FOR RESIDUE HMG B 102 source : AC2 38) chain B residue 722 type sequence K description BINDING SITE FOR RESIDUE HMG B 102 source : AC2 39) chain B residue 735 type sequence K description BINDING SITE FOR RESIDUE HMG B 102 source : AC2 40) chain B residue 752 type sequence H description BINDING SITE FOR RESIDUE HMG B 102 source : AC2 41) chain B residue 755 type sequence N description BINDING SITE FOR RESIDUE HMG B 102 source : AC2 42) chain B residue 852 type sequence S description BINDING SITE FOR RESIDUE HMG B 102 source : AC2 43) chain B residue 853 type sequence L description BINDING SITE FOR RESIDUE HMG B 102 source : AC2 44) chain C residue 559 type sequence E description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 45) chain C residue 564 type sequence A description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 46) chain C residue 565 type sequence S description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 47) chain C residue 567 type sequence N description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 48) chain C residue 568 type sequence R description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 49) chain C residue 571 type sequence R description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 50) chain C residue 720 type sequence V description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 51) chain C residue 722 type sequence K description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 52) chain C residue 735 type sequence K description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 53) chain C residue 751 type sequence A description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 54) chain C residue 752 type sequence H description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 55) chain C residue 755 type sequence N description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 56) chain C residue 852 type sequence S description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 57) chain C residue 853 type sequence L description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 58) chain C residue 856 type sequence A description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 59) chain C residue 862 type sequence L description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 60) chain C residue 865 type sequence S description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 61) chain C residue 866 type sequence H description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 62) chain D residue 479 type sequence Y description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 63) chain D residue 528 type sequence E description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 64) chain D residue 529 type sequence N description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 65) chain D residue 590 type sequence R description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 66) chain D residue 684 type sequence S description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 67) chain D residue 690 type sequence D description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 68) chain D residue 691 type sequence K description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 69) chain D residue 692 type sequence K description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 70) chain C residue 477 type sequence P description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 71) chain C residue 479 type sequence Y description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 72) chain C residue 528 type sequence E description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 73) chain C residue 529 type sequence N description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 74) chain C residue 590 type sequence R description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 75) chain C residue 684 type sequence S description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 76) chain C residue 690 type sequence D description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 77) chain C residue 691 type sequence K description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 78) chain C residue 692 type sequence K description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 79) chain D residue 559 type sequence E description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 80) chain D residue 564 type sequence A description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 81) chain D residue 565 type sequence S description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 82) chain D residue 567 type sequence N description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 83) chain D residue 568 type sequence R description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 84) chain D residue 571 type sequence R description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 85) chain D residue 720 type sequence V description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 86) chain D residue 722 type sequence K description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 87) chain D residue 735 type sequence K description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 88) chain D residue 751 type sequence A description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 89) chain D residue 752 type sequence H description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 90) chain D residue 852 type sequence S description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 91) chain D residue 853 type sequence L description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 92) chain D residue 856 type sequence A description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 93) chain D residue 862 type sequence L description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 94) chain D residue 865 type sequence S description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 95) chain A residue 504 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI4 96) chain B residue 504 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI4 97) chain C residue 504 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI4 98) chain D residue 504 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI4 99) 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 100) 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 101) 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 102) 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 103) 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 104) 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 105) 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 106) 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 107) 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 108) 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 109) 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 110) 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 111) chain C residue 866 type ACT_SITE sequence H description Proton donor => ECO:0000255|PROSITE-ProRule:PRU10003 source Swiss-Prot : SWS_FT_FI2 112) chain A residue 565 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 113) chain B residue 720 type BINDING sequence V description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 114) chain C residue 565 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 115) chain C residue 626 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 116) chain C residue 653 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 117) chain C residue 720 type BINDING sequence V description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 118) chain C residue 865 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 119) chain D residue 565 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 120) chain A residue 626 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 121) chain D residue 626 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 122) chain D residue 653 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 123) chain D residue 720 type BINDING sequence V description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 124) chain D residue 865 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 125) chain A residue 653 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 126) chain A 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 865 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 128) chain B residue 565 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 129) chain B residue 626 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 130) chain B residue 653 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 131) chain A residue 559 type catalytic sequence E description 93 source MCSA : MCSA1 132) chain A residue 691 type catalytic sequence K description 93 source MCSA : MCSA1 133) chain A residue 767 type catalytic sequence D description 93 source MCSA : MCSA1 134) chain B residue 559 type catalytic sequence E description 93 source MCSA : MCSA2 135) chain B residue 691 type catalytic sequence K description 93 source MCSA : MCSA2 136) chain B residue 767 type catalytic sequence D description 93 source MCSA : MCSA2 137) chain C residue 559 type catalytic sequence E description 93 source MCSA : MCSA3 138) chain C residue 691 type catalytic sequence K description 93 source MCSA : MCSA3 139) chain C residue 767 type catalytic sequence D description 93 source MCSA : MCSA3 140) chain C residue 866 type catalytic sequence H description 93 source MCSA : MCSA3 141) chain D residue 559 type catalytic sequence E description 93 source MCSA : MCSA4 142) chain D residue 691 type catalytic sequence K description 93 source MCSA : MCSA4 143) chain D residue 767 type catalytic sequence D description 93 source MCSA : MCSA4 144) chain A residue 646-660 type prosite sequence RFQSRSGDAMGMNMI description HMG_COA_REDUCTASE_1 Hydroxymethylglutaryl-coenzyme A reductases signature 1. RfQSrSGDaMGmNmI source prosite : PS00066 145) 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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