|
|
1)
|
chain |
A |
residue |
2 |
type |
|
sequence |
T
|
description |
BINDING SITE FOR RESIDUE CA A 746
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
3 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE CA A 746
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
388 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE CA A 746
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
189 |
type |
catalytic |
sequence |
S
|
description |
900
|
source |
MCSA : MCSA1
|
|
5)
|
chain |
A |
residue |
310 |
type |
catalytic |
sequence |
E
|
description |
900
|
source |
MCSA : MCSA1
|
|
6)
|
chain |
A |
residue |
399 |
type |
catalytic |
sequence |
H
|
description |
900
|
source |
MCSA : MCSA1
|
|
7)
|
chain |
A |
residue |
176-191 |
type |
prosite |
sequence |
FGGDPDNVTVFGESAG
|
description |
CARBOXYLESTERASE_B_1 Carboxylesterases type-B serine active site. FGGdpdnVtVfGeSAG
|
source |
prosite : PS00122
|
|
8)
|
chain |
A |
residue |
80-90 |
type |
prosite |
sequence |
EDCLYVNVFAP
|
description |
CARBOXYLESTERASE_B_2 Carboxylesterases type-B signature 2. EDCLYVNVFaP
|
source |
prosite : PS00941
|
|
9)
|
chain |
A |
residue |
189 |
type |
ACT_SITE |
sequence |
S
|
description |
Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10039
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
10)
|
chain |
A |
residue |
310 |
type |
ACT_SITE |
sequence |
E
|
description |
Charge relay system => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
11)
|
chain |
A |
residue |
399 |
type |
ACT_SITE |
sequence |
H
|
description |
Charge relay system => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
12)
|
chain |
A |
residue |
189 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0000269|PubMed:17218307
|
source |
Swiss-Prot : SWS_FT_FI3
|
|