eF-site ID 1p84-C
PDB Code 1p84
Chain C

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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 C:  MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCL
VIQIVTGIFMAMHYSSNIELAFSSVEHIMRDVHNGYILRY
LHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVII
FTLTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGND
IVSWLWGGFSVSNPTIQRFFALHYLVPFIIAAMVIMHLMA
LHIHGSSNPLGITGNLDRIPMHSYFIFKDLVTVFLFMLIL
ALFVFYSPNTLGHPDNYIPGNPLVTPASIVPEWYLLPFYA
ILRSIPDKLLGVITMFAAILVLLVLPFTDRSVVRGNTFKV
LSKFFFFIFVFNFVLLGQIGACHVEVPYVLMGQIATFIYF
AYFLIIVPVISTIENVLFYIGRVNK
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 C
residue 139
type
sequence M
description BINDING SITE FOR RESIDUE DBT C 705
source : AC5
31) chain C
residue 143
type
sequence G
description BINDING SITE FOR RESIDUE DBT C 705
source : AC5
32) chain C
residue 146
type
sequence V
description BINDING SITE FOR RESIDUE DBT C 705
source : AC5
33) chain C
residue 147
type
sequence I
description BINDING SITE FOR RESIDUE DBT C 705
source : AC5
34) chain C
residue 269
type
sequence I
description BINDING SITE FOR RESIDUE DBT C 705
source : AC5
35) chain C
residue 271
type
sequence P
description BINDING SITE FOR RESIDUE DBT C 705
source : AC5
36) chain C
residue 279
type
sequence Y
description BINDING SITE FOR RESIDUE DBT C 705
source : AC5
37) chain C
residue 16
type
sequence Y
description BINDING SITE FOR RESIDUE UQ6 C 706
source : AC6
38) chain C
residue 22
type
sequence Q
description BINDING SITE FOR RESIDUE UQ6 C 706
source : AC6
39) chain C
residue 26
type
sequence I
description BINDING SITE FOR RESIDUE UQ6 C 706
source : AC6
40) chain C
residue 34
type
sequence S
description BINDING SITE FOR RESIDUE UQ6 C 706
source : AC6
41) chain C
residue 44
type
sequence I
description BINDING SITE FOR RESIDUE UQ6 C 706
source : AC6
42) chain C
residue 201
type
sequence L
description BINDING SITE FOR RESIDUE UQ6 C 706
source : AC6
43) chain C
residue 206
type
sequence S
description BINDING SITE FOR RESIDUE UQ6 C 706
source : AC6
44) chain C
residue 221
type
sequence M
description BINDING SITE FOR RESIDUE UQ6 C 706
source : AC6
45) chain C
residue 229
type
sequence D
description BINDING SITE FOR RESIDUE UQ6 C 706
source : AC6
46) chain C
residue 29
type
sequence W
description BINDING SITE FOR RESIDUE 3PE C 710
source : AC7
47) chain C
residue 97
type
sequence M
description BINDING SITE FOR RESIDUE 3PE C 710
source : AC7
48) chain C
residue 102
type
sequence Y
description BINDING SITE FOR RESIDUE 3PE C 710
source : AC7
49) chain C
residue 103
type
sequence Y
description BINDING SITE FOR RESIDUE 3PE C 710
source : AC7
50) chain C
residue 359
type
sequence Y
description BINDING SITE FOR RESIDUE 3PE C 710
source : AC7
51) chain C
residue 3
type
sequence F
description BINDING SITE FOR RESIDUE 3PE C 711
source : AC8
52) chain C
residue 7
type
sequence N
description BINDING SITE FOR RESIDUE 3PE C 711
source : AC8
53) chain C
residue 9
type
sequence Y
description BINDING SITE FOR RESIDUE 3PE C 711
source : AC8
54) chain C
residue 13
type
sequence V
description BINDING SITE FOR RESIDUE 3PE C 711
source : AC8
55) chain C
residue 112
type
sequence T
description BINDING SITE FOR RESIDUE 3PE C 711
source : AC8
56) chain C
residue 115
type
sequence N
description BINDING SITE FOR RESIDUE 3PE C 711
source : AC8
57) chain C
residue 230
type
sequence L
description BINDING SITE FOR RESIDUE 3PH A 713
source : AC9
58) chain C
residue 237
type
sequence M
description BINDING SITE FOR RESIDUE 3PH D 714
source : BC1
59) chain C
residue 253
type
sequence H
description BINDING SITE FOR RESIDUE PC1 D 715
source : BC2
60) chain C
residue 268
type
sequence S
description BINDING SITE FOR RESIDUE PC1 D 715
source : BC2
61) chain C
residue 273
type
sequence W
description BINDING SITE FOR RESIDUE PC1 D 715
source : BC2
62) chain C
residue 337
type
sequence G
description BINDING SITE FOR RESIDUE PC1 D 715
source : BC2
63) chain C
residue 27
type
sequence N
description BINDING SITE FOR RESIDUE CDL D 731
source : BC4
64) chain C
residue 28
type
sequence Y
description BINDING SITE FOR RESIDUE CDL D 731
source : BC4
65) chain C
residue 32
type
sequence M
description BINDING SITE FOR RESIDUE CDL D 731
source : BC4
66) chain C
residue 95
type
sequence M
description BINDING SITE FOR RESIDUE CDL D 731
source : BC4
67) chain C
residue 235
type
sequence L
description BINDING SITE FOR RESIDUE CDL D 731
source : BC4
68) chain C
residue 206
type catalytic
sequence S
description 208
source MCSA : MCSA1
69) chain C
residue 228
type catalytic
sequence K
description 208
source MCSA : MCSA1
70) chain C
residue 229
type catalytic
sequence D
description 208
source MCSA : MCSA1
71) chain C
residue 272
type catalytic
sequence E
description 208
source MCSA : MCSA1
72) 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
73) 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
74) 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
75) 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
76) 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
77) 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
78) 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
79) 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
80) 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
81) 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
82) 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
83) 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
84) 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
85) chain C
residue 202
type BINDING
sequence H
description BINDING => ECO:0000250|UniProtKB:P00157
source Swiss-Prot : SWS_FT_FI6
86) 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
87) 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
88) 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

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