eF-site ID 1dq9-C PDB Code 1dq9 Chain C 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 C:  KFLSDAEIIQLVNAKHIPAYKLETLIETHERGVSIRRQLL SKKLSEPSSLQYLPYRDYNYSLVMGACCENVIGYMPIPVG VAGPLCLDEKEFQVPMATTEGCLVASTNRGCRAIGLGGGA SSRVLADGMTRGPVVRLPRACDSAEVKAWLETSEGFAVIK EAFDSTSRFARLQKLHTSIAGRNLYIRFQSRSGDAMGMNM ISKGTEKALSKLHEYFPEMQILAVSGNYCTDKKPAAINWI EGRGKSVVCEAVIPAKVVREVLKTTTEAMIEVNINKNLVG SAMAGSIGGYNAHAANIVTAIYIACGQDAAQNVGSSNCIT LMEASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQ MLGVQGACKDNPGENARQLARIVCGTVMAGELSLMAALAA GHLVKSH Description Functional site 1) chain C residue 559 type sequence E description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 2) chain C residue 564 type sequence A description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 3) chain C residue 565 type sequence S description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 4) chain C residue 567 type sequence N description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 5) chain C residue 568 type sequence R description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 6) chain C residue 571 type sequence R description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 7) chain C residue 720 type sequence V description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 8) chain C residue 722 type sequence K description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 9) chain C residue 735 type sequence K description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 10) chain C residue 751 type sequence A description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 11) chain C residue 752 type sequence H description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 12) chain C residue 755 type sequence N description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 13) chain C residue 852 type sequence S description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 14) chain C residue 853 type sequence L description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 15) chain C residue 856 type sequence A description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 16) chain C residue 862 type sequence L description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 17) chain C residue 865 type sequence S description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 18) chain C residue 866 type sequence H description BINDING SITE FOR RESIDUE HMG C 103 source : AC3 19) chain C residue 477 type sequence P description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 20) chain C residue 479 type sequence Y description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 21) chain C residue 528 type sequence E description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 22) chain C residue 529 type sequence N description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 23) chain C residue 590 type sequence R description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 24) chain C residue 684 type sequence S description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 25) chain C residue 690 type sequence D description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 26) chain C residue 691 type sequence K description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 27) chain C residue 692 type sequence K description BINDING SITE FOR RESIDUE HMG D 104 source : AC4 28) chain C residue 504 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI4 29) 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 30) 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 31) 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 32) chain C residue 866 type ACT_SITE sequence H description Proton donor => ECO:0000255|PROSITE-ProRule:PRU10003 source Swiss-Prot : SWS_FT_FI2 33) chain C residue 565 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 34) chain C residue 626 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 35) chain C residue 653 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 36) chain C residue 720 type BINDING sequence V description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 37) chain C residue 865 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA source Swiss-Prot : SWS_FT_FI3 38) chain C residue 559 type catalytic sequence E description 93 source MCSA : MCSA3 39) chain C residue 691 type catalytic sequence K description 93 source MCSA : MCSA3 40) chain C residue 767 type catalytic sequence D description 93 source MCSA : MCSA3 41) chain C residue 866 type catalytic sequence H description 93 source MCSA : MCSA3

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