eF-site ID 1a2o-AB
PDB Code 1a2o
Chain A, B

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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
B:  MSKIRVLSVDDSALMRQIMTEIINSHSDMEMVATAPDPLV
ARDLIKKFNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVV
MVSSLTGKGSEVTLRALELGAIDFVTKPQLGIREGMLAYS
EMIAEKVRTAARARIAAHKPMAAPTTLKAGPLLSSEKLIA
IGASTGGTEAIRHVLQPLPLSSPAVIITQHMPPGFTRSFA
ERLNKLCQISVKEAEDGERVLPGHAYIAPGDKHMELARSG
ANYQIKIHDGPPVNRHRPSVDVLFHSVAKHAGRNAVGVIL
TGMGNDGAAGMLAMYQAGAWTIAQNEASCVVFGMPREAIN
MGGVSEVVDLSQVSQQMLAKISAGQAI
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 B
residue 164
type catalytic
sequence S
description 337
source MCSA : MCSA2

11) chain B
residue 165
type catalytic
sequence T
description 337
source MCSA : MCSA2

12) chain B
residue 190
type catalytic
sequence H
description 337
source MCSA : MCSA2

13) chain B
residue 283
type catalytic
sequence M
description 337
source MCSA : MCSA2

14) chain B
residue 286
type catalytic
sequence D
description 337
source MCSA : MCSA2

15) 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

16) 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

17) 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

18) chain B
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

19) chain B
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

20) chain B
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

21) 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

22) chain B
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


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