|
|
1)
|
chain |
D |
residue |
162 |
type |
|
sequence |
K
|
description |
LYSINE WITHIN THE P-LOOP (PHOSPHATE BINDING) MOTIF, GXXXXGKT/S.
|
source |
: PLP
|
|
2)
|
chain |
D |
residue |
188 |
type |
|
sequence |
E
|
description |
THE CARBOXYLATE GROUP OF THE GLUTAMIC ACID RESIDUE IS BELIEVED TO ACTIVATE A WATER MOLECULE FOR INLINE ATTACK ON THE GAMMA PHOSPHATE DURING ATP HYDROLYSIS. THE ARGININE RESIDUE (WHICH IS LOCATED ON AN ADJACENT ALPHA SUBUNIT) COULD HELP TO STABLIZE THE NEGATIVE CHARGE THAT DEVELOPS ON THE TERMINAL PHOSPHATE IN THE PUTATIVE PENTACOORDINATED TRANSITION STATE.
|
source |
: CAT
|
|
3)
|
chain |
D |
residue |
163 |
type |
|
sequence |
T
|
description |
BINDING SITE FOR RESIDUE MG D 601
|
source |
: AC4
|
|
4)
|
chain |
D |
residue |
159 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE ADP D 600
|
source |
: AC9
|
|
5)
|
chain |
D |
residue |
160 |
type |
|
sequence |
V
|
description |
BINDING SITE FOR RESIDUE ADP D 600
|
source |
: AC9
|
|
6)
|
chain |
D |
residue |
161 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE ADP D 600
|
source |
: AC9
|
|
7)
|
chain |
D |
residue |
162 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE ADP D 600
|
source |
: AC9
|
|
8)
|
chain |
D |
residue |
163 |
type |
|
sequence |
T
|
description |
BINDING SITE FOR RESIDUE ADP D 600
|
source |
: AC9
|
|
9)
|
chain |
D |
residue |
164 |
type |
|
sequence |
V
|
description |
BINDING SITE FOR RESIDUE ADP D 600
|
source |
: AC9
|
|
10)
|
chain |
D |
residue |
345 |
type |
|
sequence |
Y
|
description |
BINDING SITE FOR RESIDUE ADP D 600
|
source |
: AC9
|
|
11)
|
chain |
D |
residue |
418 |
type |
|
sequence |
F
|
description |
BINDING SITE FOR RESIDUE ADP D 600
|
source |
: AC9
|
|
12)
|
chain |
D |
residue |
424 |
type |
|
sequence |
F
|
description |
BINDING SITE FOR RESIDUE ADP D 600
|
source |
: AC9
|
|
13)
|
chain |
D |
residue |
425 |
type |
|
sequence |
T
|
description |
BINDING SITE FOR RESIDUE ADP D 600
|
source |
: AC9
|
|
14)
|
chain |
D |
residue |
162 |
type |
catalytic |
sequence |
K
|
description |
178
|
source |
MCSA : MCSA1
|
|
15)
|
chain |
D |
residue |
188 |
type |
catalytic |
sequence |
E
|
description |
178
|
source |
MCSA : MCSA1
|
|
16)
|
chain |
D |
residue |
189 |
type |
catalytic |
sequence |
R
|
description |
178
|
source |
MCSA : MCSA1
|
|
17)
|
chain |
D |
residue |
209 |
type |
MOD_RES |
sequence |
K
|
description |
N6-acetyllysine => ECO:0000250|UniProtKB:P36542
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
18)
|
chain |
D |
residue |
214 |
type |
MOD_RES |
sequence |
K
|
description |
N6-acetyllysine => ECO:0000250|UniProtKB:P36542
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
19)
|
chain |
D |
residue |
472 |
type |
MOD_RES |
sequence |
K
|
description |
N6-acetyllysine => ECO:0000250|UniProtKB:P36542
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
20)
|
chain |
D |
residue |
365 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0000250|UniProtKB:P06576
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
21)
|
chain |
D |
residue |
383 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0000250|UniProtKB:P10719
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
22)
|
chain |
D |
residue |
430 |
type |
MOD_RES |
sequence |
K
|
description |
N6-acetyllysine => ECO:0000250|UniProtKB:P56480
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
23)
|
chain |
D |
residue |
435 |
type |
MOD_RES |
sequence |
K
|
description |
N6-acetyllysine => ECO:0000250|UniProtKB:P56480
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
24)
|
chain |
D |
residue |
56 |
type |
CARBOHYD |
sequence |
S
|
description |
O-linked (GlcNAc) serine => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI9
|
|
25)
|
chain |
D |
residue |
346-355 |
type |
prosite |
sequence |
PAVDPLDSTS
|
description |
ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAINVGLSVS
|
source |
prosite : PS00152
|
|