eF-site ID 1amo-AB
PDB Code 1amo
Chain A, B

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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
B:  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 B
residue 319
type
sequence H
description BINDING SITE FOR RESIDUE FAD B 750
source : AC4

49) chain B
residue 424
type
sequence R
description BINDING SITE FOR RESIDUE FAD B 750
source : AC4

50) chain B
residue 454
type
sequence R
description BINDING SITE FOR RESIDUE FAD B 750
source : AC4

51) chain B
residue 455
type
sequence Y
description BINDING SITE FOR RESIDUE FAD B 750
source : AC4

52) chain B
residue 456
type
sequence Y
description BINDING SITE FOR RESIDUE FAD B 750
source : AC4

53) chain B
residue 457
type
sequence S
description BINDING SITE FOR RESIDUE FAD B 750
source : AC4

54) chain B
residue 472
type
sequence C
description BINDING SITE FOR RESIDUE FAD B 750
source : AC4

55) chain B
residue 473
type
sequence A
description BINDING SITE FOR RESIDUE FAD B 750
source : AC4

56) chain B
residue 474
type
sequence V
description BINDING SITE FOR RESIDUE FAD B 750
source : AC4

57) chain B
residue 478
type
sequence Y
description BINDING SITE FOR RESIDUE FAD B 750
source : AC4

58) chain B
residue 488
type
sequence G
description BINDING SITE FOR RESIDUE FAD B 750
source : AC4

59) chain B
residue 489
type
sequence V
description BINDING SITE FOR RESIDUE FAD B 750
source : AC4

60) chain B
residue 490
type
sequence A
description BINDING SITE FOR RESIDUE FAD B 750
source : AC4

61) chain B
residue 491
type
sequence T
description BINDING SITE FOR RESIDUE FAD B 750
source : AC4

62) chain B
residue 538
type
sequence A
description BINDING SITE FOR RESIDUE FAD B 750
source : AC4

63) chain B
residue 677
type
sequence W
description BINDING SITE FOR RESIDUE FAD B 750
source : AC4

64) chain B
residue 86
type
sequence S
description BINDING SITE FOR RESIDUE FMN B 751
source : AC5

65) chain B
residue 87
type
sequence Q
description BINDING SITE FOR RESIDUE FMN B 751
source : AC5

66) chain B
residue 88
type
sequence T
description BINDING SITE FOR RESIDUE FMN B 751
source : AC5

67) chain B
residue 89
type
sequence G
description BINDING SITE FOR RESIDUE FMN B 751
source : AC5

68) chain B
residue 90
type
sequence T
description BINDING SITE FOR RESIDUE FMN B 751
source : AC5

69) chain B
residue 91
type
sequence A
description BINDING SITE FOR RESIDUE FMN B 751
source : AC5

70) chain B
residue 138
type
sequence A
description BINDING SITE FOR RESIDUE FMN B 751
source : AC5

71) chain B
residue 139
type
sequence T
description BINDING SITE FOR RESIDUE FMN B 751
source : AC5

72) chain B
residue 140
type
sequence Y
description BINDING SITE FOR RESIDUE FMN B 751
source : AC5

73) chain B
residue 141
type
sequence G
description BINDING SITE FOR RESIDUE FMN B 751
source : AC5

74) chain B
residue 143
type
sequence G
description BINDING SITE FOR RESIDUE FMN B 751
source : AC5

75) chain B
residue 173
type
sequence L
description BINDING SITE FOR RESIDUE FMN B 751
source : AC5

76) chain B
residue 174
type
sequence G
description BINDING SITE FOR RESIDUE FMN B 751
source : AC5

77) chain B
residue 175
type
sequence N
description BINDING SITE FOR RESIDUE FMN B 751
source : AC5

78) chain B
residue 180
type
sequence H
description BINDING SITE FOR RESIDUE FMN B 751
source : AC5

79) chain B
residue 181
type
sequence F
description BINDING SITE FOR RESIDUE FMN B 751
source : AC5

80) chain B
residue 182
type
sequence N
description BINDING SITE FOR RESIDUE FMN B 751
source : AC5

81) chain B
residue 208
type
sequence D
description BINDING SITE FOR RESIDUE FMN B 751
source : AC5

82) chain B
residue 212
type
sequence L
description BINDING SITE FOR RESIDUE FMN B 751
source : AC5

83) chain B
residue 298
type
sequence R
description BINDING SITE FOR RESIDUE NAP B 752
source : AC6

84) chain B
residue 534
type
sequence G
description BINDING SITE FOR RESIDUE NAP B 752
source : AC6

85) chain B
residue 535
type
sequence T
description BINDING SITE FOR RESIDUE NAP B 752
source : AC6

86) chain B
residue 566
type
sequence C
description BINDING SITE FOR RESIDUE NAP B 752
source : AC6

87) chain B
residue 567
type
sequence R
description BINDING SITE FOR RESIDUE NAP B 752
source : AC6

88) chain B
residue 596
type
sequence S
description BINDING SITE FOR RESIDUE NAP B 752
source : AC6

89) chain B
residue 597
type
sequence R
description BINDING SITE FOR RESIDUE NAP B 752
source : AC6

90) chain B
residue 602
type
sequence K
description BINDING SITE FOR RESIDUE NAP B 752
source : AC6

91) chain B
residue 604
type
sequence Y
description BINDING SITE FOR RESIDUE NAP B 752
source : AC6

92) chain B
residue 606
type
sequence Q
description BINDING SITE FOR RESIDUE NAP B 752
source : AC6

93) chain B
residue 636
type
sequence M
description BINDING SITE FOR RESIDUE NAP B 752
source : AC6

94) chain B
residue 639
type
sequence D
description BINDING SITE FOR RESIDUE NAP B 752
source : AC6

95) 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

96) 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

97) chain B
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

98) chain B
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

99) chain B
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

100) chain B
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

101) chain B
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

102) chain B
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

103) chain B
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

104) chain B
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

105) chain B
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

106) 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

107) chain B
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

108) 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

109) 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

110) 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

111) 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

112) 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

113) 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

114) 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

115) 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

116) chain B
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

117) 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

118) 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

119) chain B
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

120) chain B
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

121) 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

122) chain B
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

123) 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

124) chain B
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

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

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

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

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

129) chain B
residue 458
type catalytic
sequence I
description 117
source MCSA : MCSA2

130) chain B
residue 631
type catalytic
sequence G
description 117
source MCSA : MCSA2

131) chain B
residue 676
type catalytic
sequence V
description 117
source MCSA : MCSA2

132) chain B
residue 678
type catalytic
sequence S
description 117
source MCSA : MCSA2


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