|
eF-site ID
|
1kb9-E |
PDB Code
|
1kb9 |
Chain
|
E |
|
click to enlarge
|
|
Title
|
YEAST CYTOCHROME BC1 COMPLEX |
Classification
|
OXIDOREDUCTASE/ELECTRON TRANSPORT |
Compound
|
UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN I |
Source
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (1KB9) |
|
Sequence
|
E: |
KSTYRTPNFDDVLKENNDADKGRSYAYFMVGAMGLLSSAG
AKSTVETFISSMTATADVLAMAKVEVNLAAIPLGKNVVVK
WQGKPVFIRHRTPHEIQEANSVDMSALKDPQTDADRVKDP
QWLIMLGICTHLGCVPIGEAGDFGGWFCPCHGSHYDISGR
IRKGPAPLNLEIPAYEFDGDKVIVG
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|
Description
|
(1) |
UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN I, UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN 2, CYTOCHROME B, CYTOCHROME C1, HEME PROTEIN, UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT, UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 17 KD PROTEIN, UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 14 KD PROTEIN, UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX UBIQUINONE-BINDING PROTEIN QP-C, UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 7.3 KD PROTEIN, HEAVY CHAIN (VH) OF FV-FRAGMENT, LIGHT CHAIN (VL) OF FV-FRAGMENT, PROTOPORPHYRIN IX CONTAINING FE, FE2/S2 (INORGANIC) CLUSTER, ESTRIOL 3-(B-D-GLUCURONIDE), 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL, 2-[(HYDROXY{[(2R,3R,5S,6R)-2,3,4,5,6-PENTAHYDROXYCYCLOHEXYL]OXY}PHOSPHORYL)OXY]-1-[(PALMITOYLOXY)METHYL]ETHYL HEPTADECANOATE, 5-AMINO-6-CYCLOHEXYL-4-HYDROXY-2-ISOBUTYL-HEXANOIC ACID, 9-(4-HYDROXY-3-(HYDROXYMETHYL)BUT-1-YL)GUANINE, 5-OXOPROLINE, 2'-DEOXYURIDINE 5'-MONOPHOSPHATE
|
|
Functional site
|
|
1)
|
chain |
E |
residue |
159 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE FES E 504
|
source |
: AC4
|
|
2)
|
chain |
E |
residue |
161 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE FES E 504
|
source |
: AC4
|
|
3)
|
chain |
E |
residue |
162 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE FES E 504
|
source |
: AC4
|
|
4)
|
chain |
E |
residue |
178 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE FES E 504
|
source |
: AC4
|
|
5)
|
chain |
E |
residue |
181 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE FES E 504
|
source |
: AC4
|
|
6)
|
chain |
E |
residue |
183 |
type |
|
sequence |
S
|
description |
BINDING SITE FOR RESIDUE FES E 504
|
source |
: AC4
|
|
7)
|
chain |
E |
residue |
181 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE SMA C 505
|
source |
: AC5
|
|
8)
|
chain |
E |
residue |
70 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE PIE C 508
|
source |
: AC7
|
|
9)
|
chain |
E |
residue |
73 |
type |
|
sequence |
S
|
description |
BINDING SITE FOR RESIDUE PIE C 508
|
source |
: AC7
|
|
10)
|
chain |
E |
residue |
76 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE PIE C 508
|
source |
: AC7
|
|
11)
|
chain |
E |
residue |
80 |
type |
|
sequence |
S
|
description |
BINDING SITE FOR RESIDUE PIE C 508
|
source |
: AC7
|
|
12)
|
chain |
E |
residue |
60 |
type |
|
sequence |
V
|
description |
BINDING SITE FOR RESIDUE PCF A 514
|
source |
: BC2
|
|
13)
|
chain |
E |
residue |
67 |
type |
|
sequence |
S
|
description |
BINDING SITE FOR RESIDUE PCF A 514
|
source |
: BC2
|
|
14)
|
chain |
E |
residue |
57 |
type |
|
sequence |
Y
|
description |
BINDING SITE FOR RESIDUE UMQ A 521
|
source |
: BC3
|
|
15)
|
chain |
E |
residue |
60 |
type |
|
sequence |
V
|
description |
BINDING SITE FOR RESIDUE UMQ A 521
|
source |
: BC3
|
|
16)
|
chain |
E |
residue |
68 |
type |
|
sequence |
S
|
description |
BINDING SITE FOR RESIDUE UMQ A 521
|
source |
: BC3
|
|
17)
|
chain |
E |
residue |
181 |
type |
catalytic |
sequence |
H
|
description |
208
|
source |
MCSA : MCSA1
|
|
18)
|
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
|
|
19)
|
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
|
|
20)
|
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
|
|
21)
|
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
|
|
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