eF-site ID 2ibz-C
PDB Code 2ibz
Chain C

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Title Yeast Cytochrome BC1 Complex with Stigmatellin
Classification OXIDOREDUCTASE
Compound Ubiquinol-cytochrome-c reductase complex core protein 1
Source ORGANISM_COMMON: baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae;
Sequence C:  MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCL
VIQIVTGIFMAMHYSSNIELAFSSVEHIMRDVHNGYILRY
LHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVII
FTLTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGND
IVSWLWGGFSVSNPTIQRFFALHYLVPFIIAAMVIMHLMA
LHIHGSSNPLGITGNLDRIPMHSYFIFKDLVTVFLFMLIL
ALFVFYSPNTLGHPDNYIPGNPLVTPASIVPEWYLLPFYA
ILRSIPDKLLGVITMFAAILVLLVLPFTDRSVVRGNTFKV
LSKFFFFIFVFNFVLLGQIGACHVEVPYVLMGQIATFIYF
AYFLIIVPVISTIENVLFYIGRVNK
Description (1)  Ubiquinol-cytochrome-c reductase complex core protein 1, mitochondrial precursor (E.C.1.10.2.2 ), Ubiquinol-cytochrome-c reductase complex core protein 2, mitochondrial precursor (E.C.1.10.2.2 ), Cytochrome b (E.C.1.10.2.2 ), Cytochrome c1, heme protein, mitochondrial precursor (E.C.1.10.2.2 ), Ubiquinol-cytochrome c reductase iron-sulfur subunit, mitochondrial precursor (E.C.1.10.2.2), Ubiquinol-cytochrome c reductase complex 17 kDa protein (E.C.1.10.2.2 ), Ubiquinol-cytochrome c reductase complex 14 kDa protein (E.C.1.10.2.2 ), Ubiquinol-cytochrome c reductase complex ubiquinone-binding protein QP-C (E.C.1.10.2.2 ), Ubiquinol-cytochrome c reductase complex 7.3 kDa protein (E.C.1.10.2.2 ), VH chain of antibody fragment, VL chain of antibody fragment


Functional site

1) chain C
residue 40
type
sequence L
description BINDING SITE FOR RESIDUE HEC C 401
source : AC1

2) chain C
residue 43
type
sequence Q
description BINDING SITE FOR RESIDUE HEC C 401
source : AC1

3) chain C
residue 47
type
sequence G
description BINDING SITE FOR RESIDUE HEC C 401
source : AC1

4) chain C
residue 48
type
sequence I
description BINDING SITE FOR RESIDUE HEC C 401
source : AC1

5) chain C
residue 50
type
sequence M
description BINDING SITE FOR RESIDUE HEC C 401
source : AC1

6) chain C
residue 51
type
sequence A
description BINDING SITE FOR RESIDUE HEC C 401
source : AC1

7) chain C
residue 79
type
sequence R
description BINDING SITE FOR RESIDUE HEC C 401
source : AC1

8) chain C
residue 82
type
sequence H
description BINDING SITE FOR RESIDUE HEC C 401
source : AC1

9) chain C
residue 89
type
sequence F
description BINDING SITE FOR RESIDUE HEC C 401
source : AC1

10) chain C
residue 127
type
sequence T
description BINDING SITE FOR RESIDUE HEC C 401
source : AC1

11) chain C
residue 128
type
sequence A
description BINDING SITE FOR RESIDUE HEC C 401
source : AC1

12) chain C
residue 131
type
sequence G
description BINDING SITE FOR RESIDUE HEC C 401
source : AC1

13) chain C
residue 135
type
sequence V
description BINDING SITE FOR RESIDUE HEC C 401
source : AC1

14) chain C
residue 183
type
sequence H
description BINDING SITE FOR RESIDUE HEC C 401
source : AC1

15) chain C
residue 184
type
sequence Y
description BINDING SITE FOR RESIDUE HEC C 401
source : AC1

16) chain C
residue 187
type
sequence P
description BINDING SITE FOR RESIDUE HEC C 401
source : AC1

17) chain C
residue 30
type
sequence W
description BINDING SITE FOR RESIDUE HEC C 402
source : AC2

18) chain C
residue 33
type
sequence G
description BINDING SITE FOR RESIDUE HEC C 402
source : AC2

19) chain C
residue 36
type
sequence L
description BINDING SITE FOR RESIDUE HEC C 402
source : AC2

20) chain C
residue 96
type
sequence H
description BINDING SITE FOR RESIDUE HEC C 402
source : AC2

21) chain C
residue 99
type
sequence K
description BINDING SITE FOR RESIDUE HEC C 402
source : AC2

22) chain C
residue 105
type
sequence S
description BINDING SITE FOR RESIDUE HEC C 402
source : AC2

23) chain C
residue 113
type
sequence L
description BINDING SITE FOR RESIDUE HEC C 402
source : AC2

24) chain C
residue 114
type
sequence W
description BINDING SITE FOR RESIDUE HEC C 402
source : AC2

25) chain C
residue 117
type
sequence G
description BINDING SITE FOR RESIDUE HEC C 402
source : AC2

26) chain C
residue 118
type
sequence V
description BINDING SITE FOR RESIDUE HEC C 402
source : AC2

27) chain C
residue 120
type
sequence I
description BINDING SITE FOR RESIDUE HEC C 402
source : AC2

28) chain C
residue 197
type
sequence H
description BINDING SITE FOR RESIDUE HEC C 402
source : AC2

29) chain C
residue 201
type
sequence L
description BINDING SITE FOR RESIDUE HEC C 402
source : AC2

30) chain C
residue 206
type
sequence S
description BINDING SITE FOR RESIDUE HEC C 402
source : AC2

31) chain C
residue 207
type
sequence S
description BINDING SITE FOR RESIDUE HEC C 402
source : AC2

32) chain C
residue 16
type
sequence Y
description BINDING SITE FOR RESIDUE UQ6 C 506
source : AC5

33) chain C
residue 22
type
sequence Q
description BINDING SITE FOR RESIDUE UQ6 C 506
source : AC5

34) chain C
residue 44
type
sequence I
description BINDING SITE FOR RESIDUE UQ6 C 506
source : AC5

35) chain C
residue 185
type
sequence L
description BINDING SITE FOR RESIDUE UQ6 C 506
source : AC5

36) chain C
residue 201
type
sequence L
description BINDING SITE FOR RESIDUE UQ6 C 506
source : AC5

37) chain C
residue 206
type
sequence S
description BINDING SITE FOR RESIDUE UQ6 C 506
source : AC5

38) chain C
residue 221
type
sequence M
description BINDING SITE FOR RESIDUE UQ6 C 506
source : AC5

39) chain C
residue 229
type
sequence D
description BINDING SITE FOR RESIDUE UQ6 C 506
source : AC5

40) chain C
residue 125
type
sequence I
description BINDING SITE FOR RESIDUE SMA C 505
source : AC6

41) chain C
residue 146
type
sequence V
description BINDING SITE FOR RESIDUE SMA C 505
source : AC6

42) chain C
residue 271
type
sequence P
description BINDING SITE FOR RESIDUE SMA C 505
source : AC6

43) chain C
residue 272
type
sequence E
description BINDING SITE FOR RESIDUE SMA C 505
source : AC6

44) chain C
residue 275
type
sequence L
description BINDING SITE FOR RESIDUE SMA C 505
source : AC6

45) chain C
residue 279
type
sequence Y
description BINDING SITE FOR RESIDUE SMA C 505
source : AC6

46) chain C
residue 295
type
sequence M
description BINDING SITE FOR RESIDUE SMA C 505
source : AC6

47) chain C
residue 296
type
sequence F
description BINDING SITE FOR RESIDUE SMA C 505
source : AC6

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

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

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

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

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

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

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

55) chain C
residue 103-110
type TOPO_DOM
sequence YGSYRSPR
description Mitochondrial matrix => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554
source Swiss-Prot : SWS_FT_FI1

56) chain C
residue 205-223
type TOPO_DOM
sequence GSSNPLGITGNLDRIPMHS
description Mitochondrial matrix => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554
source Swiss-Prot : SWS_FT_FI1

57) chain C
residue 309-319
type TOPO_DOM
sequence DRSVVRGNTFK
description Mitochondrial matrix => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554
source Swiss-Prot : SWS_FT_FI1

58) chain C
residue 365-385
type TOPO_DOM
sequence IIVPVISTIENVLFYIGRVNK
description Mitochondrial matrix => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554
source Swiss-Prot : SWS_FT_FI1

59) 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

60) 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

61) 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

62) 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

63) 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

64) 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

65) 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

66) chain C
residue 136-172
type TOPO_DOM
sequence YGQMSHWGATVITNLFSAIPFVGNDIVSWLWGGFSVS
description Mitochondrial intermembrane => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554
source Swiss-Prot : SWS_FT_FI3

67) 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

68) 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


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