eF-site ID 1gg5-B
PDB Code 1gg5
Chain B

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

36) 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

37) 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

38) 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

39) 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

40) 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

41) 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

42) 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

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

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

45) 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

46) 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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