|
|
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 |
103-110 |
type |
TOPO_DOM |
sequence |
YGSYRSPR
|
description |
Mitochondrial matrix => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
53)
|
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
|
|
54)
|
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
|
|
55)
|
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
|
|
56)
|
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
|
|
57)
|
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
|
|
58)
|
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
|
|
59)
|
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
|
|
60)
|
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
|
|
61)
|
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
|
|
62)
|
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
|
|
63)
|
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
|
|
64)
|
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
|
|
65)
|
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
|
|
66)
|
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
|
|
67)
|
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
|
|
68)
|
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
|
|