eF-site ID 3ccw-ABCD
PDB Code 3ccw
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:  EPRPNEECLQILGNAEKGAKFLSDAEIIQLVNAKHIPAYK
LETLIETHERGVSIRRQLLSKKLSEPSSLQYLPYRDYNYS
LVMGACCENVIGYMPIPVGVAGPLCLDEKEFQVPMATTEG
CLVASTNRGCRAIGLGGGASSRVLADGMTRGPVVRLPRAC
DSAEVKAWLETSEGFAVIKEAFDSTSRFARLQKLHTSIAG
RNLYIRFQSRSGDAMGMNMISKGTEKALSKLHEYFPEMQI
LAVSGNYCTDKKPAAINWIEGRGKSVVCEAVIPAKVVREV
LKTTTEAMIEVNINKNLVGSAMAGSIGGYNAHAANIVTAI
YIACGQDAAQNVGSSNCITLMEASGPTNEDLYISCTMPSI
EIGTVGGGTNLLPQQACLQMLGVQGACKDNPGENARQLAR
IVCGTVMAGELSLMAALAAGH
B:  EPRPNEECLQILGNAEKGAKFLSDAEIIQLVNAKHIPAYK
LETLIETHERGVSIRRQLLSKKLSEPSSLQYLPYRDYNYS
LVMGACCENVIGYMPIPVGVAGPLCLDEKEFQVPMATTEG
CLVASTNRGCRAIGLGGGASSRVLADGMTRGPVVRLPRAC
DSAEVKAWLETSEGFAVIKEAFDSTSRFARLQKLHTSIAG
RNLYIRFQSRSGDAMGMNMISKGTEKALSKLHEYFPEMQI
LAVSGNYCTDKKPAAINWIEGRGKSVVCEAVIPAKVVREV
LKTTTEAMIEVNINKNLVGSAMAGSIGGYNAHAANIVTAI
YIACGQDAAQNVGSSNCITLMEASGPTNEDLYISCTMPSI
EIGTVGGGTNLLPQQACLQMLGVQGACKDNPGENARQLAR
IVCGTVMAGELSLMAALAAGH
C:  PNEECLQILGNGAKFLSDAEIIQLVNAKHIPAYKLETLIE
THERGVSIRRQLLSKKLSEPSSLQYLPYRDYNYSLVMGAC
CENVIGYMPIPVGVAGPLCLDEKEFQVPMATTEGCLVAST
NRGCRAIGLGGGASSRVLADGMTRGPVVRLPRACDSAEVK
AWLETSEGFAVIKEAFDSTSRFARLQKLHTSIAGRNLYIR
FQSRSGDAMGMNMISKGTEKALSKLHEYFPEMQILAVSGN
YCTDKKPAAINWIEGRGKSVVCEAVIPAKVVREVLKTTTE
AMIEVNINKNLVGSAMAGSIGGYNAHAANIVTAIYIACGQ
DAAQNVGSSNCITLMEASGPTNEDLYISCTMPSIEIGTVG
GGTNLLPQQACLQMLGVQGACKDNPGENARQLARIVCGTV
MAGELSLMAALAAG
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 4HI B 1
source : AC1

2) chain A
residue 560
type
sequence G
description BINDING SITE FOR RESIDUE 4HI B 1
source : AC1

3) chain A
residue 561
type
sequence C
description BINDING SITE FOR RESIDUE 4HI B 1
source : AC1

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

5) chain A
residue 568
type
sequence R
description BINDING SITE FOR RESIDUE 4HI B 1
source : AC1

6) chain A
residue 735
type
sequence K
description BINDING SITE FOR RESIDUE 4HI B 1
source : AC1

7) chain A
residue 751
type
sequence A
description BINDING SITE FOR RESIDUE 4HI B 1
source : AC1

8) chain A
residue 752
type
sequence H
description BINDING SITE FOR RESIDUE 4HI B 1
source : AC1

9) chain A
residue 755
type
sequence N
description BINDING SITE FOR RESIDUE 4HI B 1
source : AC1

10) chain A
residue 853
type
sequence L
description BINDING SITE FOR RESIDUE 4HI B 1
source : AC1

11) chain B
residue 590
type
sequence R
description BINDING SITE FOR RESIDUE 4HI B 1
source : AC1

12) chain B
residue 657
type
sequence M
description BINDING SITE FOR RESIDUE 4HI B 1
source : AC1

13) chain B
residue 661
type
sequence S
description BINDING SITE FOR RESIDUE 4HI B 1
source : AC1

14) chain B
residue 684
type
sequence S
description BINDING SITE FOR RESIDUE 4HI B 1
source : AC1

15) chain B
residue 690
type
sequence D
description BINDING SITE FOR RESIDUE 4HI B 1
source : AC1

16) chain B
residue 691
type
sequence K
description BINDING SITE FOR RESIDUE 4HI B 1
source : AC1

17) chain B
residue 692
type
sequence K
description BINDING SITE FOR RESIDUE 4HI B 1
source : AC1

18) chain A
residue 590
type
sequence R
description BINDING SITE FOR RESIDUE 4HI B 2
source : AC2

19) chain A
residue 657
type
sequence M
description BINDING SITE FOR RESIDUE 4HI B 2
source : AC2

20) chain A
residue 661
type
sequence S
description BINDING SITE FOR RESIDUE 4HI B 2
source : AC2

21) chain A
residue 684
type
sequence S
description BINDING SITE FOR RESIDUE 4HI B 2
source : AC2

22) chain A
residue 690
type
sequence D
description BINDING SITE FOR RESIDUE 4HI B 2
source : AC2

23) chain A
residue 691
type
sequence K
description BINDING SITE FOR RESIDUE 4HI B 2
source : AC2

24) chain A
residue 692
type
sequence K
description BINDING SITE FOR RESIDUE 4HI B 2
source : AC2

25) chain B
residue 559
type
sequence E
description BINDING SITE FOR RESIDUE 4HI B 2
source : AC2

26) chain B
residue 560
type
sequence G
description BINDING SITE FOR RESIDUE 4HI B 2
source : AC2

27) chain B
residue 561
type
sequence C
description BINDING SITE FOR RESIDUE 4HI B 2
source : AC2

28) chain B
residue 565
type
sequence S
description BINDING SITE FOR RESIDUE 4HI B 2
source : AC2

29) chain B
residue 735
type
sequence K
description BINDING SITE FOR RESIDUE 4HI B 2
source : AC2

30) chain B
residue 751
type
sequence A
description BINDING SITE FOR RESIDUE 4HI B 2
source : AC2

31) chain B
residue 752
type
sequence H
description BINDING SITE FOR RESIDUE 4HI B 2
source : AC2

32) chain B
residue 755
type
sequence N
description BINDING SITE FOR RESIDUE 4HI B 2
source : AC2

33) chain B
residue 853
type
sequence L
description BINDING SITE FOR RESIDUE 4HI B 2
source : AC2

34) chain B
residue 856
type
sequence A
description BINDING SITE FOR RESIDUE 4HI B 2
source : AC2

35) chain C
residue 559
type
sequence E
description BINDING SITE FOR RESIDUE 4HI D 3
source : AC3

36) chain C
residue 560
type
sequence G
description BINDING SITE FOR RESIDUE 4HI D 3
source : AC3

37) chain C
residue 565
type
sequence S
description BINDING SITE FOR RESIDUE 4HI D 3
source : AC3

38) chain C
residue 735
type
sequence K
description BINDING SITE FOR RESIDUE 4HI D 3
source : AC3

39) chain C
residue 751
type
sequence A
description BINDING SITE FOR RESIDUE 4HI D 3
source : AC3

40) chain C
residue 752
type
sequence H
description BINDING SITE FOR RESIDUE 4HI D 3
source : AC3

41) chain C
residue 755
type
sequence N
description BINDING SITE FOR RESIDUE 4HI D 3
source : AC3

42) chain C
residue 853
type
sequence L
description BINDING SITE FOR RESIDUE 4HI D 3
source : AC3

43) chain C
residue 856
type
sequence A
description BINDING SITE FOR RESIDUE 4HI D 3
source : AC3

44) chain D
residue 590
type
sequence R
description BINDING SITE FOR RESIDUE 4HI D 3
source : AC3

45) chain D
residue 657
type
sequence M
description BINDING SITE FOR RESIDUE 4HI D 3
source : AC3

46) chain D
residue 661
type
sequence S
description BINDING SITE FOR RESIDUE 4HI D 3
source : AC3

47) chain D
residue 684
type
sequence S
description BINDING SITE FOR RESIDUE 4HI D 3
source : AC3

48) chain D
residue 686
type
sequence N
description BINDING SITE FOR RESIDUE 4HI D 3
source : AC3

49) chain D
residue 690
type
sequence D
description BINDING SITE FOR RESIDUE 4HI D 3
source : AC3

50) chain D
residue 691
type
sequence K
description BINDING SITE FOR RESIDUE 4HI D 3
source : AC3

51) chain D
residue 692
type
sequence K
description BINDING SITE FOR RESIDUE 4HI D 3
source : AC3

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

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

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

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

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

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

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

59) chain D
residue 560
type
sequence G
description BINDING SITE FOR RESIDUE 4HI C 4
source : AC4

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

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

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

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

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

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

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

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

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

69) chain A
residue 559
type catalytic
sequence E
description 93
source MCSA : MCSA1

70) chain A
residue 691
type catalytic
sequence K
description 93
source MCSA : MCSA1

71) chain A
residue 767
type catalytic
sequence D
description 93
source MCSA : MCSA1

72) chain B
residue 559
type catalytic
sequence E
description 93
source MCSA : MCSA2

73) chain B
residue 691
type catalytic
sequence K
description 93
source MCSA : MCSA2

74) chain B
residue 767
type catalytic
sequence D
description 93
source MCSA : MCSA2

75) chain C
residue 559
type catalytic
sequence E
description 93
source MCSA : MCSA3

76) chain C
residue 691
type catalytic
sequence K
description 93
source MCSA : MCSA3

77) chain C
residue 767
type catalytic
sequence D
description 93
source MCSA : MCSA3

78) chain D
residue 559
type catalytic
sequence E
description 93
source MCSA : MCSA4

79) chain D
residue 691
type catalytic
sequence K
description 93
source MCSA : MCSA4

80) chain D
residue 767
type catalytic
sequence D
description 93
source MCSA : MCSA4

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

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

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

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

85) 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

86) 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

87) 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

88) 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

89) 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

90) 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

91) 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

92) 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

93) 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

94) 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

95) 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

96) 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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

114) 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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