eF-site ID 1gg5-D
PDB Code 1gg5
Chain 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 D:  VGRRALIVLAHSERTSFNYAMKEAAAAALKKKGWEVVESD
LYAMNFNPIISRKDITGKLKDPANFQYPAESVLAYKEGHL
SPDIVAEQKKLEAADLVIFQFPLQWFGVPAILKGWFERVF
IGEFAYTYAAMYDKGPFRSKKAVLSITTGGSGSMYSLQGI
HGDMNVILWPIQSGILHFCGFQVLEPQLTYSIGHTPADAR
IQILEGWKKRLENIWDETPLYFAPSSLFDLNFQAGFLMKK
EVQDEEKNKKFGLSVGHHLGKSIPTDNQIKARK
Description


Functional site

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

32) 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

33) 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

34) 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

35) 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

36) 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

37) 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

38) 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

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

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

41) 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

42) 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


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