eF-site ID 1kb9-ABCDEFGHIJK
PDB Code 1kb9
Chain A, B, C, D, E, F, G, H, I, J, K

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Title YEAST CYTOCHROME BC1 COMPLEX
Classification OXIDOREDUCTASE/ELECTRON TRANSPORT
Compound UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN I
Source Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (1KB9)
Sequence A:  AEVTQLSNGIVVATEHNPSAHTASVGVVFGSGAANENPYN
NGVSNLWKNIFLSKENSAVAAKEGLALSSNISRDFQSYIV
SSLPGSTDKSLDFLNQSFIQQKANLLSSSNFEATKKSVLK
QVQDFEDNDHPNRVLEHLHSTAFQNTPLSLPTRGTLESLE
NLVVADLESFANNHFLNSNAVVVGTGNIKHEDLVNSIESK
NLSLQTGTKPVLKKKAAFLGSEVRLRDDTLPKAWISLAVE
GEPVNSPNYFVAKLAAQIFGSYNAFEPASRLQGIKLLDNI
QEYQLCDNFNHFSLSYKDSGLWGFSTATRNVTMIDDLIHF
TLKQWNRLTISVTDTEVERAKSLLKLQLGQLYESGNPVND
ANLLGAEVLIKGSKLSLGEAFKKIDAITVKDVKAWAGKRL
WDQDIAIAGTGQIEGLLDYMRIRSDMSMMRW
B:  LTVSARDAPTKISTLAVKVHGGSRYATKDGVAHLLNRFNF
QNTNTRSALKLVRESELLGGTFKSTLDREYITLKATFLKD
DLPYYVNALADVLYKTAFKPHELTESVLPAARYDYAVAEQ
CPVKSAEDQLYAITFRKGLGNPLLYDGVERVSLQDIKDFA
DKVYTKENLEVSGENVVEADLKRFVDESLLSTLPAGKSLV
SKSEPKFFLGEENRVRFIGDSVAAIGIPVNKASLAQYEVL
ANYLTSALSELSGLISSAKLDKFTDGGLFTLFVRDQDSAV
VSSNIKKIVADLKKGKDLSPAINYTKLKNAVQNESVSSPI
ELNFDAVKDFKLGKFNYVAVGDVSNLPYLDEL
C:  MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCL
VIQIVTGIFMAMHYSSNIELAFSSVEHIMRDVHNGYILRY
LHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVII
FTLTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGND
IVSWLWGGFSVSNPTIQRFFALHYLVPFIIAAMVIMHLMA
LHIHGSSNPLGITGNLDRIPMHSYFIFKDLVTVFLFMLIL
ALFVFYSPNTLGHPDNYIPGNPLVTPASIVPEWYLLPFYA
ILRSIPDKLLGVITMFAAILVLLVLPFTDRSVVRGNTFKV
LSKFFFFIFVFNFVLLGQIGACHVEVPYVLMGQIATFIYF
AYFLIIVPVISTIENVLFYIGRVNK
D:  MTAAEHGLHAPAYAWSHNGPFETFDHASIRRGYQVYREVC
AACHSLDRVAWRTLVGVSHTNEEVRNMAEEFEYDDEPDEQ
GNPKKRPGKLSDYIPGPYPNEQAARAANQGALPPDLSLIV
KARHGGCDYIFSLLTGYPDEPPAGVALPPGSNYNPYFPGG
SIAMARVLFDDMVEYEDGTPATTSQMAKDVTTFLNWCAEP
EHDERKRLGLKTVIILSSLYLLSIWVKKFKWAGIKTRKFV
FNPPKP
E:  KSTYRTPNFDDVLKENNDADKGRSYAYFMVGAMGLLSSAG
AKSTVETFISSMTATADVLAMAKVEVNLAAIPLGKNVVVK
WQGKPVFIRHRTPHEIQEANSVDMSALKDPQTDADRVKDP
QWLIMLGICTHLGCVPIGEAGDFGGWFCPCHGSHYDISGR
IRKGPAPLNLEIPAYEFDGDKVIVG
F:  VTDQLEDLREHFKNTEEGKALVHHYEECAERVKIQQQQPG
YADLEHKEDCVEEFFHLQHYLDTATAPRLFDKLK
G:  QSFTSIARIGDYILKSPVLSKLCVPVANQFINLAGYKKLG
LKFDDLIAEENPIMQTALRRLPEDESYARAYRIIRAHQTE
LTHHLLPRNEWIKAQEDVPYLLPYILEAEAAAKEKDELDN
IEVSK
H:  GPPSGKTYMGWWGHMGGPKQKGITSYAVSPYAQKPLQGIF
HNAVFNSFRRFKSQFLYVLIPAGIYWYWWKNGNEYNEFLY
SKAGREELERVNV
I:  SSLYKTFFKRNAVFVGTIFAGAFVFQTVFDTAITSWYENH
NKGKLWKDVKARIAA
J:  EVKLQESGAGLVQPSQSLSLTCSVTGYSITSGYYWNWIRL
FPGNKLEWVGYISNVGDNNYNPSLKDRLSITRDTSKNQFF
LKLNSVTTEDTATYYCARSEYYSVTGYAMDYWGQGTTVTV
SSAWRHP
K:  DIELTQTPVSLAASLGDRVTISCRASQDINNFLNWYQQKP
DGTIKLLIYYTSRLHAGVPSRFSGSGSGTDYSLTISNLEP
EDIATYFCQHHIKFPWTFGAGTKLEIK
Description (1)  UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN I, UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN 2, CYTOCHROME B, CYTOCHROME C1, HEME PROTEIN, UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT, UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 17 KD PROTEIN, UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 14 KD PROTEIN, UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX UBIQUINONE-BINDING PROTEIN QP-C, UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 7.3 KD PROTEIN, HEAVY CHAIN (VH) OF FV-FRAGMENT, LIGHT CHAIN (VL) OF FV-FRAGMENT, PROTOPORPHYRIN IX CONTAINING FE, FE2/S2 (INORGANIC) CLUSTER, ESTRIOL 3-(B-D-GLUCURONIDE), 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL, 2-[(HYDROXY{[(2R,3R,5S,6R)-2,3,4,5,6-PENTAHYDROXYCYCLOHEXYL]OXY}PHOSPHORYL)OXY]-1-[(PALMITOYLOXY)METHYL]ETHYL HEPTADECANOATE, 5-AMINO-6-CYCLOHEXYL-4-HYDROXY-2-ISOBUTYL-HEXANOIC ACID, 9-(4-HYDROXY-3-(HYDROXYMETHYL)BUT-1-YL)GUANINE, 5-OXOPROLINE, 2'-DEOXYURIDINE 5'-MONOPHOSPHATE


Functional site

1) chain C
residue 40
type
sequence L
description BINDING SITE FOR RESIDUE HEM C 501
source : AC1

2) chain C
residue 43
type
sequence Q
description BINDING SITE FOR RESIDUE HEM C 501
source : AC1

3) chain C
residue 47
type
sequence G
description BINDING SITE FOR RESIDUE HEM C 501
source : AC1

4) chain C
residue 48
type
sequence I
description BINDING SITE FOR RESIDUE HEM C 501
source : AC1

5) chain C
residue 50
type
sequence M
description BINDING SITE FOR RESIDUE HEM C 501
source : AC1

6) chain C
residue 51
type
sequence A
description BINDING SITE FOR RESIDUE HEM C 501
source : AC1

7) chain C
residue 79
type
sequence R
description BINDING SITE FOR RESIDUE HEM C 501
source : AC1

8) chain C
residue 82
type
sequence H
description BINDING SITE FOR RESIDUE HEM C 501
source : AC1

9) chain C
residue 89
type
sequence F
description BINDING SITE FOR RESIDUE HEM C 501
source : AC1

10) chain C
residue 127
type
sequence T
description BINDING SITE FOR RESIDUE HEM C 501
source : AC1

11) chain C
residue 128
type
sequence A
description BINDING SITE FOR RESIDUE HEM C 501
source : AC1

12) chain C
residue 131
type
sequence G
description BINDING SITE FOR RESIDUE HEM C 501
source : AC1

13) chain C
residue 135
type
sequence V
description BINDING SITE FOR RESIDUE HEM C 501
source : AC1

14) chain C
residue 183
type
sequence H
description BINDING SITE FOR RESIDUE HEM C 501
source : AC1

15) chain C
residue 184
type
sequence Y
description BINDING SITE FOR RESIDUE HEM C 501
source : AC1

16) chain C
residue 187
type
sequence P
description BINDING SITE FOR RESIDUE HEM C 501
source : AC1

17) chain C
residue 30
type
sequence W
description BINDING SITE FOR RESIDUE HEM C 502
source : AC2

18) chain C
residue 33
type
sequence G
description BINDING SITE FOR RESIDUE HEM C 502
source : AC2

19) chain C
residue 36
type
sequence L
description BINDING SITE FOR RESIDUE HEM C 502
source : AC2

20) chain C
residue 96
type
sequence H
description BINDING SITE FOR RESIDUE HEM C 502
source : AC2

21) chain C
residue 99
type
sequence K
description BINDING SITE FOR RESIDUE HEM C 502
source : AC2

22) chain C
residue 105
type
sequence S
description BINDING SITE FOR RESIDUE HEM C 502
source : AC2

23) chain C
residue 113
type
sequence L
description BINDING SITE FOR RESIDUE HEM C 502
source : AC2

24) chain C
residue 117
type
sequence G
description BINDING SITE FOR RESIDUE HEM C 502
source : AC2

25) chain C
residue 118
type
sequence V
description BINDING SITE FOR RESIDUE HEM C 502
source : AC2

26) chain C
residue 120
type
sequence I
description BINDING SITE FOR RESIDUE HEM C 502
source : AC2

27) chain C
residue 197
type
sequence H
description BINDING SITE FOR RESIDUE HEM C 502
source : AC2

28) chain C
residue 201
type
sequence L
description BINDING SITE FOR RESIDUE HEM C 502
source : AC2

29) chain C
residue 206
type
sequence S
description BINDING SITE FOR RESIDUE HEM C 502
source : AC2

30) chain C
residue 207
type
sequence S
description BINDING SITE FOR RESIDUE HEM C 502
source : AC2

31) chain D
residue 100
type
sequence V
description BINDING SITE FOR RESIDUE HEM D 503
source : AC3

32) chain D
residue 101
type
sequence C
description BINDING SITE FOR RESIDUE HEM D 503
source : AC3

33) chain D
residue 104
type
sequence C
description BINDING SITE FOR RESIDUE HEM D 503
source : AC3

34) chain D
residue 105
type
sequence H
description BINDING SITE FOR RESIDUE HEM D 503
source : AC3

35) chain D
residue 169
type
sequence N
description BINDING SITE FOR RESIDUE HEM D 503
source : AC3

36) chain D
residue 175
type
sequence P
description BINDING SITE FOR RESIDUE HEM D 503
source : AC3

37) chain D
residue 184
type
sequence R
description BINDING SITE FOR RESIDUE HEM D 503
source : AC3

38) chain D
residue 190
type
sequence Y
description BINDING SITE FOR RESIDUE HEM D 503
source : AC3

39) chain D
residue 191
type
sequence I
description BINDING SITE FOR RESIDUE HEM D 503
source : AC3

40) chain D
residue 218
type
sequence F
description BINDING SITE FOR RESIDUE HEM D 503
source : AC3

41) chain D
residue 223
type
sequence I
description BINDING SITE FOR RESIDUE HEM D 503
source : AC3

42) chain D
residue 224
type
sequence A
description BINDING SITE FOR RESIDUE HEM D 503
source : AC3

43) chain D
residue 225
type
sequence M
description BINDING SITE FOR RESIDUE HEM D 503
source : AC3

44) chain D
residue 228
type
sequence V
description BINDING SITE FOR RESIDUE HEM D 503
source : AC3

45) chain E
residue 159
type
sequence C
description BINDING SITE FOR RESIDUE FES E 504
source : AC4

46) chain E
residue 161
type
sequence H
description BINDING SITE FOR RESIDUE FES E 504
source : AC4

47) chain E
residue 162
type
sequence L
description BINDING SITE FOR RESIDUE FES E 504
source : AC4

48) chain E
residue 178
type
sequence C
description BINDING SITE FOR RESIDUE FES E 504
source : AC4

49) chain E
residue 181
type
sequence H
description BINDING SITE FOR RESIDUE FES E 504
source : AC4

50) chain E
residue 183
type
sequence S
description BINDING SITE FOR RESIDUE FES E 504
source : AC4

51) chain C
residue 125
type
sequence I
description BINDING SITE FOR RESIDUE SMA C 505
source : AC5

52) chain C
residue 129
type
sequence F
description BINDING SITE FOR RESIDUE SMA C 505
source : AC5

53) chain C
residue 143
type
sequence G
description BINDING SITE FOR RESIDUE SMA C 505
source : AC5

54) chain C
residue 146
type
sequence V
description BINDING SITE FOR RESIDUE SMA C 505
source : AC5

55) chain C
residue 271
type
sequence P
description BINDING SITE FOR RESIDUE SMA C 505
source : AC5

56) chain C
residue 272
type
sequence E
description BINDING SITE FOR RESIDUE SMA C 505
source : AC5

57) chain C
residue 275
type
sequence L
description BINDING SITE FOR RESIDUE SMA C 505
source : AC5

58) chain C
residue 279
type
sequence Y
description BINDING SITE FOR RESIDUE SMA C 505
source : AC5

59) chain C
residue 295
type
sequence M
description BINDING SITE FOR RESIDUE SMA C 505
source : AC5

60) chain C
residue 296
type
sequence F
description BINDING SITE FOR RESIDUE SMA C 505
source : AC5

61) chain E
residue 181
type
sequence H
description BINDING SITE FOR RESIDUE SMA C 505
source : AC5

62) chain C
residue 16
type
sequence Y
description BINDING SITE FOR RESIDUE UQ6 C 506
source : AC6

63) chain C
residue 22
type
sequence Q
description BINDING SITE FOR RESIDUE UQ6 C 506
source : AC6

64) chain C
residue 40
type
sequence L
description BINDING SITE FOR RESIDUE UQ6 C 506
source : AC6

65) chain C
residue 44
type
sequence I
description BINDING SITE FOR RESIDUE UQ6 C 506
source : AC6

66) chain C
residue 201
type
sequence L
description BINDING SITE FOR RESIDUE UQ6 C 506
source : AC6

67) chain C
residue 206
type
sequence S
description BINDING SITE FOR RESIDUE UQ6 C 506
source : AC6

68) chain C
residue 221
type
sequence M
description BINDING SITE FOR RESIDUE UQ6 C 506
source : AC6

69) chain C
residue 229
type
sequence D
description BINDING SITE FOR RESIDUE UQ6 C 506
source : AC6

70) chain C
residue 74
type
sequence N
description BINDING SITE FOR RESIDUE PIE C 508
source : AC7

71) chain C
residue 237
type
sequence M
description BINDING SITE FOR RESIDUE PIE C 508
source : AC7

72) chain C
residue 245
type
sequence F
description BINDING SITE FOR RESIDUE PIE C 508
source : AC7

73) chain D
residue 269
type
sequence L
description BINDING SITE FOR RESIDUE PIE C 508
source : AC7

74) chain D
residue 272
type
sequence K
description BINDING SITE FOR RESIDUE PIE C 508
source : AC7

75) chain D
residue 273
type
sequence T
description BINDING SITE FOR RESIDUE PIE C 508
source : AC7

76) chain D
residue 276
type
sequence I
description BINDING SITE FOR RESIDUE PIE C 508
source : AC7

77) chain E
residue 70
type
sequence G
description BINDING SITE FOR RESIDUE PIE C 508
source : AC7

78) chain E
residue 73
type
sequence S
description BINDING SITE FOR RESIDUE PIE C 508
source : AC7

79) chain E
residue 76
type
sequence E
description BINDING SITE FOR RESIDUE PIE C 508
source : AC7

80) chain E
residue 80
type
sequence S
description BINDING SITE FOR RESIDUE PIE C 508
source : AC7

81) chain C
residue 98
type
sequence A
description BINDING SITE FOR RESIDUE PEF C 510
source : AC8

82) chain C
residue 102
type
sequence Y
description BINDING SITE FOR RESIDUE PEF C 510
source : AC8

83) chain C
residue 103
type
sequence Y
description BINDING SITE FOR RESIDUE PEF C 510
source : AC8

84) chain C
residue 326
type
sequence F
description BINDING SITE FOR RESIDUE PEF C 510
source : AC8

85) chain C
residue 327
type
sequence F
description BINDING SITE FOR RESIDUE PEF C 510
source : AC8

86) chain C
residue 329
type
sequence F
description BINDING SITE FOR RESIDUE PEF C 510
source : AC8

87) chain C
residue 333
type
sequence F
description BINDING SITE FOR RESIDUE PEF C 510
source : AC8

88) chain G
residue 82
type
sequence E
description BINDING SITE FOR RESIDUE PEF C 510
source : AC8

89) chain H
residue 51
type
sequence R
description BINDING SITE FOR RESIDUE PEF C 510
source : AC8

90) chain C
residue 27
type
sequence N
description BINDING SITE FOR RESIDUE CDL C 511
source : AC9

91) chain C
residue 28
type
sequence Y
description BINDING SITE FOR RESIDUE CDL C 511
source : AC9

92) chain C
residue 29
type
sequence W
description BINDING SITE FOR RESIDUE CDL C 511
source : AC9

93) chain C
residue 32
type
sequence M
description BINDING SITE FOR RESIDUE CDL C 511
source : AC9

94) chain C
residue 95
type
sequence M
description BINDING SITE FOR RESIDUE CDL C 511
source : AC9

95) chain C
residue 231
type
sequence V
description BINDING SITE FOR RESIDUE CDL C 511
source : AC9

96) chain C
residue 235
type
sequence L
description BINDING SITE FOR RESIDUE CDL C 511
source : AC9

97) chain D
residue 281
type
sequence Y
description BINDING SITE FOR RESIDUE CDL C 511
source : AC9

98) chain D
residue 288
type
sequence K
description BINDING SITE FOR RESIDUE CDL C 511
source : AC9

99) chain D
residue 289
type
sequence K
description BINDING SITE FOR RESIDUE CDL C 511
source : AC9

100) chain G
residue 85
type
sequence H
description BINDING SITE FOR RESIDUE CDL C 511
source : AC9

101) chain C
residue 3
type
sequence F
description BINDING SITE FOR RESIDUE PEF C 513
source : BC1

102) chain C
residue 7
type
sequence N
description BINDING SITE FOR RESIDUE PEF C 513
source : BC1

103) chain C
residue 13
type
sequence V
description BINDING SITE FOR RESIDUE PEF C 513
source : BC1

104) chain C
residue 112
type
sequence T
description BINDING SITE FOR RESIDUE PEF C 513
source : BC1

105) chain C
residue 115
type
sequence N
description BINDING SITE FOR RESIDUE PEF C 513
source : BC1

106) chain A
residue 450
type
sequence S
description BINDING SITE FOR RESIDUE PCF A 514
source : BC2

107) chain C
residue 222
type
sequence H
description BINDING SITE FOR RESIDUE PCF A 514
source : BC2

108) chain E
residue 60
type
sequence V
description BINDING SITE FOR RESIDUE PCF A 514
source : BC2

109) chain E
residue 67
type
sequence S
description BINDING SITE FOR RESIDUE PCF A 514
source : BC2

110) chain A
residue 427
type
sequence W
description BINDING SITE FOR RESIDUE UMQ A 521
source : BC3

111) chain A
residue 428
type
sequence D
description BINDING SITE FOR RESIDUE UMQ A 521
source : BC3

112) chain A
residue 453
type
sequence S
description BINDING SITE FOR RESIDUE UMQ A 521
source : BC3

113) chain A
residue 454
type
sequence M
description BINDING SITE FOR RESIDUE UMQ A 521
source : BC3

114) chain A
residue 455
type
sequence M
description BINDING SITE FOR RESIDUE UMQ A 521
source : BC3

115) chain A
residue 456
type
sequence R
description BINDING SITE FOR RESIDUE UMQ A 521
source : BC3

116) chain E
residue 57
type
sequence Y
description BINDING SITE FOR RESIDUE UMQ A 521
source : BC3

117) chain E
residue 60
type
sequence V
description BINDING SITE FOR RESIDUE UMQ A 521
source : BC3

118) chain E
residue 68
type
sequence S
description BINDING SITE FOR RESIDUE UMQ A 521
source : BC3

119) chain I
residue 14
type
sequence N
description BINDING SITE FOR RESIDUE UMQ A 521
source : BC3

120) chain I
residue 15
type
sequence A
description BINDING SITE FOR RESIDUE UMQ A 521
source : BC3

121) chain I
residue 16
type
sequence V
description BINDING SITE FOR RESIDUE UMQ A 521
source : BC3

122) chain I
residue 17
type
sequence F
description BINDING SITE FOR RESIDUE UMQ A 521
source : BC3

123) chain I
residue 18
type
sequence V
description BINDING SITE FOR RESIDUE UMQ A 521
source : BC3

124) chain E
residue 181
type catalytic
sequence H
description 208
source MCSA : MCSA1

125) chain C
residue 206
type catalytic
sequence S
description 208
source MCSA : MCSA1

126) chain C
residue 228
type catalytic
sequence K
description 208
source MCSA : MCSA1

127) chain C
residue 229
type catalytic
sequence D
description 208
source MCSA : MCSA1

128) chain C
residue 272
type catalytic
sequence E
description 208
source MCSA : MCSA1

129) chain E
residue 159
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV, ECO:0007744|PDB:1KB9, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:1P84, ECO:0007744|PDB:2IBZ, ECO:0007744|PDB:3CX5, ECO:0007744|PDB:3CXH, ECO:0007744|PDB:4PD4
source Swiss-Prot : SWS_FT_FI4

130) chain E
residue 161
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV, ECO:0007744|PDB:1KB9, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:1P84, ECO:0007744|PDB:2IBZ, ECO:0007744|PDB:3CX5, ECO:0007744|PDB:3CXH, ECO:0007744|PDB:4PD4
source Swiss-Prot : SWS_FT_FI4

131) chain E
residue 178
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV, ECO:0007744|PDB:1KB9, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:1P84, ECO:0007744|PDB:2IBZ, ECO:0007744|PDB:3CX5, ECO:0007744|PDB:3CXH, ECO:0007744|PDB:4PD4
source Swiss-Prot : SWS_FT_FI4

132) chain E
residue 181
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV, ECO:0007744|PDB:1KB9, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:1P84, ECO:0007744|PDB:2IBZ, ECO:0007744|PDB:3CX5, ECO:0007744|PDB:3CXH, ECO:0007744|PDB:4PD4
source Swiss-Prot : SWS_FT_FI4

133) chain D
residue 225
type BINDING
sequence M
description axial binding residue => ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV, ECO:0007744|PDB:1KYO
source Swiss-Prot : SWS_FT_FI5

134) chain C
residue 96
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV, ECO:0007744|PDB:1KYO
source Swiss-Prot : SWS_FT_FI5

135) chain C
residue 183
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV, ECO:0007744|PDB:1KYO
source Swiss-Prot : SWS_FT_FI5

136) chain C
residue 197
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV, ECO:0007744|PDB:1KYO
source Swiss-Prot : SWS_FT_FI5

137) chain C
residue 202
type BINDING
sequence H
description BINDING => ECO:0000250|UniProtKB:P00157
source Swiss-Prot : SWS_FT_FI6

138) chain H
residue 81-94
type TOPO_DOM
sequence YSKAGREELERVNV
description Mitochondrial intermembrane => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554
source Swiss-Prot : SWS_FT_FI3

139) chain D
residue 104
type TOPO_DOM
sequence C
description Mitochondrial intermembrane => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554
source Swiss-Prot : SWS_FT_FI3

140) chain C
residue 247-287
type TOPO_DOM
sequence SPNTLGHPDNYIPGNPLVTPASIVPEWYLLPFYAILRSIP
D
description Mitochondrial intermembrane => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554
source Swiss-Prot : SWS_FT_FI3

141) chain C
residue 341-347
type TOPO_DOM
sequence ACHVEVP
description Mitochondrial intermembrane => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554
source Swiss-Prot : SWS_FT_FI3

142) chain I
residue 18-43
type TRANSMEM
sequence VGTIFAGAFVFQTVFDTAITSWYENH
description Helical => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554
source Swiss-Prot : SWS_FT_FI1

143) chain C
residue 103-110
type TRANSMEM
sequence YGSYRSPR
description Helical => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554
source Swiss-Prot : SWS_FT_FI1

144) chain C
residue 205-223
type TRANSMEM
sequence GSSNPLGITGNLDRIPMHS
description Helical => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554
source Swiss-Prot : SWS_FT_FI1

145) chain C
residue 309-319
type TRANSMEM
sequence DRSVVRGNTFK
description Helical => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554
source Swiss-Prot : SWS_FT_FI1

146) chain C
residue 365-385
type TRANSMEM
sequence IIVPVISTIENVLFYIGRVNK
description Helical => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554
source Swiss-Prot : SWS_FT_FI1

147) chain H
residue 50-80
type TRANSMEM
sequence RRFKSQFLYVLIPAGIYWYWWKNGNEYNEFL
description Helical => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554
source Swiss-Prot : SWS_FT_FI2

148) chain C
residue 75-102
type TRANSMEM
sequence GYILRYLHANGASFFFMVMFMHMAKGLY
description Helical => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554
source Swiss-Prot : SWS_FT_FI2

149) chain C
residue 111-135
type TRANSMEM
sequence VTLWNVGVIIFTLTIATAFLGYCCV
description Helical => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554
source Swiss-Prot : SWS_FT_FI2

150) chain C
residue 173-204
type TRANSMEM
sequence NPTIQRFFALHYLVPFIIAAMVIMHLMALHIH
description Helical => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554
source Swiss-Prot : SWS_FT_FI2

151) chain C
residue 224-246
type TRANSMEM
sequence YFIFKDLVTVFLFMLILALFVFY
description Helical => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554
source Swiss-Prot : SWS_FT_FI2

152) chain C
residue 288-308
type TRANSMEM
sequence KLLGVITMFAAILVLLVLPFT
description Helical => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554
source Swiss-Prot : SWS_FT_FI2

153) chain C
residue 320-340
type TRANSMEM
sequence VLSKFFFFIFVFNFVLLGQIG
description Helical => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554
source Swiss-Prot : SWS_FT_FI2

154) chain C
residue 348-364
type TRANSMEM
sequence YVLMGQIATFIYFAYFL
description Helical => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554
source Swiss-Prot : SWS_FT_FI2

155) chain B
residue 37-59
type prosite
sequence GGSRYATKDGVAHLLNRFNFQNT
description INSULINASE Insulinase family, zinc-binding region signature. Ggsryatkd.GvAHLLNRFnFqNT
source prosite : PS00143


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