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