eF-site ID 3aec-ABCD
PDB Code 3aec
Chain A, B, C, D

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Title Crystal structure of porcine heart mitochondrial complex II bound with 2-Iodo-N-(1-methylethyl)-benzamid
Classification OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR
Compound Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial
Source ORGANISM_COMMON: Pig; ORGANISM_SCIENTIFIC: Sus scrofa;
Sequence A:  STQYPVVDHEFDAVVVGAGGAGLRAAFGLSEAGFNTACVT
KLFPTRSHTVAAQGGINAALGNMEEDNWRWHFYDTVKGSD
WLGDQDAIHYMTEQAPASVVELENYGMPFSRTEDGKIYQR
AFGGQSLKFGKGGQAHRCCCVADRTGHSLLHTLYGRSLRY
DTSYFVEYFALDLLMENGECRGVIALCIEDGSIHRIRARN
TVVATGGYGRTYFSCTSAHTSTGDGTAMVTRAGLPCQDLE
FVQFHPTGIYGAGCLITEGCRGEGGILINSQGERFMERYA
PVAKDLASRDVVSRSMTLEIREGRGCGPEKDHVYLQLHHL
PPEQLAVRLPGISETAMIFAGVDVTKEPIPVLPTVHYNMG
GIPTNYKGQVLRHVNGQDQVVPGLYACGEAACASVHGANR
LGANSLLDLVVFGRACALSIAESCRPGDKVPSIKPNAGEE
SVMNLDKLRFANGTIRTSELRLSMQKSMQSHAAVFRVGSV
LQEGCEKILRLYGDLQHLKTFDRGMVWNTDLVETLELQNL
MLCALQTIYGAEARKESRGAHAREDFKERVDEYDYSKPIQ
GQQKKPFQEHWRKHTLSYVDVKTGKVSLEYRPVIDKTLNE
ADCATVPPAIRSY
B:  PRIKKFAIYRWDPDKTGDKPHMQTYEIDLNNCGPMVLDAL
IKIKNEIDSTLTFRRSCREGICGSCAMNINGGNTLACTRR
IDTNLDKVSKIYPLPHMYVIKDLVPDLSNFYAQYKSIEPY
LKKKDESQEGKQQYLQSIEEREKLDGLYECILCACCSTSC
PSYWWNGDKYLGPAVLMQAYRWMIDSRDDFTEERLAKLQD
PFSLYRCHTIMNCTGTCPKGLNPGKAIAEIKKMMATYKE
C:  TTAKEEMERFWNKNLGSNRPLSPHITIYRWSLPMAMSICH
RGTGIALSAGVSLFGLSALLLPGNFESHLELVKSLCLGPT
LIYTAKFGIVFPLMYHTWNGIRHLIWDLGKGLTIPQLTQS
GVVVLILTVLSSVGLAAM
D:  SSKAASLHWTGERVVSVLLLGLLPAAYLNPCSAMDYSLAA
ALTLHGHWGIGQVVTDYVRGDALQKAAKAGLLALSAFTFA
GLCYFNYHDVGICKAVAMLWKL
Description


Functional site

1) chain A
residue 26
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 700
source : AC1

2) chain A
residue 27
type
sequence A
description BINDING SITE FOR RESIDUE FAD A 700
source : AC1

3) chain A
residue 28
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 700
source : AC1

4) chain A
residue 29
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 700
source : AC1

5) chain A
residue 30
type
sequence A
description BINDING SITE FOR RESIDUE FAD A 700
source : AC1

6) chain A
residue 49
type
sequence T
description BINDING SITE FOR RESIDUE FAD A 700
source : AC1

7) chain A
residue 50
type
sequence K
description BINDING SITE FOR RESIDUE FAD A 700
source : AC1

8) chain A
residue 51
type
sequence L
description BINDING SITE FOR RESIDUE FAD A 700
source : AC1

9) chain A
residue 56
type
sequence S
description BINDING SITE FOR RESIDUE FAD A 700
source : AC1

10) chain A
residue 57
type
sequence H
description BINDING SITE FOR RESIDUE FAD A 700
source : AC1

11) chain A
residue 58
type
sequence T
description BINDING SITE FOR RESIDUE FAD A 700
source : AC1

12) chain A
residue 60
type
sequence A
description BINDING SITE FOR RESIDUE FAD A 700
source : AC1

13) chain A
residue 61
type
sequence A
description BINDING SITE FOR RESIDUE FAD A 700
source : AC1

14) chain A
residue 62
type
sequence Q
description BINDING SITE FOR RESIDUE FAD A 700
source : AC1

15) chain A
residue 63
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 700
source : AC1

16) chain A
residue 64
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 700
source : AC1

17) chain A
residue 177
type
sequence Y
description BINDING SITE FOR RESIDUE FAD A 700
source : AC1

18) chain A
residue 178
type
sequence F
description BINDING SITE FOR RESIDUE FAD A 700
source : AC1

19) chain A
residue 179
type
sequence A
description BINDING SITE FOR RESIDUE FAD A 700
source : AC1

20) chain A
residue 214
type
sequence T
description BINDING SITE FOR RESIDUE FAD A 700
source : AC1

21) chain A
residue 215
type
sequence G
description BINDING SITE FOR RESIDUE FAD A 700
source : AC1

22) chain A
residue 225
type
sequence T
description BINDING SITE FOR RESIDUE FAD A 700
source : AC1

23) chain A
residue 226
type
sequence S
description BINDING SITE FOR RESIDUE FAD A 700
source : AC1

24) chain A
residue 233
type
sequence D
description BINDING SITE FOR RESIDUE FAD A 700
source : AC1

25) chain A
residue 398
type
sequence E
description BINDING SITE FOR RESIDUE FAD A 700
source : AC1

26) chain A
residue 409
type
sequence R
description BINDING SITE FOR RESIDUE FAD A 700
source : AC1

27) chain A
residue 412
type
sequence A
description BINDING SITE FOR RESIDUE FAD A 700
source : AC1

28) chain A
residue 414
type
sequence S
description BINDING SITE FOR RESIDUE FAD A 700
source : AC1

29) chain A
residue 415
type
sequence L
description BINDING SITE FOR RESIDUE FAD A 700
source : AC1

30) chain A
residue 418
type
sequence L
description BINDING SITE FOR RESIDUE FAD A 700
source : AC1

31) chain B
residue 64
type
sequence S
description BINDING SITE FOR RESIDUE FES B 302
source : AC2

32) chain B
residue 65
type
sequence C
description BINDING SITE FOR RESIDUE FES B 302
source : AC2

33) chain B
residue 66
type
sequence R
description BINDING SITE FOR RESIDUE FES B 302
source : AC2

34) chain B
residue 68
type
sequence G
description BINDING SITE FOR RESIDUE FES B 302
source : AC2

35) chain B
residue 70
type
sequence C
description BINDING SITE FOR RESIDUE FES B 302
source : AC2

36) chain B
residue 71
type
sequence G
description BINDING SITE FOR RESIDUE FES B 302
source : AC2

37) chain B
residue 73
type
sequence C
description BINDING SITE FOR RESIDUE FES B 302
source : AC2

38) chain B
residue 85
type
sequence C
description BINDING SITE FOR RESIDUE FES B 302
source : AC2

39) chain B
residue 158
type
sequence C
description BINDING SITE FOR RESIDUE SF4 B 303
source : AC3

40) chain B
residue 159
type
sequence I
description BINDING SITE FOR RESIDUE SF4 B 303
source : AC3

41) chain B
residue 161
type
sequence C
description BINDING SITE FOR RESIDUE SF4 B 303
source : AC3

42) chain B
residue 162
type
sequence A
description BINDING SITE FOR RESIDUE SF4 B 303
source : AC3

43) chain B
residue 164
type
sequence C
description BINDING SITE FOR RESIDUE SF4 B 303
source : AC3

44) chain B
residue 182
type
sequence A
description BINDING SITE FOR RESIDUE SF4 B 303
source : AC3

45) chain B
residue 225
type
sequence C
description BINDING SITE FOR RESIDUE SF4 B 303
source : AC3

46) chain B
residue 226
type
sequence P
description BINDING SITE FOR RESIDUE SF4 B 303
source : AC3

47) chain B
residue 168
type
sequence C
description BINDING SITE FOR RESIDUE F3S B 304
source : AC4

48) chain B
residue 178
type
sequence Y
description BINDING SITE FOR RESIDUE F3S B 304
source : AC4

49) chain B
residue 181
type
sequence P
description BINDING SITE FOR RESIDUE F3S B 304
source : AC4

50) chain B
residue 215
type
sequence C
description BINDING SITE FOR RESIDUE F3S B 304
source : AC4

51) chain B
residue 216
type
sequence H
description BINDING SITE FOR RESIDUE F3S B 304
source : AC4

52) chain B
residue 217
type
sequence T
description BINDING SITE FOR RESIDUE F3S B 304
source : AC4

53) chain B
residue 218
type
sequence I
description BINDING SITE FOR RESIDUE F3S B 304
source : AC4

54) chain B
residue 219
type
sequence M
description BINDING SITE FOR RESIDUE F3S B 304
source : AC4

55) chain B
residue 220
type
sequence N
description BINDING SITE FOR RESIDUE F3S B 304
source : AC4

56) chain B
residue 221
type
sequence C
description BINDING SITE FOR RESIDUE F3S B 304
source : AC4

57) chain B
residue 216
type
sequence H
description BINDING SITE FOR RESIDUE HEM C 1305
source : AC5

58) chain C
residue 45
type
sequence H
description BINDING SITE FOR RESIDUE HEM C 1305
source : AC5

59) chain C
residue 46
type
sequence R
description BINDING SITE FOR RESIDUE HEM C 1305
source : AC5

60) chain C
residue 49
type
sequence G
description BINDING SITE FOR RESIDUE HEM C 1305
source : AC5

61) chain C
residue 52
type
sequence L
description BINDING SITE FOR RESIDUE HEM C 1305
source : AC5

62) chain C
residue 53
type
sequence S
description BINDING SITE FOR RESIDUE HEM C 1305
source : AC5

63) chain C
residue 101
type
sequence H
description BINDING SITE FOR RESIDUE HEM C 1305
source : AC5

64) chain C
residue 108
type
sequence H
description BINDING SITE FOR RESIDUE HEM C 1305
source : AC5

65) chain D
residue 53
type
sequence L
description BINDING SITE FOR RESIDUE HEM C 1305
source : AC5

66) chain D
residue 57
type
sequence L
description BINDING SITE FOR RESIDUE HEM C 1305
source : AC5

67) chain D
residue 79
type
sequence H
description BINDING SITE FOR RESIDUE HEM C 1305
source : AC5

68) chain D
residue 83
type
sequence G
description BINDING SITE FOR RESIDUE HEM C 1305
source : AC5

69) chain C
residue 140
type
sequence L
description BINDING SITE FOR RESIDUE EPH D 1306
source : AC6

70) chain D
residue 60
type
sequence A
description BINDING SITE FOR RESIDUE EPH D 1306
source : AC6

71) chain D
residue 61
type
sequence Y
description BINDING SITE FOR RESIDUE EPH D 1306
source : AC6

72) chain D
residue 62
type
sequence L
description BINDING SITE FOR RESIDUE EPH D 1306
source : AC6

73) chain D
residue 64
type
sequence P
description BINDING SITE FOR RESIDUE EPH D 1306
source : AC6

74) chain D
residue 127
type
sequence C
description BINDING SITE FOR RESIDUE EPH D 1306
source : AC6

75) chain D
residue 131
type
sequence A
description BINDING SITE FOR RESIDUE EPH D 1306
source : AC6

76) chain D
residue 134
type
sequence W
description BINDING SITE FOR RESIDUE EPH D 1306
source : AC6

77) chain B
residue 170
type
sequence S
description BINDING SITE FOR RESIDUE EBM C 1201
source : AC7

78) chain B
residue 173
type
sequence W
description BINDING SITE FOR RESIDUE EBM C 1201
source : AC7

79) chain B
residue 216
type
sequence H
description BINDING SITE FOR RESIDUE EBM C 1201
source : AC7

80) chain B
residue 218
type
sequence I
description BINDING SITE FOR RESIDUE EBM C 1201
source : AC7

81) chain C
residue 42
type
sequence S
description BINDING SITE FOR RESIDUE EBM C 1201
source : AC7

82) chain C
residue 46
type
sequence R
description BINDING SITE FOR RESIDUE EBM C 1201
source : AC7

83) chain D
residue 90
type
sequence D
description BINDING SITE FOR RESIDUE EBM C 1201
source : AC7

84) chain D
residue 91
type
sequence Y
description BINDING SITE FOR RESIDUE EBM C 1201
source : AC7

85) chain B
residue 65-73
type prosite
sequence CREGICGSC
description 2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CREGICGSC
source prosite : PS00197

86) chain B
residue 158-169
type prosite
sequence CILCACCSTSCP
description 4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiLCAcCStSCP
source prosite : PS00198

87) chain A
residue 55-64
type prosite
sequence RSHTVAAQGG
description FRD_SDH_FAD_BINDING Fumarate reductase / succinate dehydrogenase FAD-binding site. RSHTvaAqGG
source prosite : PS00504

88) chain C
residue 24-48
type prosite
sequence RPLSPHITIYRWSLPMAMSICHRGT
description SDH_CYT_1 Succinate dehydrogenase cytochrome b subunit signature 1. RPLsphItiyrwsLpmamSicHRgT
source prosite : PS01000

89) chain C
residue 101-114
type prosite
sequence HTWNGIRHLIWDLG
description SDH_CYT_2 Succinate dehydrogenase cytochrome b subunit signature 2. HtwnGIRHLiWDlG
source prosite : PS01001

90) chain D
residue 41-62
type TRANSMEM
sequence LHWTGERVVSVLLLGLLPAAYL
description Helical => ECO:0000305|PubMed:15989954
source Swiss-Prot : SWS_FT_FI1

91) chain B
residue 221
type TRANSMEM
sequence C
description Helical => ECO:0000305|PubMed:15989954
source Swiss-Prot : SWS_FT_FI1

92) chain B
residue 225
type TRANSMEM
sequence C
description Helical => ECO:0000305|PubMed:15989954
source Swiss-Prot : SWS_FT_FI1

93) chain D
residue 68-88
type TRANSMEM
sequence MDYSLAAALTLHGHWGIGQVV
description Helical => ECO:0000305|PubMed:15989954
source Swiss-Prot : SWS_FT_FI1

94) chain D
residue 98-119
type TRANSMEM
sequence QKAAKAGLLALSAFTFAGLCYF
description Helical => ECO:0000305|PubMed:15989954
source Swiss-Prot : SWS_FT_FI1

95) chain B
residue 85
type TRANSMEM
sequence C
description Helical => ECO:0000305|PubMed:15989954
source Swiss-Prot : SWS_FT_FI1

96) chain B
residue 158
type TRANSMEM
sequence C
description Helical => ECO:0000305|PubMed:15989954
source Swiss-Prot : SWS_FT_FI1

97) chain B
residue 161
type TRANSMEM
sequence C
description Helical => ECO:0000305|PubMed:15989954
source Swiss-Prot : SWS_FT_FI1

98) chain B
residue 164
type TRANSMEM
sequence C
description Helical => ECO:0000305|PubMed:15989954
source Swiss-Prot : SWS_FT_FI1

99) chain B
residue 168
type TRANSMEM
sequence C
description Helical => ECO:0000305|PubMed:15989954
source Swiss-Prot : SWS_FT_FI1

100) chain B
residue 215
type TRANSMEM
sequence C
description Helical => ECO:0000305|PubMed:15989954
source Swiss-Prot : SWS_FT_FI1

101) chain D
residue 63-67
type TOPO_DOM
sequence NPCSA
description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954
source Swiss-Prot : SWS_FT_FI2

102) chain A
residue 254
type TOPO_DOM
sequence H
description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954
source Swiss-Prot : SWS_FT_FI2

103) chain A
residue 266
type TOPO_DOM
sequence T
description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954
source Swiss-Prot : SWS_FT_FI2

104) chain A
residue 365
type TOPO_DOM
sequence H
description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954
source Swiss-Prot : SWS_FT_FI2

105) chain A
residue 398
type TOPO_DOM
sequence E
description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954
source Swiss-Prot : SWS_FT_FI2

106) chain A
residue 409
type TOPO_DOM
sequence R
description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954
source Swiss-Prot : SWS_FT_FI2

107) chain A
residue 412
type TOPO_DOM
sequence A
description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954
source Swiss-Prot : SWS_FT_FI2

108) chain A
residue 414
type TOPO_DOM
sequence S
description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954
source Swiss-Prot : SWS_FT_FI2

109) chain A
residue 415
type TOPO_DOM
sequence L
description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954
source Swiss-Prot : SWS_FT_FI2

110) chain D
residue 120-136
type TOPO_DOM
sequence NYHDVGICKAVAMLWKL
description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954
source Swiss-Prot : SWS_FT_FI2

111) chain C
residue 119-140
type TOPO_DOM
sequence IPQLTQSGVVVLILTVLSSVGL
description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954
source Swiss-Prot : SWS_FT_FI2

112) chain A
residue 50
type TOPO_DOM
sequence K
description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954
source Swiss-Prot : SWS_FT_FI2

113) chain A
residue 56
type TOPO_DOM
sequence S
description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954
source Swiss-Prot : SWS_FT_FI2

114) chain A
residue 58
type TOPO_DOM
sequence T
description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954
source Swiss-Prot : SWS_FT_FI2

115) chain A
residue 63
type TOPO_DOM
sequence G
description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954
source Swiss-Prot : SWS_FT_FI2

116) chain A
residue 179
type TOPO_DOM
sequence A
description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954
source Swiss-Prot : SWS_FT_FI2

117) chain A
residue 233
type TOPO_DOM
sequence D
description Mitochondrial intermembrane => ECO:0000305|PubMed:15989954
source Swiss-Prot : SWS_FT_FI2

118) chain D
residue 89-97
type TOPO_DOM
sequence TDYVRGDAL
description Mitochondrial matrix => ECO:0000305|PubMed:15989954
source Swiss-Prot : SWS_FT_FI3

119) chain C
residue 141-143
type TOPO_DOM
sequence AAM
description Mitochondrial matrix => ECO:0000305|PubMed:15989954
source Swiss-Prot : SWS_FT_FI3

120) chain D
residue 79
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:15989954, ECO:0007744|PDB:1ZOY, ECO:0007744|PDB:1ZP0
source Swiss-Prot : SWS_FT_FI4

121) chain A
residue 605
type BINDING
sequence K
description axial binding residue => ECO:0000269|PubMed:15989954, ECO:0007744|PDB:1ZOY, ECO:0007744|PDB:1ZP0
source Swiss-Prot : SWS_FT_FI4

122) chain A
residue 140
type BINDING
sequence K
description axial binding residue => ECO:0000269|PubMed:15989954, ECO:0007744|PDB:1ZOY, ECO:0007744|PDB:1ZP0
source Swiss-Prot : SWS_FT_FI4

123) chain A
residue 438
type BINDING
sequence K
description axial binding residue => ECO:0000269|PubMed:15989954, ECO:0007744|PDB:1ZOY, ECO:0007744|PDB:1ZP0
source Swiss-Prot : SWS_FT_FI4

124) chain A
residue 475
type BINDING
sequence K
description axial binding residue => ECO:0000269|PubMed:15989954, ECO:0007744|PDB:1ZOY, ECO:0007744|PDB:1ZP0
source Swiss-Prot : SWS_FT_FI4

125) chain A
residue 508
type BINDING
sequence K
description axial binding residue => ECO:0000269|PubMed:15989954, ECO:0007744|PDB:1ZOY, ECO:0007744|PDB:1ZP0
source Swiss-Prot : SWS_FT_FI4

126) chain A
residue 556
type BINDING
sequence K
description axial binding residue => ECO:0000269|PubMed:15989954, ECO:0007744|PDB:1ZOY, ECO:0007744|PDB:1ZP0
source Swiss-Prot : SWS_FT_FI4

127) chain A
residue 582
type BINDING
sequence K
description axial binding residue => ECO:0000269|PubMed:15989954, ECO:0007744|PDB:1ZOY, ECO:0007744|PDB:1ZP0
source Swiss-Prot : SWS_FT_FI4

128) chain A
residue 591
type BINDING
sequence K
description axial binding residue => ECO:0000269|PubMed:15989954, ECO:0007744|PDB:1ZOY, ECO:0007744|PDB:1ZP0
source Swiss-Prot : SWS_FT_FI4

129) chain A
residue 594
type BINDING
sequence K
description axial binding residue => ECO:0000269|PubMed:15989954, ECO:0007744|PDB:1ZOY, ECO:0007744|PDB:1ZP0
source Swiss-Prot : SWS_FT_FI4

130) chain D
residue 91
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:15989954
source Swiss-Prot : SWS_FT_FI5

131) chain A
residue 293
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:15989954
source Swiss-Prot : SWS_FT_FI5

132) chain A
residue 443
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:15989954
source Swiss-Prot : SWS_FT_FI5

133) chain A
residue 456
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:15989954
source Swiss-Prot : SWS_FT_FI5

134) chain A
residue 496
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:15989954
source Swiss-Prot : SWS_FT_FI5

135) chain A
residue 173
type MOD_RES
sequence Y
description Phosphotyrosine; by SRC => ECO:0000250|UniProtKB:P31040
source Swiss-Prot : SWS_FT_FI6

136) chain A
residue 566
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P31040
source Swiss-Prot : SWS_FT_FI7

137) chain A
residue 573
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q8K2B3
source Swiss-Prot : SWS_FT_FI8


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