eF-site ID 3bcc-ABCDEFGHIJ
PDB Code 3bcc
Chain A, B, C, D, E, F, G, H, I, J

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Title STIGMATELLIN AND ANTIMYCIN BOUND CYTOCHROME BC1 COMPLEX FROM CHICKEN
Classification OXIDOREDUCTASE
Compound UBIQUINOL CYTOCHROME C OXIDOREDUCTASE
Source ORGANISM_COMMON: chicken; ORGANISM_SCIENTIFIC: Gallus gallus;
Sequence A:  YAQALQSVPETQVSQLDNGVRVASEQSSQPTCTVGVWIDA
GSRYESEKNNGAGYFLEHLAFKGTKNRPQNALEKEVESMG
AHLNAYSSREHTAYYIKALSKDVPKAVELLADIVQNCSLE
DSQIEKERDVIVRELQENDTSMREVVFNYLHATAFQGTGL
AQSVEGPSENIRKLSRADLTEYLSTHYTAPRMVLAAAGGV
EHQQLLELAQKHFGGVPFTYDDDAVPTLSKCRFTGSQIRH
REDGLPLAHVAIAVEGPGWAHPDLVALQVANAIIGHYDRT
YGGGLHSSSPLASIAVTNKLCQSFQTFSICYSETGLFGFY
FVCDRMSIDDMMFVLQGQWMRLCTSISESEVLRGKNFLRN
ALVSHLDGTTPVCEDIGRELLTYGRRIPLEEWEERLAEVD
ARMVREVCSKYIYDQCPAVAGPGPIEQLPDYNRIRSGMFW
LR
B:  PPHPQDLEITKLPNGLVIASLENYSPGSTIGVFIKAGSRY
ENSSNLGTSHLLRLASSLTTKGASSFKITRGIEAVGGKLS
VESTRENMAYTVECLRDDVEILMEFLLNVTTAPEFRPWEV
ADLQPQLKIDKAVAFQNPQTHVIENLHAAAYRNALADSLY
CPDYRIGKVTSVELHDFVQNHFTSARMALVGLGVSHPVLK
NVAEQLLNIRGGLGLSGAKAKYRGGEIREQNGDSLVHAAI
VAESAAIGGAEANAFSVLQHVLGANPHVKRGNPFDVSAFN
ASYSDSGLFGFYTISQAAYAGQVIKAAYNQVKTIAQGNVS
NENVQAAKNKLKAKYLMSVESSEGFLEEVGSQALAAGSYN
PPSTVLQQIDAVADADVIKAAKKFVSRQKSMAASGNLGHT
PFVDEL
C:  APNIRKSHPLLKMINNSLIDLPAPSNISAWWNFGSLLAVC
LMTQILTGLLLAMHYTADTSLAFSSVAHTCRNVQYGWLIR
NLHANGASFFFICIFLHIGRGLYYGSYLYKETWNTGVILL
LTLMATAFVGYVLPWGQMSFWGATVITNLFSAIPYIGHTL
VEWAWGGFSVDNPTLTRFFALHFLLPFAIAGITIIHLTFL
HESGSNNPLGISSDSDKIPFHPYYSFKDILGLTLMLTPFL
TLALFSPNLLGDPENFTPANPLVTPPHIKPEWYFLFAYAI
LRSIPNKLGGVLALAASVLILFLIPFLHKSKQRTMTFRPL
SQTLFWLLVANLLILTWIGSQPVEHPFIIIGQMASLSYFT
ILLILFPTIGTLENKMLNY
D:  SDLELHPPSYPWSHRGPLSSLDHTSIRRGFQVYKQVCSSC
HSMDYVAYRHLVGVCYTEDEAKALAEEVEVQDGPNEDGEM
FMRPGKLSDYFPKPYPNPEAARAANNGALPPDLSYIVRAR
HGGEDYVFSLLTGYCEPPTGVSVREGLYFNPYFPGQAIGM
APPIYNDVLEFDDGTPATMSQVAKDVCTFLRWAAEPEHDH
RKRMGLKMLLMMGLLVPLVYYMKRHKWSVLKSRKLAYRPP
K
E:  SHTDIKVPNFSDYRRPPDDYSTKSSRESDPSRKGFSYLVT
AVTTLGVAYAAKNVVTQFVSSMSASADVLAMSKIEIKLSD
IPEGKNMAFKWRGKPLFVRHRTKKEIDQEAAVEVSQLRDP
QHDLERVKKPEWVILIGVCTHLGCVPIANAGDFGGYYCPC
HGSHYDASGRIRKGPAPLNLEVPSYEFTSDDMVIVG
F:  SRWLEGIRKWYYNAAGFNKYGLMRDDTIYENDDVKEAIRR
LPENLYDDRMFRIKRALDLNMRQQILPKEQWTKYEEDVPY
LEPYLKEVIRERKEREEWDK
G:  RQFGHLTRVRHLITYSLSPFEQRPFPHYFSKGVPNVWRRL
RACILRVAPPFLAFYLLYTWGTQEFEKSKRKNPAAYVN
H:  LVDPLTTVREQCEQLEKCVKARERLELCDERVSSRSQTEE
DCTEELFDFLHARDHCVAHKLFNSLK
I:  XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
J:  TLTARLYSLLFRRTSTFALTIVVGALLFERAFDQGADAIY
EHINEGKLWKHIKHKYENK
Description


Functional site

1) chain C
residue 45
type
sequence Q
description BINDING SITE FOR RESIDUE HEM C 381
source : AC1

2) chain C
residue 46
type
sequence I
description BINDING SITE FOR RESIDUE HEM C 381
source : AC1

3) chain C
residue 49
type
sequence G
description BINDING SITE FOR RESIDUE HEM C 381
source : AC1

4) chain C
residue 50
type
sequence L
description BINDING SITE FOR RESIDUE HEM C 381
source : AC1

5) chain C
residue 52
type
sequence L
description BINDING SITE FOR RESIDUE HEM C 381
source : AC1

6) chain C
residue 53
type
sequence A
description BINDING SITE FOR RESIDUE HEM C 381
source : AC1

7) chain C
residue 81
type
sequence R
description BINDING SITE FOR RESIDUE HEM C 381
source : AC1

8) chain C
residue 84
type
sequence H
description BINDING SITE FOR RESIDUE HEM C 381
source : AC1

9) chain C
residue 85
type
sequence A
description BINDING SITE FOR RESIDUE HEM C 381
source : AC1

10) chain C
residue 124
type
sequence L
description BINDING SITE FOR RESIDUE HEM C 381
source : AC1

11) chain C
residue 127
type
sequence T
description BINDING SITE FOR RESIDUE HEM C 381
source : AC1

12) chain C
residue 128
type
sequence A
description BINDING SITE FOR RESIDUE HEM C 381
source : AC1

13) chain C
residue 131
type
sequence G
description BINDING SITE FOR RESIDUE HEM C 381
source : AC1

14) chain C
residue 132
type
sequence Y
description BINDING SITE FOR RESIDUE HEM C 381
source : AC1

15) chain C
residue 134
type
sequence L
description BINDING SITE FOR RESIDUE HEM C 381
source : AC1

16) chain C
residue 135
type
sequence P
description BINDING SITE FOR RESIDUE HEM C 381
source : AC1

17) chain C
residue 183
type
sequence H
description BINDING SITE FOR RESIDUE HEM C 381
source : AC1

18) chain C
residue 184
type
sequence F
description BINDING SITE FOR RESIDUE HEM C 381
source : AC1

19) chain C
residue 187
type
sequence P
description BINDING SITE FOR RESIDUE HEM C 381
source : AC1

20) chain C
residue 32
type
sequence W
description BINDING SITE FOR RESIDUE HEM C 382
source : AC2

21) chain C
residue 34
type
sequence F
description BINDING SITE FOR RESIDUE HEM C 382
source : AC2

22) chain C
residue 35
type
sequence G
description BINDING SITE FOR RESIDUE HEM C 382
source : AC2

23) chain C
residue 36
type
sequence S
description BINDING SITE FOR RESIDUE HEM C 382
source : AC2

24) chain C
residue 38
type
sequence L
description BINDING SITE FOR RESIDUE HEM C 382
source : AC2

25) chain C
residue 39
type
sequence A
description BINDING SITE FOR RESIDUE HEM C 382
source : AC2

26) chain C
residue 98
type
sequence H
description BINDING SITE FOR RESIDUE HEM C 382
source : AC2

27) chain C
residue 99
type
sequence I
description BINDING SITE FOR RESIDUE HEM C 382
source : AC2

28) chain C
residue 101
type
sequence R
description BINDING SITE FOR RESIDUE HEM C 382
source : AC2

29) chain C
residue 107
type
sequence S
description BINDING SITE FOR RESIDUE HEM C 382
source : AC2

30) chain C
residue 110
type
sequence Y
description BINDING SITE FOR RESIDUE HEM C 382
source : AC2

31) chain C
residue 114
type
sequence W
description BINDING SITE FOR RESIDUE HEM C 382
source : AC2

32) chain C
residue 117
type
sequence G
description BINDING SITE FOR RESIDUE HEM C 382
source : AC2

33) chain C
residue 118
type
sequence V
description BINDING SITE FOR RESIDUE HEM C 382
source : AC2

34) chain C
residue 120
type
sequence L
description BINDING SITE FOR RESIDUE HEM C 382
source : AC2

35) chain C
residue 121
type
sequence L
description BINDING SITE FOR RESIDUE HEM C 382
source : AC2

36) chain C
residue 194
type
sequence T
description BINDING SITE FOR RESIDUE HEM C 382
source : AC2

37) chain C
residue 197
type
sequence H
description BINDING SITE FOR RESIDUE HEM C 382
source : AC2

38) chain C
residue 201
type
sequence L
description BINDING SITE FOR RESIDUE HEM C 382
source : AC2

39) chain C
residue 207
type
sequence N
description BINDING SITE FOR RESIDUE HEM C 382
source : AC2

40) chain D
residue 36
type
sequence V
description BINDING SITE FOR RESIDUE HEM D 242
source : AC3

41) chain D
residue 37
type
sequence C
description BINDING SITE FOR RESIDUE HEM D 242
source : AC3

42) chain D
residue 40
type
sequence C
description BINDING SITE FOR RESIDUE HEM D 242
source : AC3

43) chain D
residue 41
type
sequence H
description BINDING SITE FOR RESIDUE HEM D 242
source : AC3

44) chain D
residue 105
type
sequence N
description BINDING SITE FOR RESIDUE HEM D 242
source : AC3

45) chain D
residue 110
type
sequence P
description BINDING SITE FOR RESIDUE HEM D 242
source : AC3

46) chain D
residue 111
type
sequence P
description BINDING SITE FOR RESIDUE HEM D 242
source : AC3

47) chain D
residue 120
type
sequence R
description BINDING SITE FOR RESIDUE HEM D 242
source : AC3

48) chain D
residue 126
type
sequence Y
description BINDING SITE FOR RESIDUE HEM D 242
source : AC3

49) chain D
residue 153
type
sequence F
description BINDING SITE FOR RESIDUE HEM D 242
source : AC3

50) chain D
residue 158
type
sequence I
description BINDING SITE FOR RESIDUE HEM D 242
source : AC3

51) chain D
residue 159
type
sequence G
description BINDING SITE FOR RESIDUE HEM D 242
source : AC3

52) chain D
residue 160
type
sequence M
description BINDING SITE FOR RESIDUE HEM D 242
source : AC3

53) chain D
residue 163
type
sequence P
description BINDING SITE FOR RESIDUE HEM D 242
source : AC3

54) chain D
residue 186
type
sequence V
description BINDING SITE FOR RESIDUE HEM D 242
source : AC3

55) chain E
residue 139
type
sequence C
description BINDING SITE FOR RESIDUE FES E 197
source : AC4

56) chain E
residue 141
type
sequence H
description BINDING SITE FOR RESIDUE FES E 197
source : AC4

57) chain E
residue 144
type
sequence C
description BINDING SITE FOR RESIDUE FES E 197
source : AC4

58) chain E
residue 158
type
sequence C
description BINDING SITE FOR RESIDUE FES E 197
source : AC4

59) chain E
residue 160
type
sequence C
description BINDING SITE FOR RESIDUE FES E 197
source : AC4

60) chain E
residue 161
type
sequence H
description BINDING SITE FOR RESIDUE FES E 197
source : AC4

61) chain E
residue 162
type
sequence G
description BINDING SITE FOR RESIDUE FES E 197
source : AC4

62) chain E
residue 163
type
sequence S
description BINDING SITE FOR RESIDUE FES E 197
source : AC4

63) chain C
residue 125
type
sequence M
description BINDING SITE FOR RESIDUE SIG C 383
source : AC5

64) chain C
residue 129
type
sequence F
description BINDING SITE FOR RESIDUE SIG C 383
source : AC5

65) chain C
residue 130
type
sequence V
description BINDING SITE FOR RESIDUE SIG C 383
source : AC5

66) chain C
residue 146
type
sequence V
description BINDING SITE FOR RESIDUE SIG C 383
source : AC5

67) chain C
residue 147
type
sequence I
description BINDING SITE FOR RESIDUE SIG C 383
source : AC5

68) chain C
residue 182
type
sequence L
description BINDING SITE FOR RESIDUE SIG C 383
source : AC5

69) chain C
residue 271
type
sequence P
description BINDING SITE FOR RESIDUE SIG C 383
source : AC5

70) chain C
residue 275
type
sequence F
description BINDING SITE FOR RESIDUE SIG C 383
source : AC5

71) chain C
residue 279
type
sequence Y
description BINDING SITE FOR RESIDUE SIG C 383
source : AC5

72) chain C
residue 295
type
sequence L
description BINDING SITE FOR RESIDUE SIG C 383
source : AC5

73) chain C
residue 18
type
sequence S
description BINDING SITE FOR RESIDUE AMY C 384
source : AC6

74) chain C
residue 32
type
sequence W
description BINDING SITE FOR RESIDUE AMY C 384
source : AC6

75) chain C
residue 33
type
sequence N
description BINDING SITE FOR RESIDUE AMY C 384
source : AC6

76) chain C
residue 35
type
sequence G
description BINDING SITE FOR RESIDUE AMY C 384
source : AC6

77) chain C
residue 36
type
sequence S
description BINDING SITE FOR RESIDUE AMY C 384
source : AC6

78) chain C
residue 39
type
sequence A
description BINDING SITE FOR RESIDUE AMY C 384
source : AC6

79) chain C
residue 42
type
sequence L
description BINDING SITE FOR RESIDUE AMY C 384
source : AC6

80) chain C
residue 43
type
sequence M
description BINDING SITE FOR RESIDUE AMY C 384
source : AC6

81) chain C
residue 191
type
sequence A
description BINDING SITE FOR RESIDUE AMY C 384
source : AC6

82) chain C
residue 194
type
sequence T
description BINDING SITE FOR RESIDUE AMY C 384
source : AC6

83) chain C
residue 195
type
sequence I
description BINDING SITE FOR RESIDUE AMY C 384
source : AC6

84) chain C
residue 198
type
sequence L
description BINDING SITE FOR RESIDUE AMY C 384
source : AC6

85) chain C
residue 221
type
sequence F
description BINDING SITE FOR RESIDUE AMY C 384
source : AC6

86) chain C
residue 225
type
sequence Y
description BINDING SITE FOR RESIDUE AMY C 384
source : AC6

87) chain C
residue 228
type
sequence K
description BINDING SITE FOR RESIDUE AMY C 384
source : AC6

88) chain C
residue 229
type
sequence D
description BINDING SITE FOR RESIDUE AMY C 384
source : AC6

89) chain B
residue 54-77
type prosite
sequence GSRYENSSNLGTSHLLRLASSLTT
description INSULINASE Insulinase family, zinc-binding region signature. GsryenssnlGtSHLLRLAsSlTT
source prosite : PS00143

90) chain D
residue 124
type TOPO_DOM
sequence E
description Mitochondrial matrix => ECO:0000269|PubMed:9651245
source Swiss-Prot : SWS_FT_FI1

91) chain C
residue 114-134
type TOPO_DOM
sequence WNTGVILLLTLMATAFVGYVL
description Mitochondrial matrix => ECO:0000269|PubMed:9651245
source Swiss-Prot : SWS_FT_FI1

92) chain C
residue 179-199
type TOPO_DOM
sequence FFALHFLLPFAIAGITIIHLT
description Mitochondrial matrix => ECO:0000269|PubMed:9651245
source Swiss-Prot : SWS_FT_FI1

93) chain C
residue 227-247
type TOPO_DOM
sequence FKDILGLTLMLTPFLTLALFS
description Mitochondrial matrix => ECO:0000269|PubMed:9651245
source Swiss-Prot : SWS_FT_FI1

94) chain C
residue 289-309
type TOPO_DOM
sequence LGGVLALAASVLILFLIPFLH
description Mitochondrial matrix => ECO:0000269|PubMed:9651245
source Swiss-Prot : SWS_FT_FI1

95) chain C
residue 321-341
type TOPO_DOM
sequence LSQTLFWLLVANLLILTWIGS
description Mitochondrial matrix => ECO:0000269|PubMed:9651245
source Swiss-Prot : SWS_FT_FI1

96) chain C
residue 348-368
type TOPO_DOM
sequence FIIIGQMASLSYFTILLILFP
description Mitochondrial matrix => ECO:0000269|PubMed:9651245
source Swiss-Prot : SWS_FT_FI1

97) chain J
residue 22-47
type TRANSMEM
sequence LTIVVGALLFERAFDQGADAIYEHIN
description Helical => ECO:0000269|PubMed:9651245
source Swiss-Prot : SWS_FT_FI2

98) chain F
residue 83
type TRANSMEM
sequence Y
description Helical => ECO:0000269|PubMed:9651245
source Swiss-Prot : SWS_FT_FI2

99) chain F
residue 96
type TRANSMEM
sequence E
description Helical => ECO:0000269|PubMed:9651245
source Swiss-Prot : SWS_FT_FI2

100) chain G
residue 33
type MOD_RES
sequence G
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CQ69
source Swiss-Prot : SWS_FT_FI3

101) chain F
residue 88
type MOD_RES
sequence P
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CQ69
source Swiss-Prot : SWS_FT_FI3

102) chain E
residue 139
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:9651245, ECO:0007744|PDB:1BE3, ECO:0007744|PDB:1BGY
source Swiss-Prot : SWS_FT_FI4

103) chain E
residue 141
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:9651245, ECO:0007744|PDB:1BE3, ECO:0007744|PDB:1BGY
source Swiss-Prot : SWS_FT_FI4

104) chain E
residue 158
type BINDING
sequence C
description BINDING => ECO:0000269|PubMed:9651245, ECO:0007744|PDB:1BE3, ECO:0007744|PDB:1BGY
source Swiss-Prot : SWS_FT_FI4

105) chain E
residue 161
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:9651245, ECO:0007744|PDB:1BE3, ECO:0007744|PDB:1BGY
source Swiss-Prot : SWS_FT_FI4

106) chain E
residue 163
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:9651245, ECO:0007744|PDB:1BE3, ECO:0007744|PDB:1BGY
source Swiss-Prot : SWS_FT_FI4

107) chain C
residue 202
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:21575592, ECO:0000269|PubMed:22690928, ECO:0000269|PubMed:9565029, ECO:0007744|PDB:1BCC, ECO:0007744|PDB:3CWB, ECO:0007744|PDB:3H1K, ECO:0007744|PDB:3L72
source Swiss-Prot : SWS_FT_FI5


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