eF-site ID 6c12-ABCD
PDB Code 6c12
Chain A, B, C, D

click to enlarge
Title SDHA-SDHE complex
Classification Oxidoreductase/Chaperon
Compound Succinate dehydrogenase flavoprotein subunit
Source (SDHE_ECOLI)
Sequence A:  MKLPVREFDAVVIGAGGAGMRAALQISQSGQTCALLSKVF
PTRSHTVSAQGHMYDTVKGSDYIGDQDAIEYMCKTGPEAI
LELEHMGLPFADRTGHALLHTLYQQNLKNHTTIFSEWYAL
DLVKNQDGAVVGCTALCIETGEVVYFKARATVLATGGAGR
IYQSTTNAHINTGDGVGMAIRAGVPVQDMEMWQFHPTGIA
GAGVLVTEGCRGEGGYLLNKHGERFMERYAPNAKDLAGRD
VVARSIMIEIREGRGCDGPWGPHAKLKLDHLGKEVLESRL
PGILELSRTFAHVDPVKEPIPVIPTCHYMMGGIPTKVTGQ
ALTVNEKGEDVVVPGLFAVGEIACVSVHGANRLGGNSLLD
LVVFGRAAGLHLQESIAEQGALRDASESDVEASLDRLNRW
NNNRNGEDPVAIRKALQECMQHNFSVFREGDAMAKGLEQL
KVIRERLKNARLDDTSSEFNTQRVECLELDNLMETAYATA
VSANFRTESRGAHSRFDFPDRDDENWLCHSLYLPESESMT
RRSVNMEPKLRPAFPP
B:  MKLPVREFDAVVIGAGGAGMRAALQISQSGQTCALLSKVF
PTRSHTVSAQGGNWEWHMYDTVKGSDYIGDQDAIEYMCKT
GPEAILELEHMADRTGHALLHTLYQQNLKNHTTIFSEWYA
LDLVKNQDGAVVGCTALCIETGEVVYFKARATVLATGGAG
RIYQSTTNAHINTGDGVGMAIRAGVPVQDMEMWQFHPTGI
AGAGVLVTEGCRGEGGYLLNKHGERFMERYAPNAKDLAGR
DVVARSIMIEIREGRGCDGPWGPHAKLKLDHLGKEVLESR
LPGILELSRTFAHVDPVKEPIPVIPTCHYMMGGIPTKVTG
QALTVNEKGEDVVVPGLFAVGEIACVSVHGANRLGGNSLL
DLVVFGRAAGLHLQESIAEQGALRDASESDVEASLDRLNR
WNNNRNGEDPVAIRKALQECMQHNFSVFREGDAMAKGLEQ
LKVIRERLKNARLDDTSSEFNTQRVECLELDNLMETAYAT
AVSANFRTESRGAHSRFDFPDRDDENWLCHSLYLPESESM
TRRSVNMEPKLRPAFPP
C:  DINNKARIHWACRRGMRELDISIMPFFEHEYDSLSDDEKR
IFIRLLECDDPDLFNWLMNHGKPADAELEMMVRLIQTRNR
ERGPV
D:  DINNKARIHWACRRGMRELDISIMPFFEHEYDSLSDDEKR
IFIRLLECDDPDLFNWLMNHGKPADAELEMMVRLIQTRNR
ERGPVA
Description


Functional site

1) chain B
residue 14
type
sequence G
description binding site for residue FAD B 601
source : AC1

2) chain B
residue 15
type
sequence A
description binding site for residue FAD B 601
source : AC1

3) chain B
residue 16
type
sequence G
description binding site for residue FAD B 601
source : AC1

4) chain B
residue 17
type
sequence G
description binding site for residue FAD B 601
source : AC1

5) chain B
residue 18
type
sequence A
description binding site for residue FAD B 601
source : AC1

6) chain B
residue 37
type
sequence S
description binding site for residue FAD B 601
source : AC1

7) chain B
residue 38
type
sequence K
description binding site for residue FAD B 601
source : AC1

8) chain B
residue 39
type
sequence V
description binding site for residue FAD B 601
source : AC1

9) chain B
residue 44
type
sequence S
description binding site for residue FAD B 601
source : AC1

10) chain B
residue 45
type
sequence H
description binding site for residue FAD B 601
source : AC1

11) chain B
residue 46
type
sequence T
description binding site for residue FAD B 601
source : AC1

12) chain B
residue 48
type
sequence S
description binding site for residue FAD B 601
source : AC1

13) chain B
residue 49
type
sequence A
description binding site for residue FAD B 601
source : AC1

14) chain B
residue 50
type
sequence Q
description binding site for residue FAD B 601
source : AC1

15) chain B
residue 164
type
sequence W
description binding site for residue FAD B 601
source : AC1

16) chain B
residue 165
type
sequence Y
description binding site for residue FAD B 601
source : AC1

17) chain B
residue 166
type
sequence A
description binding site for residue FAD B 601
source : AC1

18) chain B
residue 201
type
sequence A
description binding site for residue FAD B 601
source : AC1

19) chain B
residue 202
type
sequence T
description binding site for residue FAD B 601
source : AC1

20) chain B
residue 203
type
sequence G
description binding site for residue FAD B 601
source : AC1

21) chain B
residue 213
type
sequence T
description binding site for residue FAD B 601
source : AC1

22) chain B
residue 214
type
sequence N
description binding site for residue FAD B 601
source : AC1

23) chain B
residue 221
type
sequence D
description binding site for residue FAD B 601
source : AC1

24) chain B
residue 354
type
sequence H
description binding site for residue FAD B 601
source : AC1

25) chain B
residue 355
type
sequence Y
description binding site for residue FAD B 601
source : AC1

26) chain B
residue 387
type
sequence G
description binding site for residue FAD B 601
source : AC1

27) chain B
residue 388
type
sequence E
description binding site for residue FAD B 601
source : AC1

28) chain B
residue 402
type
sequence G
description binding site for residue FAD B 601
source : AC1

29) chain B
residue 404
type
sequence S
description binding site for residue FAD B 601
source : AC1

30) chain B
residue 405
type
sequence L
description binding site for residue FAD B 601
source : AC1

31) chain B
residue 408
type
sequence L
description binding site for residue FAD B 601
source : AC1

32) chain B
residue 356
type
sequence M
description binding site for residue NA B 602
source : AC2

33) chain B
residue 357
type
sequence M
description binding site for residue NA B 602
source : AC2

34) chain B
residue 358
type
sequence G
description binding site for residue NA B 602
source : AC2

35) chain B
residue 388
type
sequence E
description binding site for residue NA B 602
source : AC2

36) chain B
residue 390
type
sequence A
description binding site for residue NA B 602
source : AC2

37) chain A
residue 356
type
sequence M
description binding site for residue NA A 602
source : AC3

38) chain A
residue 357
type
sequence M
description binding site for residue NA A 602
source : AC3

39) chain A
residue 358
type
sequence G
description binding site for residue NA A 602
source : AC3

40) chain A
residue 388
type
sequence E
description binding site for residue NA A 602
source : AC3

41) chain A
residue 390
type
sequence A
description binding site for residue NA A 602
source : AC3

42) chain A
residue 14
type
sequence G
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

43) chain A
residue 15
type
sequence A
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

44) chain A
residue 16
type
sequence G
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

45) chain A
residue 17
type
sequence G
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

46) chain A
residue 18
type
sequence A
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

47) chain A
residue 37
type
sequence S
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

48) chain A
residue 38
type
sequence K
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

49) chain A
residue 39
type
sequence V
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

50) chain A
residue 44
type
sequence S
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

51) chain A
residue 46
type
sequence T
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

52) chain A
residue 47
type
sequence V
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

53) chain A
residue 48
type
sequence S
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

54) chain A
residue 49
type
sequence A
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

55) chain A
residue 50
type
sequence Q
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

56) chain A
residue 51
type
sequence G
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

57) chain A
residue 164
type
sequence W
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

58) chain A
residue 165
type
sequence Y
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

59) chain A
residue 166
type
sequence A
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

60) chain A
residue 201
type
sequence A
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

61) chain A
residue 202
type
sequence T
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

62) chain A
residue 203
type
sequence G
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

63) chain A
residue 213
type
sequence T
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

64) chain A
residue 214
type
sequence N
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

65) chain A
residue 215
type
sequence A
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

66) chain A
residue 221
type
sequence D
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

67) chain A
residue 354
type
sequence H
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

68) chain A
residue 355
type
sequence Y
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

69) chain A
residue 387
type
sequence G
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

70) chain A
residue 388
type
sequence E
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

71) chain A
residue 402
type
sequence G
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

72) chain A
residue 404
type
sequence S
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

73) chain A
residue 405
type
sequence L
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

74) chain A
residue 408
type
sequence L
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

75) chain C
residue 16
type
sequence G
description binding site for Di-peptide FAD A 601 and HIS A 45
source : AC4

76) chain B
residue 267
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:18723842
source Swiss-Prot : SWS_FT_FI5

77) chain A
residue 267
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000269|PubMed:18723842
source Swiss-Prot : SWS_FT_FI5

78) chain B
residue 43-52
type prosite
sequence RSHTVSAQGG
description FRD_SDH_FAD_BINDING Fumarate reductase / succinate dehydrogenase FAD-binding site. RSHTvsAqGG
source prosite : PS00504

79) chain B
residue 354
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:19710024
source Swiss-Prot : SWS_FT_FI3

80) chain B
residue 399
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:19710024
source Swiss-Prot : SWS_FT_FI3

81) chain A
residue 242
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:19710024
source Swiss-Prot : SWS_FT_FI3

82) chain A
residue 254
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:19710024
source Swiss-Prot : SWS_FT_FI3

83) chain A
residue 354
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:19710024
source Swiss-Prot : SWS_FT_FI3

84) chain A
residue 399
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:19710024
source Swiss-Prot : SWS_FT_FI3

85) chain B
residue 242
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:19710024
source Swiss-Prot : SWS_FT_FI3

86) chain B
residue 254
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:19710024
source Swiss-Prot : SWS_FT_FI3

87) chain B
residue 45
type MOD_RES
sequence H
description Tele-8alpha-FAD histidine => ECO:0000269|PubMed:12560550, ECO:0000269|PubMed:16407191, ECO:0000269|PubMed:19710024
source Swiss-Prot : SWS_FT_FI4

88) chain A
residue 45
type MOD_RES
sequence H
description Tele-8alpha-FAD histidine => ECO:0000269|PubMed:12560550, ECO:0000269|PubMed:16407191, ECO:0000269|PubMed:19710024
source Swiss-Prot : SWS_FT_FI4

89) chain B
residue 286
type ACT_SITE
sequence R
description Proton acceptor => ECO:0000269|PubMed:19710024
source Swiss-Prot : SWS_FT_FI1

90) chain A
residue 286
type ACT_SITE
sequence R
description Proton acceptor => ECO:0000269|PubMed:19710024
source Swiss-Prot : SWS_FT_FI1

91) chain B
residue 221
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:12560550, ECO:0000269|PubMed:16407191, ECO:0000269|PubMed:19710024
source Swiss-Prot : SWS_FT_FI2

92) chain B
residue 388
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12560550, ECO:0000269|PubMed:16407191, ECO:0000269|PubMed:19710024
source Swiss-Prot : SWS_FT_FI2

93) chain B
residue 14
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:12560550, ECO:0000269|PubMed:16407191, ECO:0000269|PubMed:19710024
source Swiss-Prot : SWS_FT_FI2

94) chain B
residue 37
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:12560550, ECO:0000269|PubMed:16407191, ECO:0000269|PubMed:19710024
source Swiss-Prot : SWS_FT_FI2

95) chain B
residue 404
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:12560550, ECO:0000269|PubMed:16407191, ECO:0000269|PubMed:19710024
source Swiss-Prot : SWS_FT_FI2

96) chain A
residue 14
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:12560550, ECO:0000269|PubMed:16407191, ECO:0000269|PubMed:19710024
source Swiss-Prot : SWS_FT_FI2

97) chain A
residue 37
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:12560550, ECO:0000269|PubMed:16407191, ECO:0000269|PubMed:19710024
source Swiss-Prot : SWS_FT_FI2

98) chain A
residue 221
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:12560550, ECO:0000269|PubMed:16407191, ECO:0000269|PubMed:19710024
source Swiss-Prot : SWS_FT_FI2

99) chain A
residue 388
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12560550, ECO:0000269|PubMed:16407191, ECO:0000269|PubMed:19710024
source Swiss-Prot : SWS_FT_FI2

100) chain A
residue 404
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:12560550, ECO:0000269|PubMed:16407191, ECO:0000269|PubMed:19710024
source Swiss-Prot : SWS_FT_FI2


Display surface

Download
Links