eF-site ID 1oqb-ABCDEF
PDB Code 1oqb
Chain A, B, C, D, E, F

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Title The Crystal Structure of the one-iron form of the di-iron center in Stearoyl Acyl Carrier Protein Desaturase from Ricinus Communis (Castor Bean).
Classification OXIDOREDUCTASE
Compound Acyl-[acyl-carrier protein] desaturase
Source Ricinus communis (Castor bean) (STAD_RICCO)
Sequence A:  FMPPREVHVQVTHSMPPQKIEIFKSLDNWAEENILVHLKP
VEKCWQPQDFLPDPASDGFDEQVRELRERAKEIPDDYFVV
LVGDMITEEALPTYQTMLNTLDGVRDETGASPTSWAIWTR
AWTAEENRHGDLLNKYLYLSGRVDMRQIEKTIQYLIGSGM
DPRTENSPYLGFIYTSFQERATFISHGNTARQAKEHGDIK
LAQICGTIAADEKRHETAYTKIVEKLFEIDPDGTVLAFAD
MMRKKISMPAHLMYDGRDDNLFDHFSAVAQRLGVYTAKDY
ADILEFLVGRWKVDKLTGLSAEGQKAQDYVCRLPPRIRRL
EERAQGRAKEAPTMPFSWIFDRQVKL
B:  FMPPREVHVQVTHSMPPQKIEIFKSLDNWAEENILVHLKP
VEKCWQPQDFLPDPASDGFDEQVRELRERAKEIPDDYFVV
LVGDMITEEALPTYQTMLNTLDGVRDETGASPTSWAIWTR
AWTAEENRHGDLLNKYLYLSGRVDMRQIEKTIQYLIGSGM
DPRTENSPYLGFIYTSFQERATFISHGNTARQAKEHGDIK
LAQICGTIAADEKRHETAYTKIVEKLFEIDPDGTVLAFAD
MMRKKISMPAHLMYDGRDDNLFDHFSAVAQRLGVYTAKDY
ADILEFLVGRWKVDKLTGLSAEGQKAQDYVCRLPPRIRRL
EERAQGRAKEAPTMPFSWIFDRQVKL
C:  FMPPREVHVQVTHSMPPQKIEIFKSLDNWAEENILVHLKP
VEKCWQPQDFLPDPASDGFDEQVRELRERAKEIPDDYFVV
LVGDMITEEALPTYQTMLNTLDGVRDETGASPTSWAIWTR
AWTAEENRHGDLLNKYLYLSGRVDMRQIEKTIQYLIGSGM
DPRTENSPYLGFIYTSFQERATFISHGNTARQAKEHGDIK
LAQICGTIAADEKRHETAYTKIVEKLFEIDPDGTVLAFAD
MMRKKISMPAHLMYDGRDDNLFDHFSAVAQRLGVYTAKDY
ADILEFLVGRWKVDKLTGLSAEGQKAQDYVCRLPPRIRRL
EERAQGRAKEAPTMPFSWIFDRQVKL
D:  FMPPREVHVQVTHSMPPQKIEIFKSLDNWAEENILVHLKP
VEKCWQPQDFLPDPASDGFDEQVRELRERAKEIPDDYFVV
LVGDMITEEALPTYQTMLNTLDGVRDETGASPTSWAIWTR
AWTAEENRHGDLLNKYLYLSGRVDMRQIEKTIQYLIGSGM
DPRTENSPYLGFIYTSFQERATFISHGNTARQAKEHGDIK
LAQICGTIAADEKRHETAYTKIVEKLFEIDPDGTVLAFAD
MMRKKISMPAHLMYDGRDDNLFDHFSAVAQRLGVYTAKDY
ADILEFLVGRWKVDKLTGLSAEGQKAQDYVCRLPPRIRRL
EERAQGRAKEAPTMPFSWIFDRQVKL
E:  FMPPREVHVQVTHSMPPQKIEIFKSLDNWAEENILVHLKP
VEKCWQPQDFLPDPASDGFDEQVRELRERAKEIPDDYFVV
LVGDMITEEALPTYQTMLNTLDGVRDETGASPTSWAIWTR
AWTAEENRHGDLLNKYLYLSGRVDMRQIEKTIQYLIGSGM
DPRTENSPYLGFIYTSFQERATFISHGNTARQAKEHGDIK
LAQICGTIAADEKRHETAYTKIVEKLFEIDPDGTVLAFAD
MMRKKISMPAHLMYDGRDDNLFDHFSAVAQRLGVYTAKDY
ADILEFLVGRWKVDKLTGLSAEGQKAQDYVCRLPPRIRRL
EERAQGRAKEAPTMPFSWIFDRQVKL
F:  FMPPREVHVQVTHSMPPQKIEIFKSLDNWAEENILVHLKP
VEKCWQPQDFLPDPASDGFDEQVRELRERAKEIPDDYFVV
LVGDMITEEALPTYQTMLNTLDGVRDETGASPTSWAIWTR
AWTAEENRHGDLLNKYLYLSGRVDMRQIEKTIQYLIGSGM
DPRTENSPYLGFIYTSFQERATFISHGNTARQAKEHGDIK
LAQICGTIAADEKRHETAYTKIVEKLFEIDPDGTVLAFAD
MMRKKISMPAHLMYDGRDDNLFDHFSAVAQRLGVYTAKDY
ADILEFLVGRWKVDKLTGLSAEGQKAQDYVCRLPPRIRRL
EERAQGRAKEAPTMPFSWIFDRQVKL
Description


Functional site

1) chain A
residue 105
type
sequence E
description BINDING SITE FOR RESIDUE FE2 A 364
source : AC1

2) chain A
residue 143
type
sequence E
description BINDING SITE FOR RESIDUE FE2 A 364
source : AC1

3) chain A
residue 146
type
sequence H
description BINDING SITE FOR RESIDUE FE2 A 364
source : AC1

4) chain A
residue 229
type
sequence E
description BINDING SITE FOR RESIDUE FE2 A 364
source : AC1

5) chain B
residue 105
type
sequence E
description BINDING SITE FOR RESIDUE FE2 B 364
source : AC2

6) chain B
residue 143
type
sequence E
description BINDING SITE FOR RESIDUE FE2 B 364
source : AC2

7) chain B
residue 146
type
sequence H
description BINDING SITE FOR RESIDUE FE2 B 364
source : AC2

8) chain B
residue 229
type
sequence E
description BINDING SITE FOR RESIDUE FE2 B 364
source : AC2

9) chain C
residue 105
type
sequence E
description BINDING SITE FOR RESIDUE FE2 C 364
source : AC3

10) chain C
residue 143
type
sequence E
description BINDING SITE FOR RESIDUE FE2 C 364
source : AC3

11) chain C
residue 146
type
sequence H
description BINDING SITE FOR RESIDUE FE2 C 364
source : AC3

12) chain C
residue 229
type
sequence E
description BINDING SITE FOR RESIDUE FE2 C 364
source : AC3

13) chain D
residue 105
type
sequence E
description BINDING SITE FOR RESIDUE FE2 D 364
source : AC4

14) chain D
residue 143
type
sequence E
description BINDING SITE FOR RESIDUE FE2 D 364
source : AC4

15) chain D
residue 146
type
sequence H
description BINDING SITE FOR RESIDUE FE2 D 364
source : AC4

16) chain D
residue 229
type
sequence E
description BINDING SITE FOR RESIDUE FE2 D 364
source : AC4

17) chain E
residue 105
type
sequence E
description BINDING SITE FOR RESIDUE FE2 E 364
source : AC5

18) chain E
residue 143
type
sequence E
description BINDING SITE FOR RESIDUE FE2 E 364
source : AC5

19) chain E
residue 146
type
sequence H
description BINDING SITE FOR RESIDUE FE2 E 364
source : AC5

20) chain E
residue 229
type
sequence E
description BINDING SITE FOR RESIDUE FE2 E 364
source : AC5

21) chain F
residue 105
type
sequence E
description BINDING SITE FOR RESIDUE FE2 F 364
source : AC6

22) chain F
residue 143
type
sequence E
description BINDING SITE FOR RESIDUE FE2 F 364
source : AC6

23) chain F
residue 146
type
sequence H
description BINDING SITE FOR RESIDUE FE2 F 364
source : AC6

24) chain F
residue 229
type
sequence E
description BINDING SITE FOR RESIDUE FE2 F 364
source : AC6

25) chain A
residue 62
type catalytic
sequence W
description 136
source MCSA : MCSA1

26) chain A
residue 105
type catalytic
sequence E
description 136
source MCSA : MCSA1

27) chain A
residue 143
type catalytic
sequence E
description 136
source MCSA : MCSA1

28) chain A
residue 146
type catalytic
sequence H
description 136
source MCSA : MCSA1

29) chain A
residue 196
type catalytic
sequence E
description 136
source MCSA : MCSA1

30) chain A
residue 199
type catalytic
sequence T
description 136
source MCSA : MCSA1

31) chain A
residue 228
type catalytic
sequence D
description 136
source MCSA : MCSA1

32) chain A
residue 229
type catalytic
sequence E
description 136
source MCSA : MCSA1

33) chain A
residue 232
type catalytic
sequence H
description 136
source MCSA : MCSA1

34) chain B
residue 62
type catalytic
sequence W
description 136
source MCSA : MCSA2

35) chain B
residue 105
type catalytic
sequence E
description 136
source MCSA : MCSA2

36) chain B
residue 143
type catalytic
sequence E
description 136
source MCSA : MCSA2

37) chain B
residue 146
type catalytic
sequence H
description 136
source MCSA : MCSA2

38) chain B
residue 196
type catalytic
sequence E
description 136
source MCSA : MCSA2

39) chain B
residue 199
type catalytic
sequence T
description 136
source MCSA : MCSA2

40) chain B
residue 228
type catalytic
sequence D
description 136
source MCSA : MCSA2

41) chain B
residue 229
type catalytic
sequence E
description 136
source MCSA : MCSA2

42) chain B
residue 232
type catalytic
sequence H
description 136
source MCSA : MCSA2

43) chain C
residue 62
type catalytic
sequence W
description 136
source MCSA : MCSA3

44) chain C
residue 105
type catalytic
sequence E
description 136
source MCSA : MCSA3

45) chain C
residue 143
type catalytic
sequence E
description 136
source MCSA : MCSA3

46) chain C
residue 146
type catalytic
sequence H
description 136
source MCSA : MCSA3

47) chain C
residue 196
type catalytic
sequence E
description 136
source MCSA : MCSA3

48) chain C
residue 199
type catalytic
sequence T
description 136
source MCSA : MCSA3

49) chain C
residue 228
type catalytic
sequence D
description 136
source MCSA : MCSA3

50) chain C
residue 229
type catalytic
sequence E
description 136
source MCSA : MCSA3

51) chain C
residue 232
type catalytic
sequence H
description 136
source MCSA : MCSA3

52) chain D
residue 62
type catalytic
sequence W
description 136
source MCSA : MCSA4

53) chain D
residue 105
type catalytic
sequence E
description 136
source MCSA : MCSA4

54) chain D
residue 143
type catalytic
sequence E
description 136
source MCSA : MCSA4

55) chain D
residue 146
type catalytic
sequence H
description 136
source MCSA : MCSA4

56) chain D
residue 196
type catalytic
sequence E
description 136
source MCSA : MCSA4

57) chain D
residue 199
type catalytic
sequence T
description 136
source MCSA : MCSA4

58) chain D
residue 228
type catalytic
sequence D
description 136
source MCSA : MCSA4

59) chain D
residue 229
type catalytic
sequence E
description 136
source MCSA : MCSA4

60) chain D
residue 232
type catalytic
sequence H
description 136
source MCSA : MCSA4

61) chain E
residue 62
type catalytic
sequence W
description 136
source MCSA : MCSA5

62) chain E
residue 105
type catalytic
sequence E
description 136
source MCSA : MCSA5

63) chain E
residue 143
type catalytic
sequence E
description 136
source MCSA : MCSA5

64) chain E
residue 146
type catalytic
sequence H
description 136
source MCSA : MCSA5

65) chain E
residue 196
type catalytic
sequence E
description 136
source MCSA : MCSA5

66) chain E
residue 199
type catalytic
sequence T
description 136
source MCSA : MCSA5

67) chain E
residue 228
type catalytic
sequence D
description 136
source MCSA : MCSA5

68) chain E
residue 229
type catalytic
sequence E
description 136
source MCSA : MCSA5

69) chain E
residue 232
type catalytic
sequence H
description 136
source MCSA : MCSA5

70) chain F
residue 62
type catalytic
sequence W
description 136
source MCSA : MCSA6

71) chain F
residue 105
type catalytic
sequence E
description 136
source MCSA : MCSA6

72) chain F
residue 143
type catalytic
sequence E
description 136
source MCSA : MCSA6

73) chain F
residue 146
type catalytic
sequence H
description 136
source MCSA : MCSA6

74) chain F
residue 196
type catalytic
sequence E
description 136
source MCSA : MCSA6

75) chain F
residue 199
type catalytic
sequence T
description 136
source MCSA : MCSA6

76) chain F
residue 228
type catalytic
sequence D
description 136
source MCSA : MCSA6

77) chain F
residue 229
type catalytic
sequence E
description 136
source MCSA : MCSA6

78) chain F
residue 232
type catalytic
sequence H
description 136
source MCSA : MCSA6

79) chain A
residue 283-302
type prosite
sequence SAVAQRLGVYTAKDYADILE
description FATTY_ACID_DESATUR_2 Fatty acid desaturases family 2 signature. SAvaqRLgvytakDYadILE
source prosite : PS00574

80) chain A
residue 105
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

81) chain B
residue 196
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

82) chain B
residue 229
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

83) chain B
residue 232
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

84) chain C
residue 105
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

85) chain C
residue 143
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

86) chain C
residue 146
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

87) chain C
residue 196
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

88) chain C
residue 229
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

89) chain C
residue 232
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

90) chain D
residue 105
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

91) chain A
residue 143
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

92) chain D
residue 143
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

93) chain D
residue 146
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

94) chain D
residue 196
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

95) chain D
residue 229
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

96) chain D
residue 232
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

97) chain E
residue 105
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

98) chain E
residue 143
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

99) chain E
residue 146
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

100) chain E
residue 196
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

101) chain E
residue 229
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

102) chain A
residue 146
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

103) chain E
residue 232
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

104) chain F
residue 105
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

105) chain F
residue 143
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

106) chain F
residue 146
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

107) chain F
residue 196
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

108) chain F
residue 229
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

109) chain F
residue 232
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

110) chain A
residue 196
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

111) chain A
residue 229
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

112) chain A
residue 232
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

113) chain B
residue 105
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

114) chain B
residue 143
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1

115) chain B
residue 146
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:12704186, ECO:0000269|PubMed:17088542, ECO:0000269|PubMed:8861937
source Swiss-Prot : SWS_FT_FI1


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