eF-site ID 3cd7-ABCD
PDB Code 3cd7
Chain A, B, C, D

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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:  AKFLSDAEIIQLVNAIETHERGVSIRRQLLSKKLSEPSSL
QYLPYRDYNYSLVMGACCENVIGYMPIPVGVAGPLCLDEK
EFQVPMATTEGCLVASTNRGCRAIGLGGGASSRVLADGMT
RGPVVRLPRACDSAEVKAWLETSEGFAVIKEAFDSTSRFA
RLQKLHTSIAGRNLYIRFQSRSGDAMGMNMISKGTEKALS
KLHEYFPEMQILAVSGNYCTDKKPAAINWIEGRGKSVVCE
AVIPAKVVREVLKTTTEAMIEVNINKNLVGSAMAGSIGGY
NAHAANIVTAIYIACGQDAAQNVGSSNCITLMEASGPTNE
DLYISCTMPSIEIGTVGGGTNLLPQQACLQMLGVQGACKD
NPGENARQLARIVCGTVMAGELSLMAALAAGH
B:  AKFLSDAEIIQLVNAKHIPAYKLETLIHERGVSIRRQLLS
KKLSEPSSLQYLPYRDYNYSLVMGACCENVIGYMPIPVGV
AGPLCLDEKEFQVPMATTEGCLVASTNRGCRAIGLGGGAS
SRVLADGMTRGPVVRLPRACDSAEVKAWLETSEGFAVIKE
AFDSTSRFARLQKLHTSIAGRNLYIRFQSRSGDAMGMNMI
SKGTEKALSKLHEYFPEMQILAVSGNYCTDKKPAAINWIE
GRGKSVVCEAVIPAKVVREVLKTTTEAMIEVNINKNLVGS
AMAGSIGGYNAHAANIVTAIYIACGQDAAQNVGSSNCITL
MEASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQM
LGVQGACKDNPGENARQLARIVCGTVMAGELSLMAALAAG
H
C:  PNEECLQILGNAEGAKFLSDAEIIQLVNAKHIPAYKLETL
IETHERGVSIRRQLLSKKLSEPSSLQYLPYRDYNYSLVMG
ACCENVIGYMPIPVGVAGPLCLDEKEFQVPMATTEGCLVA
STNRGCRAIGLGGGASSRVLADGMTRGPVVRLPRACDSAE
VKAWLETSEGFAVIKEAFDSTSRFARLQKLHTSIAGRNLY
IRFQSRSGDAMGMNMISKGTEKALSKLHEYFPEMQILAVS
GNYCTDKKPAAINWIEGRGKSVVCEAVIPAKVVREVLKTT
TEAMIEVNINKNLVGSAMAGSIGGYNAHAANIVTAIYIAC
GQDAAQNVGSSNCITLMEASGPTNEDLYISCTMPSIEIGT
VGGGTNLLPQQACLQMLGVQGACKDNPGENARQLARIVCG
TVMAGELSLMAALAAG
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 882 A 1
source : AC1

2) chain A
residue 561
type
sequence C
description BINDING SITE FOR RESIDUE 882 A 1
source : AC1

3) chain A
residue 562
type
sequence L
description BINDING SITE FOR RESIDUE 882 A 1
source : AC1

4) chain A
residue 565
type
sequence S
description BINDING SITE FOR RESIDUE 882 A 1
source : AC1

5) chain A
residue 568
type
sequence R
description BINDING SITE FOR RESIDUE 882 A 1
source : AC1

6) chain A
residue 735
type
sequence K
description BINDING SITE FOR RESIDUE 882 A 1
source : AC1

7) chain A
residue 751
type
sequence A
description BINDING SITE FOR RESIDUE 882 A 1
source : AC1

8) chain A
residue 752
type
sequence H
description BINDING SITE FOR RESIDUE 882 A 1
source : AC1

9) chain A
residue 755
type
sequence N
description BINDING SITE FOR RESIDUE 882 A 1
source : AC1

10) chain A
residue 853
type
sequence L
description BINDING SITE FOR RESIDUE 882 A 1
source : AC1

11) chain A
residue 856
type
sequence A
description BINDING SITE FOR RESIDUE 882 A 1
source : AC1

12) chain A
residue 861
type
sequence H
description BINDING SITE FOR RESIDUE 882 A 1
source : AC1

13) chain B
residue 590
type
sequence R
description BINDING SITE FOR RESIDUE 882 A 1
source : AC1

14) chain B
residue 657
type
sequence M
description BINDING SITE FOR RESIDUE 882 A 1
source : AC1

15) chain B
residue 661
type
sequence S
description BINDING SITE FOR RESIDUE 882 A 1
source : AC1

16) chain B
residue 684
type
sequence S
description BINDING SITE FOR RESIDUE 882 A 1
source : AC1

17) chain B
residue 690
type
sequence D
description BINDING SITE FOR RESIDUE 882 A 1
source : AC1

18) chain B
residue 691
type
sequence K
description BINDING SITE FOR RESIDUE 882 A 1
source : AC1

19) chain B
residue 692
type
sequence K
description BINDING SITE FOR RESIDUE 882 A 1
source : AC1

20) chain A
residue 590
type
sequence R
description BINDING SITE FOR RESIDUE 882 A 2
source : AC2

21) chain A
residue 661
type
sequence S
description BINDING SITE FOR RESIDUE 882 A 2
source : AC2

22) chain A
residue 684
type
sequence S
description BINDING SITE FOR RESIDUE 882 A 2
source : AC2

23) chain A
residue 686
type
sequence N
description BINDING SITE FOR RESIDUE 882 A 2
source : AC2

24) chain A
residue 690
type
sequence D
description BINDING SITE FOR RESIDUE 882 A 2
source : AC2

25) chain A
residue 691
type
sequence K
description BINDING SITE FOR RESIDUE 882 A 2
source : AC2

26) chain A
residue 692
type
sequence K
description BINDING SITE FOR RESIDUE 882 A 2
source : AC2

27) chain B
residue 559
type
sequence E
description BINDING SITE FOR RESIDUE 882 A 2
source : AC2

28) chain B
residue 560
type
sequence G
description BINDING SITE FOR RESIDUE 882 A 2
source : AC2

29) chain B
residue 561
type
sequence C
description BINDING SITE FOR RESIDUE 882 A 2
source : AC2

30) chain B
residue 562
type
sequence L
description BINDING SITE FOR RESIDUE 882 A 2
source : AC2

31) chain B
residue 565
type
sequence S
description BINDING SITE FOR RESIDUE 882 A 2
source : AC2

32) chain B
residue 735
type
sequence K
description BINDING SITE FOR RESIDUE 882 A 2
source : AC2

33) chain B
residue 751
type
sequence A
description BINDING SITE FOR RESIDUE 882 A 2
source : AC2

34) chain B
residue 752
type
sequence H
description BINDING SITE FOR RESIDUE 882 A 2
source : AC2

35) chain B
residue 755
type
sequence N
description BINDING SITE FOR RESIDUE 882 A 2
source : AC2

36) chain B
residue 853
type
sequence L
description BINDING SITE FOR RESIDUE 882 A 2
source : AC2

37) chain B
residue 856
type
sequence A
description BINDING SITE FOR RESIDUE 882 A 2
source : AC2

38) chain B
residue 857
type
sequence L
description BINDING SITE FOR RESIDUE 882 A 2
source : AC2

39) chain B
residue 860
type
sequence G
description BINDING SITE FOR RESIDUE 882 A 2
source : AC2

40) chain C
residue 559
type
sequence E
description BINDING SITE FOR RESIDUE 882 D 3
source : AC3

41) chain C
residue 561
type
sequence C
description BINDING SITE FOR RESIDUE 882 D 3
source : AC3

42) chain C
residue 562
type
sequence L
description BINDING SITE FOR RESIDUE 882 D 3
source : AC3

43) chain C
residue 565
type
sequence S
description BINDING SITE FOR RESIDUE 882 D 3
source : AC3

44) chain C
residue 735
type
sequence K
description BINDING SITE FOR RESIDUE 882 D 3
source : AC3

45) chain C
residue 751
type
sequence A
description BINDING SITE FOR RESIDUE 882 D 3
source : AC3

46) chain C
residue 752
type
sequence H
description BINDING SITE FOR RESIDUE 882 D 3
source : AC3

47) chain C
residue 755
type
sequence N
description BINDING SITE FOR RESIDUE 882 D 3
source : AC3

48) chain C
residue 853
type
sequence L
description BINDING SITE FOR RESIDUE 882 D 3
source : AC3

49) chain C
residue 856
type
sequence A
description BINDING SITE FOR RESIDUE 882 D 3
source : AC3

50) chain C
residue 860
type
sequence G
description BINDING SITE FOR RESIDUE 882 D 3
source : AC3

51) chain D
residue 590
type
sequence R
description BINDING SITE FOR RESIDUE 882 D 3
source : AC3

52) chain D
residue 657
type
sequence M
description BINDING SITE FOR RESIDUE 882 D 3
source : AC3

53) chain D
residue 661
type
sequence S
description BINDING SITE FOR RESIDUE 882 D 3
source : AC3

54) chain D
residue 684
type
sequence S
description BINDING SITE FOR RESIDUE 882 D 3
source : AC3

55) chain D
residue 686
type
sequence N
description BINDING SITE FOR RESIDUE 882 D 3
source : AC3

56) chain D
residue 690
type
sequence D
description BINDING SITE FOR RESIDUE 882 D 3
source : AC3

57) chain D
residue 691
type
sequence K
description BINDING SITE FOR RESIDUE 882 D 3
source : AC3

58) chain D
residue 692
type
sequence K
description BINDING SITE FOR RESIDUE 882 D 3
source : AC3

59) chain C
residue 590
type
sequence R
description BINDING SITE FOR RESIDUE 882 C 4
source : AC4

60) chain C
residue 661
type
sequence S
description BINDING SITE FOR RESIDUE 882 C 4
source : AC4

61) chain C
residue 684
type
sequence S
description BINDING SITE FOR RESIDUE 882 C 4
source : AC4

62) chain C
residue 686
type
sequence N
description BINDING SITE FOR RESIDUE 882 C 4
source : AC4

63) chain C
residue 690
type
sequence D
description BINDING SITE FOR RESIDUE 882 C 4
source : AC4

64) chain C
residue 691
type
sequence K
description BINDING SITE FOR RESIDUE 882 C 4
source : AC4

65) chain C
residue 692
type
sequence K
description BINDING SITE FOR RESIDUE 882 C 4
source : AC4

66) chain D
residue 559
type
sequence E
description BINDING SITE FOR RESIDUE 882 C 4
source : AC4

67) chain D
residue 561
type
sequence C
description BINDING SITE FOR RESIDUE 882 C 4
source : AC4

68) chain D
residue 562
type
sequence L
description BINDING SITE FOR RESIDUE 882 C 4
source : AC4

69) chain D
residue 565
type
sequence S
description BINDING SITE FOR RESIDUE 882 C 4
source : AC4

70) chain D
residue 568
type
sequence R
description BINDING SITE FOR RESIDUE 882 C 4
source : AC4

71) chain D
residue 735
type
sequence K
description BINDING SITE FOR RESIDUE 882 C 4
source : AC4

72) chain D
residue 751
type
sequence A
description BINDING SITE FOR RESIDUE 882 C 4
source : AC4

73) chain D
residue 752
type
sequence H
description BINDING SITE FOR RESIDUE 882 C 4
source : AC4

74) chain D
residue 755
type
sequence N
description BINDING SITE FOR RESIDUE 882 C 4
source : AC4

75) chain D
residue 852
type
sequence S
description BINDING SITE FOR RESIDUE 882 C 4
source : AC4

76) chain D
residue 853
type
sequence L
description BINDING SITE FOR RESIDUE 882 C 4
source : AC4

77) chain D
residue 856
type
sequence A
description BINDING SITE FOR RESIDUE 882 C 4
source : AC4

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 646-660
type prosite
sequence RFQSRSGDAMGMNMI
description HMG_COA_REDUCTASE_1 Hydroxymethylglutaryl-coenzyme A reductases signature 1. RfQSrSGDaMGmNmI
source prosite : PS00066

91) chain A
residue 802-809
type prosite
sequence IGTVGGGT
description HMG_COA_REDUCTASE_2 Hydroxymethylglutaryl-coenzyme A reductases signature 2. IGtVGGGT
source prosite : PS00318

92) 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

93) 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

94) 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

95) 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

96) 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

97) 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

98) 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

99) 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

100) 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

101) 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

102) 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

103) 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

104) chain A
residue 565
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA
source Swiss-Prot : SWS_FT_FI3

105) chain B
residue 720
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA
source Swiss-Prot : SWS_FT_FI3

106) chain C
residue 565
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA
source Swiss-Prot : SWS_FT_FI3

107) chain C
residue 626
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA
source Swiss-Prot : SWS_FT_FI3

108) chain C
residue 653
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA
source Swiss-Prot : SWS_FT_FI3

109) chain C
residue 720
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA
source Swiss-Prot : SWS_FT_FI3

110) chain D
residue 565
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA
source Swiss-Prot : SWS_FT_FI3

111) chain A
residue 626
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA
source Swiss-Prot : SWS_FT_FI3

112) chain D
residue 626
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA
source Swiss-Prot : SWS_FT_FI3

113) chain D
residue 653
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA
source Swiss-Prot : SWS_FT_FI3

114) chain D
residue 720
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA
source Swiss-Prot : SWS_FT_FI3

115) chain A
residue 653
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA
source Swiss-Prot : SWS_FT_FI3

116) chain A
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 565
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA
source Swiss-Prot : SWS_FT_FI3

118) chain B
residue 626
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA
source Swiss-Prot : SWS_FT_FI3

119) chain B
residue 653
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:11349148, ECO:0007744|PDB:1DQA
source Swiss-Prot : SWS_FT_FI3

120) chain A
residue 504
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI4

121) chain B
residue 504
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI4

122) chain C
residue 504
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI4

123) 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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