eF-site ID 5efz-F PDB Code 5efz Chain F click to enlarge Title Monoclinic structure of the acetyl esterase MekB Classification HYDROLASE Compound Homoserine O-acetyltransferase Source (Q0MRG5_9PSED) Sequence F:  SYYTEENHGPFELINIGPLPLEEGRCMPECLLAVAVHGAL NADKSNAILVPTWYSGTSKAMEQIYIGEGRALDPSKYCII VVNQIGNGLSSSASNTGGSLAGPGFANVRIGDDVSAQHTL LTEYFGIESLALVVGGSMGAQQTYEWAVRYPDFVKRAAAI AGTARNSEHDFLFTEILIEAITTDPAFQAGLYRSSSAVAA GLERHAKLWTLMGWSPEFFRTGRHKALGFESMQMFVDGFM KRYFAPMDPNNLLTMAWKWQRGDVSRHTGGDLAKALGRIK AKTYVMPISHDQFFTVDDCLSEQKMIPNSEFRPLRSIDGH LGLFGTDAQMLDQLDAHLAELLSSPAY Description (1)  Homoserine O-acetyltransferase (E.C.2.3.1.-,2.3.1.31) Functional site 1) chain F residue 45 type sequence D description binding site for residue EDO A 403 source : AC3 2) chain F residue 294 type sequence Q description binding site for residue EDO C 401 source : AD7 3) chain F residue 312 type sequence E description binding site for residue EDO C 404 source : AE1 4) chain F residue 291 type sequence S description binding site for residue EDO C 406 source : AE3 5) chain F residue 293 type sequence D description binding site for residue EDO C 406 source : AE3 6) chain F residue 218 type sequence P description binding site for residue EDO D 401 source : AE7 7) chain F residue 222 type sequence R description binding site for residue EDO D 401 source : AE7 8) chain F residue 222 type sequence R description binding site for residue EDO D 402 source : AE8 9) chain F residue 299 type sequence D description binding site for residue EDO D 403 source : AE9 10) chain F residue 178 type sequence I description binding site for residue GOL D 405 source : AF2 11) chain F residue 182 type sequence A description binding site for residue GOL D 405 source : AF2 12) chain F residue 167 type sequence R description binding site for residue EDO F 401 source : AF8 13) chain F residue 272 type sequence G description binding site for residue EDO F 401 source : AF8 14) chain F residue 273 type sequence D description binding site for residue EDO F 401 source : AF8 15) chain F residue 274 type sequence L description binding site for residue EDO F 401 source : AF8 16) chain F residue 275 type sequence A description binding site for residue EDO F 401 source : AF8 17) chain F residue 177 type sequence E description binding site for residue EDO F 402 source : AF9 18) chain F residue 167 type sequence R description binding site for residue GOL F 403 source : AG1 19) chain F residue 169 type sequence S description binding site for residue GOL F 403 source : AG1 20) chain F residue 274 type sequence L description binding site for residue GOL F 403 source : AG1 21) chain F residue 300 type sequence D description binding site for residue GOL F 403 source : AG1 22) chain F residue 303 type sequence S description binding site for residue GOL F 403 source : AG1 23) chain F residue 304 type sequence E description binding site for residue GOL F 403 source : AG1 24) chain F residue 43 type sequence N description binding site for residue GOL F 404 source : AG2 25) chain F residue 45 type sequence D description binding site for residue GOL F 404 source : AG2 26) chain F residue 47 type sequence S description binding site for residue GOL F 404 source : AG2 27) chain F residue 55 type sequence W description binding site for residue ACT F 406 source : AG4 28) chain F residue 56 type sequence Y description binding site for residue ACT F 406 source : AG4 29) chain F residue 139 type sequence S description binding site for residue ACT F 406 source : AG4 30) chain F residue 140 type sequence M description binding site for residue ACT F 406 source : AG4 31) chain F residue 322 type sequence H description binding site for residue ACT F 406 source : AG4 32) chain F residue 139 type ACT_SITE sequence S description Nucleophile => ECO:0000305|PubMed:26787467 source Swiss-Prot : SWS_FT_FI1 33) chain F residue 293 type ACT_SITE sequence D description ACT_SITE => ECO:0000305|PubMed:26787467 source Swiss-Prot : SWS_FT_FI2 34) chain F residue 322 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:26787467 source Swiss-Prot : SWS_FT_FI2

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