eF-site ID 1amo-A
PDB Code 1amo
Chain A

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Title THREE-DIMENSIONAL STRUCTURE OF NADPH-CYTOCHROME P450 REDUCTASE: PROTOTYPE FOR FMN-AND FAD-CONTAINING ENZYMES
Classification OXIDOREDUCTASE
Compound NADPH-CYTOCHROME P450 REDUCTASE
Source Rattus norvegicus (Rat) (NCPR_RAT)
Sequence A:  VKESSFVEKMKKTGRNIIVFYGSQTGTAEEFANRLSKDAH
RYGMRGMSADPEEYDLADLSSLPEIDKSLVVFCMATYGEG
DPTDNAQDFYDWLQETDVDLTGVKFAVFGLGNKTYEHFNA
MGKYVDQRLEQLGAQRIFELGLGDDDGNLEEDFITWREQF
WPAVCEFFGVEARQYELVVHEDMDVAKVYTGEMGRLKSYE
NQKPPFDAKNPFLAAVTANRKLNQGTERHLMHLELDISDS
KIRYESGDHVAVYPANDSALVNQIGEILGADLDVIMSLNN
LDEESNKKHPFPCPTTYRTALTYYLDITNPPRTNVLYELA
QYASEPSEQEHLHKMASSSGEGKELYLSWVVEARRHILAI
LQDYPSLRPPIDHLCELLPRLQARYYSIASSSKVHPNSVH
ICAVAVEYEAKSGRVNKGVATSWLRAKEPALVPMFVRKSQ
FRLPFKSTTPVIMVGPGTGIAPFMGFIQERAWLREQGKEV
GETLLYYGCRRSDEDYLYREELARFHKDGALTQLNVAFSR
EQAHKVYVQHLLKRDREHLWKLIHEGGAHIYVCGDARNMA
KDVQNTFYDIVAEFGPMEHTQAVDYVKKLMTKGRYSLDVW
S
Description


Functional site

1) chain A
residue 319
type
sequence H
description BINDING SITE FOR RESIDUE FAD A 750
source : AC1

2) chain A
residue 424
type
sequence R
description BINDING SITE FOR RESIDUE FAD A 750
source : AC1

3) chain A
residue 454
type
sequence R
description BINDING SITE FOR RESIDUE FAD A 750
source : AC1

4) chain A
residue 455
type
sequence Y
description BINDING SITE FOR RESIDUE FAD A 750
source : AC1

5) chain A
residue 456
type
sequence Y
description BINDING SITE FOR RESIDUE FAD A 750
source : AC1

6) chain A
residue 457
type
sequence S
description BINDING SITE FOR RESIDUE FAD A 750
source : AC1

7) chain A
residue 472
type
sequence C
description BINDING SITE FOR RESIDUE FAD A 750
source : AC1

8) chain A
residue 473
type
sequence A
description BINDING SITE FOR RESIDUE FAD A 750
source : AC1

9) chain A
residue 474
type
sequence V
description BINDING SITE FOR RESIDUE FAD A 750
source : AC1

10) chain A
residue 478
type
sequence Y
description BINDING SITE FOR RESIDUE FAD A 750
source : AC1

11) chain A
residue 488
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 750
source : AC1

12) chain A
residue 489
type
sequence V
description BINDING SITE FOR RESIDUE FAD A 750
source : AC1

13) chain A
residue 490
type
sequence A
description BINDING SITE FOR RESIDUE FAD A 750
source : AC1

14) chain A
residue 491
type
sequence T
description BINDING SITE FOR RESIDUE FAD A 750
source : AC1

15) chain A
residue 538
type
sequence A
description BINDING SITE FOR RESIDUE FAD A 750
source : AC1

16) chain A
residue 677
type
sequence W
description BINDING SITE FOR RESIDUE FAD A 750
source : AC1

17) chain A
residue 86
type
sequence S
description BINDING SITE FOR RESIDUE FMN A 751
source : AC2

18) chain A
residue 87
type
sequence Q
description BINDING SITE FOR RESIDUE FMN A 751
source : AC2

19) chain A
residue 88
type
sequence T
description BINDING SITE FOR RESIDUE FMN A 751
source : AC2

20) chain A
residue 89
type
sequence G
description BINDING SITE FOR RESIDUE FMN A 751
source : AC2

21) chain A
residue 90
type
sequence T
description BINDING SITE FOR RESIDUE FMN A 751
source : AC2

22) chain A
residue 91
type
sequence A
description BINDING SITE FOR RESIDUE FMN A 751
source : AC2

23) chain A
residue 138
type
sequence A
description BINDING SITE FOR RESIDUE FMN A 751
source : AC2

24) chain A
residue 139
type
sequence T
description BINDING SITE FOR RESIDUE FMN A 751
source : AC2

25) chain A
residue 140
type
sequence Y
description BINDING SITE FOR RESIDUE FMN A 751
source : AC2

26) chain A
residue 141
type
sequence G
description BINDING SITE FOR RESIDUE FMN A 751
source : AC2

27) chain A
residue 143
type
sequence G
description BINDING SITE FOR RESIDUE FMN A 751
source : AC2

28) chain A
residue 173
type
sequence L
description BINDING SITE FOR RESIDUE FMN A 751
source : AC2

29) chain A
residue 174
type
sequence G
description BINDING SITE FOR RESIDUE FMN A 751
source : AC2

30) chain A
residue 175
type
sequence N
description BINDING SITE FOR RESIDUE FMN A 751
source : AC2

31) chain A
residue 180
type
sequence H
description BINDING SITE FOR RESIDUE FMN A 751
source : AC2

32) chain A
residue 181
type
sequence F
description BINDING SITE FOR RESIDUE FMN A 751
source : AC2

33) chain A
residue 182
type
sequence N
description BINDING SITE FOR RESIDUE FMN A 751
source : AC2

34) chain A
residue 208
type
sequence D
description BINDING SITE FOR RESIDUE FMN A 751
source : AC2

35) chain A
residue 212
type
sequence L
description BINDING SITE FOR RESIDUE FMN A 751
source : AC2

36) chain A
residue 298
type
sequence R
description BINDING SITE FOR RESIDUE NAP A 752
source : AC3

37) chain A
residue 534
type
sequence G
description BINDING SITE FOR RESIDUE NAP A 752
source : AC3

38) chain A
residue 535
type
sequence T
description BINDING SITE FOR RESIDUE NAP A 752
source : AC3

39) chain A
residue 566
type
sequence C
description BINDING SITE FOR RESIDUE NAP A 752
source : AC3

40) chain A
residue 567
type
sequence R
description BINDING SITE FOR RESIDUE NAP A 752
source : AC3

41) chain A
residue 596
type
sequence S
description BINDING SITE FOR RESIDUE NAP A 752
source : AC3

42) chain A
residue 597
type
sequence R
description BINDING SITE FOR RESIDUE NAP A 752
source : AC3

43) chain A
residue 602
type
sequence K
description BINDING SITE FOR RESIDUE NAP A 752
source : AC3

44) chain A
residue 604
type
sequence Y
description BINDING SITE FOR RESIDUE NAP A 752
source : AC3

45) chain A
residue 606
type
sequence Q
description BINDING SITE FOR RESIDUE NAP A 752
source : AC3

46) chain A
residue 636
type
sequence M
description BINDING SITE FOR RESIDUE NAP A 752
source : AC3

47) chain A
residue 639
type
sequence D
description BINDING SITE FOR RESIDUE NAP A 752
source : AC3

48) chain A
residue 458
type catalytic
sequence I
description 117
source MCSA : MCSA1

49) chain A
residue 631
type catalytic
sequence G
description 117
source MCSA : MCSA1

50) chain A
residue 676
type catalytic
sequence V
description 117
source MCSA : MCSA1

51) chain A
residue 678
type catalytic
sequence S
description 117
source MCSA : MCSA1

52) chain A
residue 87
type BINDING
sequence Q
description BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990, ECO:0000269|Ref.8
source Swiss-Prot : SWS_FT_FI1

53) chain A
residue 678
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990, ECO:0000269|Ref.8
source Swiss-Prot : SWS_FT_FI1

54) chain A
residue 139
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990, ECO:0000269|Ref.8
source Swiss-Prot : SWS_FT_FI1

55) chain A
residue 174
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990, ECO:0000269|Ref.8
source Swiss-Prot : SWS_FT_FI1

56) chain A
residue 455
type BINDING
sequence Y
description BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990, ECO:0000269|Ref.8
source Swiss-Prot : SWS_FT_FI1

57) chain A
residue 479
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990, ECO:0000269|Ref.8
source Swiss-Prot : SWS_FT_FI1

58) chain A
residue 489
type BINDING
sequence V
description BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990, ECO:0000269|Ref.8
source Swiss-Prot : SWS_FT_FI1

59) chain A
residue 536
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990, ECO:0000269|Ref.8
source Swiss-Prot : SWS_FT_FI1

60) chain A
residue 597
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990, ECO:0000269|Ref.8
source Swiss-Prot : SWS_FT_FI1

61) chain A
residue 603
type BINDING
sequence V
description BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990, ECO:0000269|Ref.8
source Swiss-Prot : SWS_FT_FI1

62) chain A
residue 209
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990
source Swiss-Prot : SWS_FT_FI2

63) chain A
residue 299
type BINDING
sequence H
description BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990
source Swiss-Prot : SWS_FT_FI3

64) chain A
residue 640
type BINDING
sequence V
description BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990
source Swiss-Prot : SWS_FT_FI3

65) chain A
residue 425
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:21345800, ECO:0000269|Ref.8
source Swiss-Prot : SWS_FT_FI4

66) chain A
residue 473
type BINDING
sequence A
description BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:9237990, ECO:0000269|Ref.8
source Swiss-Prot : SWS_FT_FI5


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