eF-site ID 1p84-ABCDEFGHIJK
PDB Code 1p84
Chain A, B, C, D, E, F, G, H, I, J, K

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Title HDBT inhibited Yeast Cytochrome bc1 Complex
Classification OXIDOREDUCTASE
Compound Ubiquinol-cytochrome C reductase complex core protein I
Source ORGANISM_COMMON: baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae;
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


Functional site

1) chain C
residue 40
type
sequence L
description BINDING SITE FOR RESIDUE HEC C 701
source : AC1

2) chain C
residue 43
type
sequence Q
description BINDING SITE FOR RESIDUE HEC C 701
source : AC1

3) chain C
residue 47
type
sequence G
description BINDING SITE FOR RESIDUE HEC C 701
source : AC1

4) chain C
residue 50
type
sequence M
description BINDING SITE FOR RESIDUE HEC C 701
source : AC1

5) chain C
residue 79
type
sequence R
description BINDING SITE FOR RESIDUE HEC C 701
source : AC1

6) chain C
residue 82
type
sequence H
description BINDING SITE FOR RESIDUE HEC C 701
source : AC1

7) chain C
residue 89
type
sequence F
description BINDING SITE FOR RESIDUE HEC C 701
source : AC1

8) chain C
residue 127
type
sequence T
description BINDING SITE FOR RESIDUE HEC C 701
source : AC1

9) chain C
residue 128
type
sequence A
description BINDING SITE FOR RESIDUE HEC C 701
source : AC1

10) chain C
residue 131
type
sequence G
description BINDING SITE FOR RESIDUE HEC C 701
source : AC1

11) chain C
residue 135
type
sequence V
description BINDING SITE FOR RESIDUE HEC C 701
source : AC1

12) chain C
residue 183
type
sequence H
description BINDING SITE FOR RESIDUE HEC C 701
source : AC1

13) chain C
residue 184
type
sequence Y
description BINDING SITE FOR RESIDUE HEC C 701
source : AC1

14) chain C
residue 187
type
sequence P
description BINDING SITE FOR RESIDUE HEC C 701
source : AC1

15) chain C
residue 30
type
sequence W
description BINDING SITE FOR RESIDUE HEC C 702
source : AC2

16) chain C
residue 33
type
sequence G
description BINDING SITE FOR RESIDUE HEC C 702
source : AC2

17) chain C
residue 36
type
sequence L
description BINDING SITE FOR RESIDUE HEC C 702
source : AC2

18) chain C
residue 96
type
sequence H
description BINDING SITE FOR RESIDUE HEC C 702
source : AC2

19) chain C
residue 97
type
sequence M
description BINDING SITE FOR RESIDUE HEC C 702
source : AC2

20) chain C
residue 99
type
sequence K
description BINDING SITE FOR RESIDUE HEC C 702
source : AC2

21) chain C
residue 105
type
sequence S
description BINDING SITE FOR RESIDUE HEC C 702
source : AC2

22) chain C
residue 113
type
sequence L
description BINDING SITE FOR RESIDUE HEC C 702
source : AC2

23) chain C
residue 117
type
sequence G
description BINDING SITE FOR RESIDUE HEC C 702
source : AC2

24) chain C
residue 120
type
sequence I
description BINDING SITE FOR RESIDUE HEC C 702
source : AC2

25) chain C
residue 194
type
sequence V
description BINDING SITE FOR RESIDUE HEC C 702
source : AC2

26) chain C
residue 197
type
sequence H
description BINDING SITE FOR RESIDUE HEC C 702
source : AC2

27) chain C
residue 201
type
sequence L
description BINDING SITE FOR RESIDUE HEC C 702
source : AC2

28) chain C
residue 206
type
sequence S
description BINDING SITE FOR RESIDUE HEC C 702
source : AC2

29) chain C
residue 207
type
sequence S
description BINDING SITE FOR RESIDUE HEC C 702
source : AC2

30) chain D
residue 100
type
sequence V
description BINDING SITE FOR RESIDUE HEC D 703
source : AC3

31) chain D
residue 101
type
sequence C
description BINDING SITE FOR RESIDUE HEC D 703
source : AC3

32) chain D
residue 104
type
sequence C
description BINDING SITE FOR RESIDUE HEC D 703
source : AC3

33) chain D
residue 105
type
sequence H
description BINDING SITE FOR RESIDUE HEC D 703
source : AC3

34) chain D
residue 184
type
sequence R
description BINDING SITE FOR RESIDUE HEC D 703
source : AC3

35) chain D
residue 190
type
sequence Y
description BINDING SITE FOR RESIDUE HEC D 703
source : AC3

36) chain D
residue 191
type
sequence I
description BINDING SITE FOR RESIDUE HEC D 703
source : AC3

37) chain D
residue 218
type
sequence F
description BINDING SITE FOR RESIDUE HEC D 703
source : AC3

38) chain D
residue 223
type
sequence I
description BINDING SITE FOR RESIDUE HEC D 703
source : AC3

39) chain D
residue 224
type
sequence A
description BINDING SITE FOR RESIDUE HEC D 703
source : AC3

40) chain D
residue 225
type
sequence M
description BINDING SITE FOR RESIDUE HEC D 703
source : AC3

41) chain D
residue 228
type
sequence V
description BINDING SITE FOR RESIDUE HEC D 703
source : AC3

42) chain E
residue 159
type
sequence C
description BINDING SITE FOR RESIDUE FES E 704
source : AC4

43) chain E
residue 161
type
sequence H
description BINDING SITE FOR RESIDUE FES E 704
source : AC4

44) chain E
residue 162
type
sequence L
description BINDING SITE FOR RESIDUE FES E 704
source : AC4

45) chain E
residue 178
type
sequence C
description BINDING SITE FOR RESIDUE FES E 704
source : AC4

46) chain E
residue 181
type
sequence H
description BINDING SITE FOR RESIDUE FES E 704
source : AC4

47) chain E
residue 183
type
sequence S
description BINDING SITE FOR RESIDUE FES E 704
source : AC4

48) chain C
residue 139
type
sequence M
description BINDING SITE FOR RESIDUE DBT C 705
source : AC5

49) chain C
residue 143
type
sequence G
description BINDING SITE FOR RESIDUE DBT C 705
source : AC5

50) chain C
residue 146
type
sequence V
description BINDING SITE FOR RESIDUE DBT C 705
source : AC5

51) chain C
residue 147
type
sequence I
description BINDING SITE FOR RESIDUE DBT C 705
source : AC5

52) chain C
residue 269
type
sequence I
description BINDING SITE FOR RESIDUE DBT C 705
source : AC5

53) chain C
residue 271
type
sequence P
description BINDING SITE FOR RESIDUE DBT C 705
source : AC5

54) chain C
residue 279
type
sequence Y
description BINDING SITE FOR RESIDUE DBT C 705
source : AC5

55) chain E
residue 181
type
sequence H
description BINDING SITE FOR RESIDUE DBT C 705
source : AC5

56) chain C
residue 16
type
sequence Y
description BINDING SITE FOR RESIDUE UQ6 C 706
source : AC6

57) chain C
residue 22
type
sequence Q
description BINDING SITE FOR RESIDUE UQ6 C 706
source : AC6

58) chain C
residue 26
type
sequence I
description BINDING SITE FOR RESIDUE UQ6 C 706
source : AC6

59) chain C
residue 34
type
sequence S
description BINDING SITE FOR RESIDUE UQ6 C 706
source : AC6

60) chain C
residue 44
type
sequence I
description BINDING SITE FOR RESIDUE UQ6 C 706
source : AC6

61) chain C
residue 201
type
sequence L
description BINDING SITE FOR RESIDUE UQ6 C 706
source : AC6

62) chain C
residue 206
type
sequence S
description BINDING SITE FOR RESIDUE UQ6 C 706
source : AC6

63) chain C
residue 221
type
sequence M
description BINDING SITE FOR RESIDUE UQ6 C 706
source : AC6

64) chain C
residue 229
type
sequence D
description BINDING SITE FOR RESIDUE UQ6 C 706
source : AC6

65) chain C
residue 29
type
sequence W
description BINDING SITE FOR RESIDUE 3PE C 710
source : AC7

66) chain C
residue 97
type
sequence M
description BINDING SITE FOR RESIDUE 3PE C 710
source : AC7

67) chain C
residue 102
type
sequence Y
description BINDING SITE FOR RESIDUE 3PE C 710
source : AC7

68) chain C
residue 103
type
sequence Y
description BINDING SITE FOR RESIDUE 3PE C 710
source : AC7

69) chain C
residue 359
type
sequence Y
description BINDING SITE FOR RESIDUE 3PE C 710
source : AC7

70) chain G
residue 82
type
sequence E
description BINDING SITE FOR RESIDUE 3PE C 710
source : AC7

71) chain H
residue 51
type
sequence R
description BINDING SITE FOR RESIDUE 3PE C 710
source : AC7

72) chain H
residue 52
type
sequence F
description BINDING SITE FOR RESIDUE 3PE C 710
source : AC7

73) chain C
residue 3
type
sequence F
description BINDING SITE FOR RESIDUE 3PE C 711
source : AC8

74) chain C
residue 7
type
sequence N
description BINDING SITE FOR RESIDUE 3PE C 711
source : AC8

75) chain C
residue 9
type
sequence Y
description BINDING SITE FOR RESIDUE 3PE C 711
source : AC8

76) chain C
residue 13
type
sequence V
description BINDING SITE FOR RESIDUE 3PE C 711
source : AC8

77) chain C
residue 112
type
sequence T
description BINDING SITE FOR RESIDUE 3PE C 711
source : AC8

78) chain C
residue 115
type
sequence N
description BINDING SITE FOR RESIDUE 3PE C 711
source : AC8

79) chain A
residue 450
type
sequence S
description BINDING SITE FOR RESIDUE 3PH A 713
source : AC9

80) chain C
residue 230
type
sequence L
description BINDING SITE FOR RESIDUE 3PH A 713
source : AC9

81) chain E
residue 60
type
sequence V
description BINDING SITE FOR RESIDUE 3PH A 713
source : AC9

82) chain E
residue 67
type
sequence S
description BINDING SITE FOR RESIDUE 3PH A 713
source : AC9

83) chain C
residue 237
type
sequence M
description BINDING SITE FOR RESIDUE 3PH D 714
source : BC1

84) chain D
residue 272
type
sequence K
description BINDING SITE FOR RESIDUE 3PH D 714
source : BC1

85) chain D
residue 273
type
sequence T
description BINDING SITE FOR RESIDUE 3PH D 714
source : BC1

86) chain D
residue 276
type
sequence I
description BINDING SITE FOR RESIDUE 3PH D 714
source : BC1

87) chain E
residue 70
type
sequence G
description BINDING SITE FOR RESIDUE 3PH D 714
source : BC1

88) chain E
residue 73
type
sequence S
description BINDING SITE FOR RESIDUE 3PH D 714
source : BC1

89) chain C
residue 253
type
sequence H
description BINDING SITE FOR RESIDUE PC1 D 715
source : BC2

90) chain C
residue 268
type
sequence S
description BINDING SITE FOR RESIDUE PC1 D 715
source : BC2

91) chain C
residue 273
type
sequence W
description BINDING SITE FOR RESIDUE PC1 D 715
source : BC2

92) chain C
residue 337
type
sequence G
description BINDING SITE FOR RESIDUE PC1 D 715
source : BC2

93) chain D
residue 185
type
sequence H
description BINDING SITE FOR RESIDUE PC1 D 715
source : BC2

94) chain A
residue 427
type
sequence W
description BINDING SITE FOR RESIDUE UMQ A 721
source : BC3

95) chain A
residue 428
type
sequence D
description BINDING SITE FOR RESIDUE UMQ A 721
source : BC3

96) chain A
residue 453
type
sequence S
description BINDING SITE FOR RESIDUE UMQ A 721
source : BC3

97) chain A
residue 454
type
sequence M
description BINDING SITE FOR RESIDUE UMQ A 721
source : BC3

98) chain A
residue 455
type
sequence M
description BINDING SITE FOR RESIDUE UMQ A 721
source : BC3

99) chain A
residue 456
type
sequence R
description BINDING SITE FOR RESIDUE UMQ A 721
source : BC3

100) chain E
residue 57
type
sequence Y
description BINDING SITE FOR RESIDUE UMQ A 721
source : BC3

101) chain E
residue 68
type
sequence S
description BINDING SITE FOR RESIDUE UMQ A 721
source : BC3

102) chain I
residue 14
type
sequence N
description BINDING SITE FOR RESIDUE UMQ A 721
source : BC3

103) chain I
residue 15
type
sequence A
description BINDING SITE FOR RESIDUE UMQ A 721
source : BC3

104) chain I
residue 16
type
sequence V
description BINDING SITE FOR RESIDUE UMQ A 721
source : BC3

105) chain I
residue 17
type
sequence F
description BINDING SITE FOR RESIDUE UMQ A 721
source : BC3

106) chain I
residue 18
type
sequence V
description BINDING SITE FOR RESIDUE UMQ A 721
source : BC3

107) chain C
residue 27
type
sequence N
description BINDING SITE FOR RESIDUE CDL D 731
source : BC4

108) chain C
residue 28
type
sequence Y
description BINDING SITE FOR RESIDUE CDL D 731
source : BC4

109) chain C
residue 32
type
sequence M
description BINDING SITE FOR RESIDUE CDL D 731
source : BC4

110) chain C
residue 95
type
sequence M
description BINDING SITE FOR RESIDUE CDL D 731
source : BC4

111) chain C
residue 235
type
sequence L
description BINDING SITE FOR RESIDUE CDL D 731
source : BC4

112) chain D
residue 281
type
sequence Y
description BINDING SITE FOR RESIDUE CDL D 731
source : BC4

113) chain D
residue 288
type
sequence K
description BINDING SITE FOR RESIDUE CDL D 731
source : BC4

114) chain D
residue 289
type
sequence K
description BINDING SITE FOR RESIDUE CDL D 731
source : BC4

115) chain G
residue 85
type
sequence H
description BINDING SITE FOR RESIDUE CDL D 731
source : BC4

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

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

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

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

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

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

122) chain I
residue 19-44
type TRANSMEM
sequence GTIFAGAFVFQTVFDTAITSWYENHN
description Helical => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554
source Swiss-Prot : SWS_FT_FI1

123) 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

124) 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

125) 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

126) 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

127) 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

128) 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

129) 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

130) 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

131) 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

132) 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

133) 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

134) 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

135) 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

136) 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

137) 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

138) 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

139) 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

140) 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

141) 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

142) 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

143) 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

144) 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

145) 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

146) 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

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


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