eF-site ID 2yiu-ABCDEF
PDB Code 2yiu
Chain A, B, C, D, E, F

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Title X-ray structure of the dimeric cytochrome BC1 complex from the soil bacterium paracoccus denitrificans at 2.7 angstrom resolution
Classification OXIDOREDUCTASE
Compound CYTOCHROME B
Source ORGANISM_SCIENTIFIC: PARACOCCUS DENITRIFICANS;
Sequence A:  GIPHDHYEPKTGFERWLHRRLPIVSLVYDTLMIPTPKNLN
WWWIWGIVLAFCLVLQIATGIVLVMHYTPHVDLAFASVEH
IMRDVNGGYMLRYLHANGASLFFLAVYIHIFRGLYYGSYK
APREVTWIVGMLIYLMMMGTAFMGYVLPWGQMSFWGATVI
TGLFGAIPGVGEAIQTWLLGGPAVDNPTLNRFFSLHYLLP
FVIAALVVVHIWAFHTTGNNNPTGVEVRRGSKEEAKKDTL
PFWPYFVIKDLFALAVVLVVFFAIVGFMPNYLGHPDNYIE
ANPLVTPAHIVPEWYFLPFYAILRAFTADVWVVMLVNWLS
FGIIDAKFFGVIAMFGAILVMALVPWLDTSRVRSGQYRPL
FKWWFWLLAVDFVVLMWVGAMPAEGIYPYIALAGSAYWFA
YFLIILPLLGIIEKPDAMPQTIEEDFNA
B:  DISFSFEGPFGKFDQHQLQRGLQVYTEVCSACHGLRYVPL
RTLADEGGPQLPEDQVRAYAANFDITDPETEEDRPRVPTD
HFPTVSGEGMGPDLSLMAKARIGGPEYIHAVLTGYDGEEK
VLYHNAAFAGNWIQMAAPLSDDQVTYEDGTPATVDQMATD
VAAFLMWTAEPKMMDRKQVGFVSVIFLIVLAALLYLTNKK
LWQPIK
C:  DFLYYATAGAGTVAAGAAAWTLVNQMNPSADVQALASIQV
DVSGVETGTQLTVKWLGKPVFIRRRTEDEIQAGREVDLGQ
LIDRSAQNSNKPDAPATDENRTMDEAGEWLVMIGVCTHLG
CVPIGDGAGDFGGWFCPCHGSHYDTSGRIRRGPAPQNLHI
PVAEFLDDTTIKLG
D:  GIPHDHYEPKTGFERWLHRRLPIVSLVYDTLMIPTPKNLN
WWWIWGIVLAFCLVLQIATGIVLVMHYTPHVDLAFASVEH
IMRDVNGGYMLRYLHANGASLFFLAVYIHIFRGLYYGSYK
APREVTWIVGMLIYLMMMGTAFMGYVLPWGQMSFWGATVI
TGLFGAIPGVGEAIQTWLLGGPAVDNPTLNRFFSLHYLLP
FVIAALVVVHIWAFHTTGNNNPTGVEVRRGSKEEAKKDTL
PFWPYFVIKDLFALAVVLVVFFAIVGFMPNYLGHPDNYIE
ANPLVTPAHIVPEWYFLPFYAILRAFTADVWVVMLVNWLS
FGIIDAKFFGVIAMFGAILVMALVPWLDTSRVRSGQYRPL
FKWWFWLLAVDFVVLMWVGAMPAEGIYPYIALAGSAYWFA
YFLIILPLLGIIEKPDAMPQTIEEDFNA
E:  DISFSFEGPFGKFDQHQLQRGLQVYTEVCSACHGLRYVPL
RTLADEGGPQLPEDQVRAYAANFDITDPETEEDRPRVPTD
HFPTVSGEGMGPDLSLMAKARIGGPEYIHAVLTGYDGEEK
VLYHNAAFAGNWIQMAAPLSDDQVTYEDGTPATVDQMATD
VAAFLMWTAEPKMMDRKQVGFVSVIFLIVLAALLYLTNKK
LWQPIK
F:  DFLYYATAGAGTVAAGAAAWTLVNQMNPSADVQALASIQV
DVSGVETGTQLTVKWLGKPVFIRRRTEDEIQAGREVDLGQ
LIDRSAQNSNKPDAPATDENRTMDEAGEWLVMIGVCTHLG
CVPIGDGAGDFGGWFCPCHGSHYDTSGRIRRGPAPQNLHI
PVAEFLDDTTIKLG
Description


Functional site

1) chain A
residue 58
type
sequence Q
description BINDING SITE FOR RESIDUE HEM A 500
source : AC1

2) chain A
residue 62
type
sequence G
description BINDING SITE FOR RESIDUE HEM A 500
source : AC1

3) chain A
residue 63
type
sequence I
description BINDING SITE FOR RESIDUE HEM A 500
source : AC1

4) chain A
residue 66
type
sequence V
description BINDING SITE FOR RESIDUE HEM A 500
source : AC1

5) chain A
residue 94
type
sequence R
description BINDING SITE FOR RESIDUE HEM A 500
source : AC1

6) chain A
residue 97
type
sequence H
description BINDING SITE FOR RESIDUE HEM A 500
source : AC1

7) chain A
residue 104
type
sequence F
description BINDING SITE FOR RESIDUE HEM A 500
source : AC1

8) chain A
residue 142
type
sequence T
description BINDING SITE FOR RESIDUE HEM A 500
source : AC1

9) chain A
residue 146
type
sequence G
description BINDING SITE FOR RESIDUE HEM A 500
source : AC1

10) chain A
residue 149
type
sequence L
description BINDING SITE FOR RESIDUE HEM A 500
source : AC1

11) chain A
residue 150
type
sequence P
description BINDING SITE FOR RESIDUE HEM A 500
source : AC1

12) chain A
residue 198
type
sequence H
description BINDING SITE FOR RESIDUE HEM A 500
source : AC1

13) chain A
residue 202
type
sequence P
description BINDING SITE FOR RESIDUE HEM A 500
source : AC1

14) chain A
residue 45
type
sequence W
description BINDING SITE FOR RESIDUE HEM A 501
source : AC2

15) chain A
residue 48
type
sequence G
description BINDING SITE FOR RESIDUE HEM A 501
source : AC2

16) chain A
residue 51
type
sequence L
description BINDING SITE FOR RESIDUE HEM A 501
source : AC2

17) chain A
residue 52
type
sequence A
description BINDING SITE FOR RESIDUE HEM A 501
source : AC2

18) chain A
residue 111
type
sequence H
description BINDING SITE FOR RESIDUE HEM A 501
source : AC2

19) chain A
residue 114
type
sequence R
description BINDING SITE FOR RESIDUE HEM A 501
source : AC2

20) chain A
residue 120
type
sequence S
description BINDING SITE FOR RESIDUE HEM A 501
source : AC2

21) chain A
residue 125
type
sequence R
description BINDING SITE FOR RESIDUE HEM A 501
source : AC2

22) chain A
residue 129
type
sequence W
description BINDING SITE FOR RESIDUE HEM A 501
source : AC2

23) chain A
residue 132
type
sequence G
description BINDING SITE FOR RESIDUE HEM A 501
source : AC2

24) chain A
residue 133
type
sequence M
description BINDING SITE FOR RESIDUE HEM A 501
source : AC2

25) chain A
residue 135
type
sequence I
description BINDING SITE FOR RESIDUE HEM A 501
source : AC2

26) chain A
residue 212
type
sequence H
description BINDING SITE FOR RESIDUE HEM A 501
source : AC2

27) chain A
residue 216
type
sequence F
description BINDING SITE FOR RESIDUE HEM A 501
source : AC2

28) chain A
residue 220
type
sequence G
description BINDING SITE FOR RESIDUE HEM A 501
source : AC2

29) chain A
residue 221
type
sequence N
description BINDING SITE FOR RESIDUE HEM A 501
source : AC2

30) chain A
residue 222
type
sequence N
description BINDING SITE FOR RESIDUE HEM A 501
source : AC2

31) chain A
residue 137
type
sequence L
description BINDING SITE FOR RESIDUE SMA A 502
source : AC3

32) chain A
residue 154
type
sequence M
description BINDING SITE FOR RESIDUE SMA A 502
source : AC3

33) chain A
residue 158
type
sequence G
description BINDING SITE FOR RESIDUE SMA A 502
source : AC3

34) chain A
residue 161
type
sequence V
description BINDING SITE FOR RESIDUE SMA A 502
source : AC3

35) chain A
residue 194
type
sequence F
description BINDING SITE FOR RESIDUE SMA A 502
source : AC3

36) chain A
residue 292
type
sequence I
description BINDING SITE FOR RESIDUE SMA A 502
source : AC3

37) chain A
residue 295
type
sequence E
description BINDING SITE FOR RESIDUE SMA A 502
source : AC3

38) chain A
residue 298
type
sequence F
description BINDING SITE FOR RESIDUE SMA A 502
source : AC3

39) chain A
residue 302
type
sequence Y
description BINDING SITE FOR RESIDUE SMA A 502
source : AC3

40) chain A
residue 336
type
sequence M
description BINDING SITE FOR RESIDUE SMA A 502
source : AC3

41) chain A
residue 337
type
sequence F
description BINDING SITE FOR RESIDUE SMA A 502
source : AC3

42) chain F
residue 154
type
sequence C
description BINDING SITE FOR RESIDUE SMA A 502
source : AC3

43) chain F
residue 155
type
sequence H
description BINDING SITE FOR RESIDUE SMA A 502
source : AC3

44) chain B
residue 81
type
sequence V
description BINDING SITE FOR RESIDUE HEC B 500
source : AC4

45) chain B
residue 82
type
sequence C
description BINDING SITE FOR RESIDUE HEC B 500
source : AC4

46) chain B
residue 85
type
sequence C
description BINDING SITE FOR RESIDUE HEC B 500
source : AC4

47) chain B
residue 86
type
sequence H
description BINDING SITE FOR RESIDUE HEC B 500
source : AC4

48) chain B
residue 145
type
sequence P
description BINDING SITE FOR RESIDUE HEC B 500
source : AC4

49) chain B
residue 154
type
sequence R
description BINDING SITE FOR RESIDUE HEC B 500
source : AC4

50) chain B
residue 177
type
sequence Y
description BINDING SITE FOR RESIDUE HEC B 500
source : AC4

51) chain B
residue 182
type
sequence L
description BINDING SITE FOR RESIDUE HEC B 500
source : AC4

52) chain B
residue 203
type
sequence F
description BINDING SITE FOR RESIDUE HEC B 500
source : AC4

53) chain B
residue 209
type
sequence Q
description BINDING SITE FOR RESIDUE HEC B 500
source : AC4

54) chain B
residue 210
type
sequence M
description BINDING SITE FOR RESIDUE HEC B 500
source : AC4

55) chain C
residue 132
type
sequence C
description BINDING SITE FOR RESIDUE FES C 500
source : AC5

56) chain C
residue 134
type
sequence H
description BINDING SITE FOR RESIDUE FES C 500
source : AC5

57) chain C
residue 135
type
sequence L
description BINDING SITE FOR RESIDUE FES C 500
source : AC5

58) chain C
residue 152
type
sequence C
description BINDING SITE FOR RESIDUE FES C 500
source : AC5

59) chain C
residue 155
type
sequence H
description BINDING SITE FOR RESIDUE FES C 500
source : AC5

60) chain C
residue 157
type
sequence S
description BINDING SITE FOR RESIDUE FES C 500
source : AC5

61) chain D
residue 58
type
sequence Q
description BINDING SITE FOR RESIDUE HEM D 500
source : AC6

62) chain D
residue 62
type
sequence G
description BINDING SITE FOR RESIDUE HEM D 500
source : AC6

63) chain D
residue 63
type
sequence I
description BINDING SITE FOR RESIDUE HEM D 500
source : AC6

64) chain D
residue 66
type
sequence V
description BINDING SITE FOR RESIDUE HEM D 500
source : AC6

65) chain D
residue 94
type
sequence R
description BINDING SITE FOR RESIDUE HEM D 500
source : AC6

66) chain D
residue 97
type
sequence H
description BINDING SITE FOR RESIDUE HEM D 500
source : AC6

67) chain D
residue 98
type
sequence A
description BINDING SITE FOR RESIDUE HEM D 500
source : AC6

68) chain D
residue 104
type
sequence F
description BINDING SITE FOR RESIDUE HEM D 500
source : AC6

69) chain D
residue 146
type
sequence G
description BINDING SITE FOR RESIDUE HEM D 500
source : AC6

70) chain D
residue 149
type
sequence L
description BINDING SITE FOR RESIDUE HEM D 500
source : AC6

71) chain D
residue 150
type
sequence P
description BINDING SITE FOR RESIDUE HEM D 500
source : AC6

72) chain D
residue 198
type
sequence H
description BINDING SITE FOR RESIDUE HEM D 500
source : AC6

73) chain D
residue 202
type
sequence P
description BINDING SITE FOR RESIDUE HEM D 500
source : AC6

74) chain D
residue 45
type
sequence W
description BINDING SITE FOR RESIDUE HEM D 501
source : AC7

75) chain D
residue 48
type
sequence G
description BINDING SITE FOR RESIDUE HEM D 501
source : AC7

76) chain D
residue 51
type
sequence L
description BINDING SITE FOR RESIDUE HEM D 501
source : AC7

77) chain D
residue 52
type
sequence A
description BINDING SITE FOR RESIDUE HEM D 501
source : AC7

78) chain D
residue 111
type
sequence H
description BINDING SITE FOR RESIDUE HEM D 501
source : AC7

79) chain D
residue 114
type
sequence R
description BINDING SITE FOR RESIDUE HEM D 501
source : AC7

80) chain D
residue 120
type
sequence S
description BINDING SITE FOR RESIDUE HEM D 501
source : AC7

81) chain D
residue 125
type
sequence R
description BINDING SITE FOR RESIDUE HEM D 501
source : AC7

82) chain D
residue 132
type
sequence G
description BINDING SITE FOR RESIDUE HEM D 501
source : AC7

83) chain D
residue 133
type
sequence M
description BINDING SITE FOR RESIDUE HEM D 501
source : AC7

84) chain D
residue 135
type
sequence I
description BINDING SITE FOR RESIDUE HEM D 501
source : AC7

85) chain D
residue 209
type
sequence V
description BINDING SITE FOR RESIDUE HEM D 501
source : AC7

86) chain D
residue 212
type
sequence H
description BINDING SITE FOR RESIDUE HEM D 501
source : AC7

87) chain D
residue 216
type
sequence F
description BINDING SITE FOR RESIDUE HEM D 501
source : AC7

88) chain D
residue 220
type
sequence G
description BINDING SITE FOR RESIDUE HEM D 501
source : AC7

89) chain D
residue 221
type
sequence N
description BINDING SITE FOR RESIDUE HEM D 501
source : AC7

90) chain D
residue 222
type
sequence N
description BINDING SITE FOR RESIDUE HEM D 501
source : AC7

91) chain C
residue 154
type
sequence C
description BINDING SITE FOR RESIDUE SMA D 502
source : AC8

92) chain C
residue 155
type
sequence H
description BINDING SITE FOR RESIDUE SMA D 502
source : AC8

93) chain D
residue 137
type
sequence L
description BINDING SITE FOR RESIDUE SMA D 502
source : AC8

94) chain D
residue 140
type
sequence M
description BINDING SITE FOR RESIDUE SMA D 502
source : AC8

95) chain D
residue 161
type
sequence V
description BINDING SITE FOR RESIDUE SMA D 502
source : AC8

96) chain D
residue 292
type
sequence I
description BINDING SITE FOR RESIDUE SMA D 502
source : AC8

97) chain D
residue 294
type
sequence P
description BINDING SITE FOR RESIDUE SMA D 502
source : AC8

98) chain D
residue 295
type
sequence E
description BINDING SITE FOR RESIDUE SMA D 502
source : AC8

99) chain D
residue 298
type
sequence F
description BINDING SITE FOR RESIDUE SMA D 502
source : AC8

100) chain D
residue 302
type
sequence Y
description BINDING SITE FOR RESIDUE SMA D 502
source : AC8

101) chain D
residue 336
type
sequence M
description BINDING SITE FOR RESIDUE SMA D 502
source : AC8

102) chain D
residue 337
type
sequence F
description BINDING SITE FOR RESIDUE SMA D 502
source : AC8

103) chain D
residue 340
type
sequence I
description BINDING SITE FOR RESIDUE SMA D 502
source : AC8

104) chain E
residue 81
type
sequence V
description BINDING SITE FOR RESIDUE HEC E 500
source : AC9

105) chain E
residue 82
type
sequence C
description BINDING SITE FOR RESIDUE HEC E 500
source : AC9

106) chain E
residue 85
type
sequence C
description BINDING SITE FOR RESIDUE HEC E 500
source : AC9

107) chain E
residue 86
type
sequence H
description BINDING SITE FOR RESIDUE HEC E 500
source : AC9

108) chain E
residue 154
type
sequence R
description BINDING SITE FOR RESIDUE HEC E 500
source : AC9

109) chain E
residue 177
type
sequence Y
description BINDING SITE FOR RESIDUE HEC E 500
source : AC9

110) chain E
residue 203
type
sequence F
description BINDING SITE FOR RESIDUE HEC E 500
source : AC9

111) chain E
residue 209
type
sequence Q
description BINDING SITE FOR RESIDUE HEC E 500
source : AC9

112) chain E
residue 210
type
sequence M
description BINDING SITE FOR RESIDUE HEC E 500
source : AC9

113) chain E
residue 213
type
sequence P
description BINDING SITE FOR RESIDUE HEC E 500
source : AC9

114) chain F
residue 132
type
sequence C
description BINDING SITE FOR RESIDUE FES F 500
source : BC1

115) chain F
residue 134
type
sequence H
description BINDING SITE FOR RESIDUE FES F 500
source : BC1

116) chain F
residue 135
type
sequence L
description BINDING SITE FOR RESIDUE FES F 500
source : BC1

117) chain F
residue 152
type
sequence C
description BINDING SITE FOR RESIDUE FES F 500
source : BC1

118) chain F
residue 155
type
sequence H
description BINDING SITE FOR RESIDUE FES F 500
source : BC1

119) chain F
residue 157
type
sequence S
description BINDING SITE FOR RESIDUE FES F 500
source : BC1

120) chain C
residue 18-39
type TRANSMEM
sequence FLYYATAGAGTVAAGAAAWTLV
description Helical => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

121) chain F
residue 18-39
type TRANSMEM
sequence FLYYATAGAGTVAAGAAAWTLV
description Helical => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

122) chain A
residue 129-149
type TRANSMEM
sequence WIVGMLIYLMMMGTAFMGYVL
description Helical => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

123) chain A
residue 156-176
type TRANSMEM
sequence FWGATVITGLFGAIPGVGEAI
description Helical => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

124) chain A
residue 194-214
type TRANSMEM
sequence FFSLHYLLPFVIAALVVVHIW
description Helical => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

125) chain A
residue 253-273
type TRANSMEM
sequence LFALAVVLVVFFAIVGFMPNY
description Helical => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

126) chain A
residue 296-315
type TRANSMEM
sequence WYFLPFYAILRAFTADVWVV
description Helical => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

127) chain A
residue 330-350
type TRANSMEM
sequence FFGVIAMFGAILVMALVPWLD
description Helical => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

128) chain A
residue 365-385
type TRANSMEM
sequence WWFWLLAVDFVVLMWVGAMPA
description Helical => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

129) chain A
residue 394-414
type TRANSMEM
sequence LAGSAYWFAYFLIILPLLGII
description Helical => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

130) chain D
residue 46-66
type TRANSMEM
sequence IWGIVLAFCLVLQIATGIVLV
description Helical => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

131) chain D
residue 100-120
type TRANSMEM
sequence GASLFFLAVYIHIFRGLYYGS
description Helical => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

132) chain D
residue 129-149
type TRANSMEM
sequence WIVGMLIYLMMMGTAFMGYVL
description Helical => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

133) chain D
residue 156-176
type TRANSMEM
sequence FWGATVITGLFGAIPGVGEAI
description Helical => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

134) chain D
residue 194-214
type TRANSMEM
sequence FFSLHYLLPFVIAALVVVHIW
description Helical => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

135) chain D
residue 253-273
type TRANSMEM
sequence LFALAVVLVVFFAIVGFMPNY
description Helical => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

136) chain D
residue 296-315
type TRANSMEM
sequence WYFLPFYAILRAFTADVWVV
description Helical => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

137) chain D
residue 330-350
type TRANSMEM
sequence FFGVIAMFGAILVMALVPWLD
description Helical => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

138) chain D
residue 365-385
type TRANSMEM
sequence WWFWLLAVDFVVLMWVGAMPA
description Helical => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

139) chain D
residue 394-414
type TRANSMEM
sequence LAGSAYWFAYFLIILPLLGII
description Helical => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

140) chain C
residue 152
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628
source Swiss-Prot : SWS_FT_FI2

141) chain F
residue 132
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628
source Swiss-Prot : SWS_FT_FI2

142) chain F
residue 134
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628
source Swiss-Prot : SWS_FT_FI2

143) chain F
residue 152
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628
source Swiss-Prot : SWS_FT_FI2

144) chain F
residue 155
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628
source Swiss-Prot : SWS_FT_FI2

145) chain C
residue 155
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628
source Swiss-Prot : SWS_FT_FI2

146) chain C
residue 132
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628
source Swiss-Prot : SWS_FT_FI2

147) chain C
residue 134
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00628
source Swiss-Prot : SWS_FT_FI2

148) chain B
residue 86
type BINDING
sequence H
description axial binding residue
source Swiss-Prot : SWS_FT_FI3

149) chain E
residue 86
type BINDING
sequence H
description axial binding residue
source Swiss-Prot : SWS_FT_FI3

150) chain B
residue 210
type BINDING
sequence M
description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00433
source Swiss-Prot : SWS_FT_FI4

151) chain E
residue 210
type BINDING
sequence M
description axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00433
source Swiss-Prot : SWS_FT_FI4


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