eF-site ID 1gg5-BD
PDB Code 1gg5
Chain B, D

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Title CRYSTAL STRUCTURE OF A COMPLEX OF HUMAN NAD[P]H-QUINONE OXIDOREDUCTASE AND A CHEMOTHERAPEUTIC DRUG (E09) AT 2.5 A RESOLUTION
Classification OXIDOREDUCTASE
Compound NAD(P)H DEHYDROGENASE [QUINONE] 1
Source Homo sapiens (Human) (NQO1_HUMAN)
Sequence B:  VGRRALIVLAHSERTSFNYAMKEAAAAALKKKGWEVVESD
LYAMNFNPIISRKDITGKLKDPANFQYPAESVLAYKEGHL
SPDIVAEQKKLEAADLVIFQFPLQWFGVPAILKGWFERVF
IGEFAYTYAAMYDKGPFRSKKAVLSITTGGSGSMYSLQGI
HGDMNVILWPIQSGILHFCGFQVLEPQLTYSIGHTPADAR
IQILEGWKKRLENIWDETPLYFAPSSLFDLNFQAGFLMKK
EVQDEEKNKKFGLSVGHHLGKSIPTDNQIKARK
D:  VGRRALIVLAHSERTSFNYAMKEAAAAALKKKGWEVVESD
LYAMNFNPIISRKDITGKLKDPANFQYPAESVLAYKEGHL
SPDIVAEQKKLEAADLVIFQFPLQWFGVPAILKGWFERVF
IGEFAYTYAAMYDKGPFRSKKAVLSITTGGSGSMYSLQGI
HGDMNVILWPIQSGILHFCGFQVLEPQLTYSIGHTPADAR
IQILEGWKKRLENIWDETPLYFAPSSLFDLNFQAGFLMKK
EVQDEEKNKKFGLSVGHHLGKSIPTDNQIKARK
Description


Functional site

1) chain B
residue 11
type
sequence H
description BINDING SITE FOR RESIDUE FAD B 602
source : AC2

2) chain B
residue 15
type
sequence T
description BINDING SITE FOR RESIDUE FAD B 602
source : AC2

3) chain B
residue 16
type
sequence S
description BINDING SITE FOR RESIDUE FAD B 602
source : AC2

4) chain B
residue 17
type
sequence F
description BINDING SITE FOR RESIDUE FAD B 602
source : AC2

5) chain B
residue 18
type
sequence N
description BINDING SITE FOR RESIDUE FAD B 602
source : AC2

6) chain B
residue 20
type
sequence A
description BINDING SITE FOR RESIDUE FAD B 602
source : AC2

7) chain B
residue 102
type
sequence P
description BINDING SITE FOR RESIDUE FAD B 602
source : AC2

8) chain B
residue 103
type
sequence L
description BINDING SITE FOR RESIDUE FAD B 602
source : AC2

9) chain B
residue 104
type
sequence Q
description BINDING SITE FOR RESIDUE FAD B 602
source : AC2

10) chain B
residue 105
type
sequence W
description BINDING SITE FOR RESIDUE FAD B 602
source : AC2

11) chain B
residue 106
type
sequence F
description BINDING SITE FOR RESIDUE FAD B 602
source : AC2

12) chain B
residue 147
type
sequence T
description BINDING SITE FOR RESIDUE FAD B 602
source : AC2

13) chain B
residue 148
type
sequence T
description BINDING SITE FOR RESIDUE FAD B 602
source : AC2

14) chain B
residue 149
type
sequence G
description BINDING SITE FOR RESIDUE FAD B 602
source : AC2

15) chain B
residue 150
type
sequence G
description BINDING SITE FOR RESIDUE FAD B 602
source : AC2

16) chain B
residue 155
type
sequence Y
description BINDING SITE FOR RESIDUE FAD B 602
source : AC2

17) chain B
residue 192
type
sequence I
description BINDING SITE FOR RESIDUE FAD B 602
source : AC2

18) chain B
residue 200
type
sequence R
description BINDING SITE FOR RESIDUE FAD B 602
source : AC2

19) chain B
residue 204
type
sequence L
description BINDING SITE FOR RESIDUE FAD B 602
source : AC2

20) chain D
residue 66
type
sequence Q
description BINDING SITE FOR RESIDUE FAD B 602
source : AC2

21) chain D
residue 67
type
sequence Y
description BINDING SITE FOR RESIDUE FAD B 602
source : AC2

22) chain B
residue 66
type
sequence Q
description BINDING SITE FOR RESIDUE FAD D 604
source : AC4

23) chain B
residue 67
type
sequence Y
description BINDING SITE FOR RESIDUE FAD D 604
source : AC4

24) chain B
residue 68
type
sequence P
description BINDING SITE FOR RESIDUE FAD D 604
source : AC4

25) chain D
residue 11
type
sequence H
description BINDING SITE FOR RESIDUE FAD D 604
source : AC4

26) chain D
residue 15
type
sequence T
description BINDING SITE FOR RESIDUE FAD D 604
source : AC4

27) chain D
residue 16
type
sequence S
description BINDING SITE FOR RESIDUE FAD D 604
source : AC4

28) chain D
residue 17
type
sequence F
description BINDING SITE FOR RESIDUE FAD D 604
source : AC4

29) chain D
residue 18
type
sequence N
description BINDING SITE FOR RESIDUE FAD D 604
source : AC4

30) chain D
residue 20
type
sequence A
description BINDING SITE FOR RESIDUE FAD D 604
source : AC4

31) chain D
residue 102
type
sequence P
description BINDING SITE FOR RESIDUE FAD D 604
source : AC4

32) chain D
residue 103
type
sequence L
description BINDING SITE FOR RESIDUE FAD D 604
source : AC4

33) chain D
residue 104
type
sequence Q
description BINDING SITE FOR RESIDUE FAD D 604
source : AC4

34) chain D
residue 105
type
sequence W
description BINDING SITE FOR RESIDUE FAD D 604
source : AC4

35) chain D
residue 106
type
sequence F
description BINDING SITE FOR RESIDUE FAD D 604
source : AC4

36) chain D
residue 147
type
sequence T
description BINDING SITE FOR RESIDUE FAD D 604
source : AC4

37) chain D
residue 148
type
sequence T
description BINDING SITE FOR RESIDUE FAD D 604
source : AC4

38) chain D
residue 149
type
sequence G
description BINDING SITE FOR RESIDUE FAD D 604
source : AC4

39) chain D
residue 150
type
sequence G
description BINDING SITE FOR RESIDUE FAD D 604
source : AC4

40) chain D
residue 155
type
sequence Y
description BINDING SITE FOR RESIDUE FAD D 604
source : AC4

41) chain D
residue 192
type
sequence I
description BINDING SITE FOR RESIDUE FAD D 604
source : AC4

42) chain D
residue 200
type
sequence R
description BINDING SITE FOR RESIDUE FAD D 604
source : AC4

43) chain B
residue 105
type
sequence W
description BINDING SITE FOR RESIDUE E09 D 702
source : AC6

44) chain B
residue 106
type
sequence F
description BINDING SITE FOR RESIDUE E09 D 702
source : AC6

45) chain B
residue 149
type
sequence G
description BINDING SITE FOR RESIDUE E09 D 702
source : AC6

46) chain B
residue 150
type
sequence G
description BINDING SITE FOR RESIDUE E09 D 702
source : AC6

47) chain B
residue 161
type
sequence H
description BINDING SITE FOR RESIDUE E09 D 702
source : AC6

48) chain D
residue 68
type
sequence P
description BINDING SITE FOR RESIDUE E09 D 702
source : AC6

49) chain D
residue 126
type
sequence Y
description BINDING SITE FOR RESIDUE E09 D 702
source : AC6

50) chain D
residue 128
type
sequence Y
description BINDING SITE FOR RESIDUE E09 D 702
source : AC6

51) chain D
residue 178
type
sequence F
description BINDING SITE FOR RESIDUE E09 D 702
source : AC6

52) chain B
residue 68
type
sequence P
description BINDING SITE FOR RESIDUE E09 B 704
source : AC8

53) chain B
residue 126
type
sequence Y
description BINDING SITE FOR RESIDUE E09 B 704
source : AC8

54) chain B
residue 128
type
sequence Y
description BINDING SITE FOR RESIDUE E09 B 704
source : AC8

55) chain B
residue 174
type
sequence G
description BINDING SITE FOR RESIDUE E09 B 704
source : AC8

56) chain B
residue 178
type
sequence F
description BINDING SITE FOR RESIDUE E09 B 704
source : AC8

57) chain D
residue 106
type
sequence F
description BINDING SITE FOR RESIDUE E09 B 704
source : AC8

58) chain D
residue 149
type
sequence G
description BINDING SITE FOR RESIDUE E09 B 704
source : AC8

59) chain D
residue 150
type
sequence G
description BINDING SITE FOR RESIDUE E09 B 704
source : AC8

60) chain D
residue 161
type
sequence H
description BINDING SITE FOR RESIDUE E09 B 704
source : AC8

61) chain B
residue 149
type catalytic
sequence G
description 3
source MCSA : MCSA2

62) chain B
residue 155
type catalytic
sequence Y
description 3
source MCSA : MCSA2

63) chain B
residue 161
type catalytic
sequence H
description 3
source MCSA : MCSA2

64) chain D
residue 149
type catalytic
sequence G
description 3
source MCSA : MCSA4

65) chain D
residue 155
type catalytic
sequence Y
description 3
source MCSA : MCSA4

66) chain D
residue 161
type catalytic
sequence H
description 3
source MCSA : MCSA4

67) chain B
residue 66
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:10543876, ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396
source Swiss-Prot : SWS_FT_FI1

68) chain B
residue 103
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:10543876, ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396
source Swiss-Prot : SWS_FT_FI1

69) chain B
residue 147
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:10543876, ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396
source Swiss-Prot : SWS_FT_FI1

70) chain B
residue 155
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:10543876, ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396
source Swiss-Prot : SWS_FT_FI1

71) chain B
residue 200
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:10543876, ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396
source Swiss-Prot : SWS_FT_FI1

72) chain D
residue 11
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:10543876, ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396
source Swiss-Prot : SWS_FT_FI1

73) chain D
residue 17
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:10543876, ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396
source Swiss-Prot : SWS_FT_FI1

74) chain D
residue 66
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:10543876, ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396
source Swiss-Prot : SWS_FT_FI1

75) chain D
residue 103
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:10543876, ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396
source Swiss-Prot : SWS_FT_FI1

76) chain D
residue 147
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:10543876, ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396
source Swiss-Prot : SWS_FT_FI1

77) chain D
residue 155
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:10543876, ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396
source Swiss-Prot : SWS_FT_FI1

78) chain D
residue 200
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:10543876, ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396
source Swiss-Prot : SWS_FT_FI1

79) chain B
residue 11
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:10543876, ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396
source Swiss-Prot : SWS_FT_FI1

80) chain B
residue 17
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:10543876, ECO:0000269|PubMed:10706635, ECO:0000269|PubMed:11735396
source Swiss-Prot : SWS_FT_FI1

81) chain B
residue 125
type BINDING
sequence A
description
source Swiss-Prot : SWS_FT_FI2

82) chain D
residue 125
type BINDING
sequence A
description
source Swiss-Prot : SWS_FT_FI2

83) chain B
residue 81
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI3

84) chain D
residue 81
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI3

85) chain D
residue 249
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI4

86) chain D
residue 250
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI4

87) chain B
residue 249
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI4

88) chain B
residue 250
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI4


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