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

click to enlarge
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

Display surface

Download
Links