|
|
eF-site ID
|
1a2o-A |
|
PDB Code
|
1a2o |
|
Chain
|
A |
|
click to enlarge
|
|
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Title
|
STRUCTURAL BASIS FOR METHYLESTERASE CHEB REGULATION BY A PHOSPHORYLATION-ACTIVATED DOMAIN |
|
Classification
|
BACTERIAL CHEMOTAXIS |
|
Compound
|
CHEB METHYLESTERASE |
|
Source
|
Salmonella typhimurium (CHEB_SALTY) |
|
|
Sequence
|
A: |
MSKIRVLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLV
ARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVV
MVSSLTGKGSEVTLRALELGAIDFVTKPQLGIREGMLAYS
EMIAEKVRTAARARIAAHKPMAAPTTLKAGPLLSSEKLIA
IGASTGGTEAIRHVLQPLPLSSPAVIITQHMPPGFTRSFA
ERLNKLCQISVKEAEDGERVLPGHAYIAPGDKHMELARSG
ANYQIKIHDGPPVNRHRPSVDVLFHSVAKHAGRNAVGVIL
TGMGNDGAAGMLAMYQAGAWTIAQNEASCVVFGMPREAIN
MGGVSEVVDLSQVSQQMLAKISAGQAI
|
|
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Description
|
|
Functional site
|
|
|
1)
|
chain |
A |
| residue |
56 |
| type |
|
| sequence |
D
|
| description |
PHOSPHORYLATION SITE
|
| source |
: PON
|
|
|
2)
|
chain |
A |
| residue |
164 |
| type |
|
| sequence |
S
|
| description |
ESTERASE CATALYTIC TRIAD
|
| source |
: ESE
|
|
|
3)
|
chain |
A |
| residue |
190 |
| type |
|
| sequence |
H
|
| description |
ESTERASE CATALYTIC TRIAD
|
| source |
: ESE
|
|
|
4)
|
chain |
A |
| residue |
286 |
| type |
|
| sequence |
D
|
| description |
ESTERASE CATALYTIC TRIAD
|
| source |
: ESE
|
|
|
5)
|
chain |
A |
| residue |
164 |
| type |
catalytic |
| sequence |
S
|
| description |
337
|
| source |
MCSA : MCSA1
|
|
|
6)
|
chain |
A |
| residue |
165 |
| type |
catalytic |
| sequence |
T
|
| description |
337
|
| source |
MCSA : MCSA1
|
|
|
7)
|
chain |
A |
| residue |
190 |
| type |
catalytic |
| sequence |
H
|
| description |
337
|
| source |
MCSA : MCSA1
|
|
|
8)
|
chain |
A |
| residue |
283 |
| type |
catalytic |
| sequence |
M
|
| description |
337
|
| source |
MCSA : MCSA1
|
|
|
9)
|
chain |
A |
| residue |
286 |
| type |
catalytic |
| sequence |
D
|
| description |
337
|
| source |
MCSA : MCSA1
|
|
|
10)
|
chain |
A |
| residue |
164 |
| type |
ACT_SITE |
| sequence |
S
|
| description |
ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00099, ECO:0000305|PubMed:7608974
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
11)
|
chain |
A |
| residue |
190 |
| type |
ACT_SITE |
| sequence |
H
|
| description |
ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00099, ECO:0000305|PubMed:7608974
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
12)
|
chain |
A |
| residue |
286 |
| type |
ACT_SITE |
| sequence |
D
|
| description |
ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00099, ECO:0000305|PubMed:7608974
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
13)
|
chain |
A |
| residue |
56 |
| type |
MOD_RES |
| sequence |
D
|
| description |
4-aspartylphosphate => ECO:0000255|HAMAP-Rule:MF_00099, ECO:0000269|PubMed:9465023
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
|