eF-site ID 5efz-ABCDEF PDB Code 5efz Chain A, B, C, D, E, F click to enlarge Title Monoclinic structure of the acetyl esterase MekB Classification HYDROLASE Compound Homoserine O-acetyltransferase Source (Q0MRG5_9PSED) Sequence A:  SYYTEENHGPFELINIGPLPLEEGRCMPECLLAVAVHGAL NADKSNAILVPTWYSGTSKAMEQIYIGEGRALDPSKYCII VVNQIGNGLSSSASNTGGSLAGPGFANVRIGDDVSAQHTL LTEYFGIESLALVVGGSMGAQQTYEWAVRYPDFVKRAAAI AGTARNSEHDFLFTEILIEAITTDPAFQAGLYRSSSAVAA GLERHAKLWTLMGWSPEFFRTGRHKALGFESMQMFVDGFM KRYFAPMDPNNLLTMAWKWQRGDVSRHTGGDLAKALGRIK AKTYVMPISHDQFFTVDDCLSEQKMIPNSEFRPLRSIDGH LGLFGTDAQMLDQLDAHLAELLSSPAY B:  SYYTEENHGPFELINIGPLPLEEGRCMPECLLAVAVHGAL NADKSNAILVPTWYSGTSKAMEQIYIGEGRALDPSKYCII VVNQIGNGLSSSASNTGGSLAGPGFANVRIGDDVSAQHTL LTEYFGIESLALVVGGSMGAQQTYEWAVRYPDFVKRAAAI AGTARNSEHDFLFTEILIEAITTDPAFQAGLYRSSSAVAA GLERHAKLWTLMGWSPEFFRTGRHKALGFESMQMFVDGFM KRYFAPMDPNNLLTMAWKWQRGDVSRHTGGDLAKALGRIK AKTYVMPISHDQFFTVDDCLSEQKMIPNSEFRPLRSIDGH LGLFGTDAQMLDQLDAHLAELLSSP C:  HGPFELINIGPLPLEEGRCMPECLLAVAVHGALNADKSNA ILVPTWYSGTSKAMEQIYIGEGRALDPSKYCIIVVNQIGN GLSSSASNTGGSLAGPGFANVRIGDDVSAQHTLLTEYFGI ESLALVVGGSMGAQQTYEWAVRYPDFVKRAAAIAGTARNS EHDFLFTEILIEAITTDPAFQAGLYRSSSAVAAGLERHAK LWTLMGWSPEFFRTGRHKALGFESMQMFVDGFMKRYFAPM DPNNLLTMAWKWQRGDVSRHTGGDLAKALGRIKAKTYVMP ISHDQFFTVDDCLSEQKMIPNSEFRPLRSIDGHLGLFGTD AQMLDQLDAHLAELLSSPA D:  NSYYTEENHGPFELINIGPLPLEEGRCMPECLLAVAVHGA LNADKSNAILVPTWYSGTSKAMEQIYIGEGRALDPSKYCI IVVNQIGNGLSSSASNTGGSLAGPGFANVRIGDDVSAQHT LLTEYFGIESLALVVGGSMGAQQTYEWAVRYPDFVKRAAA IAGTARNSEHDFLFTEILIEAITTDPAFQAGLYRSSSAVA AGLERHAKLWTLMGWSPEFFRTGRHKALGFESMQMFVDGF MKRYFAPMDPNNLLTMAWKWQRGDVSRHTGGDLAKALGRI KAKTYVMPISHDQFFTVDDCLSEQKMIPNSEFRPLRSIDG HLGLFGTDAQMLDQLDAHLAELLSS E:  SYYTEENHGPFELINIGPLPLEEGRCMPECLLAVAVHGAL NADKSNAILVPTWYSGTSKAMEQIYIGEGRALDPSKYCII VVNQIGNGLSSSASNTGGSLAGPGFANVRIGDDVSAQHTL LTEYFGIESLALVVGGSMGAQQTYEWAVRYPDFVKRAAAI AGTARNSEHDFLFTEILIEAITTDPAFQAGLYRSSSAVAA GLERHAKLWTLMGWSPEFFRTGRHKALGFESMQMFVDGFM KRYFAPMDPNNLLTMAWKWQRGDVSRHTGGDLAKALGRIK AKTYVMPISHDQFFTVDDCLSEQKMIPNSEFRPLRSIDGH LGLFGTDAQMLDQLDAHLAELLSSP 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 A residue 5 type sequence Y description binding site for residue EDO A 401 source : AC1 2) chain A residue 90 type sequence G description binding site for residue EDO A 401 source : AC1 3) chain A residue 91 type sequence L description binding site for residue EDO A 401 source : AC1 4) chain A residue 97 type sequence N description binding site for residue EDO A 401 source : AC1 5) chain A residue 299 type sequence D description binding site for residue EDO A 402 source : AC2 6) chain A residue 306 type sequence K description binding site for residue EDO A 402 source : AC2 7) chain A residue 47 type sequence S description binding site for residue EDO A 403 source : AC3 8) chain A residue 158 type sequence R description binding site for residue EDO A 403 source : AC3 9) chain A residue 348 type sequence A description binding site for residue EDO A 403 source : AC3 10) chain F residue 45 type sequence D description binding site for residue EDO A 403 source : AC3 11) chain A residue 184 type sequence T description binding site for residue EDO A 404 source : AC4 12) chain A residue 185 type sequence T description binding site for residue EDO A 404 source : AC4 13) chain A residue 186 type sequence D description binding site for residue EDO A 404 source : AC4 14) chain A residue 187 type sequence P description binding site for residue EDO A 404 source : AC4 15) chain A residue 190 type sequence Q description binding site for residue EDO A 404 source : AC4 16) chain A residue 191 type sequence A description binding site for residue EDO A 404 source : AC4 17) chain A residue 167 type sequence R description binding site for residue EDO A 405 source : AC5 18) chain A residue 168 type sequence N description binding site for residue EDO A 405 source : AC5 19) chain A residue 262 type sequence Q description binding site for residue EDO A 405 source : AC5 20) chain A residue 104 type sequence G description binding site for residue EDO A 406 source : AC6 21) chain A residue 105 type sequence P description binding site for residue EDO A 406 source : AC6 22) chain A residue 107 type sequence F description binding site for residue EDO A 406 source : AC6 23) chain A residue 252 type sequence N description binding site for residue EDO A 406 source : AC6 24) chain A residue 256 type sequence T description binding site for residue EDO A 406 source : AC6 25) chain A residue 167 type sequence R description binding site for residue EDO A 407 source : AC7 26) chain A residue 169 type sequence S description binding site for residue EDO A 407 source : AC7 27) chain A residue 274 type sequence L description binding site for residue EDO A 407 source : AC7 28) chain A residue 304 type sequence E description binding site for residue EDO A 407 source : AC7 29) chain A residue 188 type sequence A description binding site for residue GOL A 408 source : AC8 30) chain A residue 195 type sequence R description binding site for residue GOL A 408 source : AC8 31) chain A residue 55 type sequence W description binding site for residue ACT A 409 source : AC9 32) chain A residue 56 type sequence Y description binding site for residue ACT A 409 source : AC9 33) chain A residue 139 type sequence S description binding site for residue ACT A 409 source : AC9 34) chain A residue 140 type sequence M description binding site for residue ACT A 409 source : AC9 35) chain A residue 322 type sequence H description binding site for residue ACT A 409 source : AC9 36) chain B residue 72 type sequence R description binding site for residue EDO B 401 source : AD1 37) chain B residue 334 type sequence D description binding site for residue EDO B 401 source : AD1 38) chain B residue 27 type sequence R description binding site for residue EDO B 402 source : AD2 39) chain B residue 101 type sequence S description binding site for residue EDO B 402 source : AD2 40) chain E residue 101 type sequence S description binding site for residue EDO B 402 source : AD2 41) chain B residue 46 type sequence K description binding site for residue EDO B 403 source : AD3 42) chain B residue 291 type sequence S description binding site for residue EDO B 404 source : AD4 43) chain B residue 263 type sequence R description binding site for residue EDO B 405 source : AD5 44) chain B residue 55 type sequence W description binding site for residue ACT B 406 source : AD6 45) chain B residue 56 type sequence Y description binding site for residue ACT B 406 source : AD6 46) chain B residue 139 type sequence S description binding site for residue ACT B 406 source : AD6 47) chain B residue 140 type sequence M description binding site for residue ACT B 406 source : AD6 48) chain B residue 322 type sequence H description binding site for residue ACT B 406 source : AD6 49) chain C residue 195 type sequence R description binding site for residue EDO C 401 source : AD7 50) chain D residue 294 type sequence Q description binding site for residue EDO C 401 source : AD7 51) chain F residue 294 type sequence Q description binding site for residue EDO C 401 source : AD7 52) chain C residue 167 type sequence R description binding site for residue EDO C 402 source : AD8 53) chain C residue 169 type sequence S description binding site for residue EDO C 402 source : AD8 54) chain C residue 274 type sequence L description binding site for residue EDO C 402 source : AD8 55) chain C residue 300 type sequence D description binding site for residue EDO C 402 source : AD8 56) chain C residue 304 type sequence E description binding site for residue EDO C 402 source : AD8 57) chain C residue 104 type sequence G description binding site for residue EDO C 403 source : AD9 58) chain C residue 105 type sequence P description binding site for residue EDO C 403 source : AD9 59) chain C residue 107 type sequence F description binding site for residue EDO C 403 source : AD9 60) chain C residue 252 type sequence N description binding site for residue EDO C 403 source : AD9 61) chain C residue 255 type sequence L description binding site for residue EDO C 403 source : AD9 62) chain C residue 256 type sequence T description binding site for residue EDO C 403 source : AD9 63) chain C residue 25 type sequence E description binding site for residue EDO C 404 source : AE1 64) chain C residue 27 type sequence R description binding site for residue EDO C 404 source : AE1 65) chain C residue 107 type sequence F description binding site for residue EDO C 404 source : AE1 66) chain C residue 109 type sequence N description binding site for residue EDO C 404 source : AE1 67) chain F residue 312 type sequence E description binding site for residue EDO C 404 source : AE1 68) chain C residue 299 type sequence D description binding site for residue EDO C 405 source : AE2 69) chain C residue 306 type sequence K description binding site for residue EDO C 405 source : AE2 70) chain E residue 222 type sequence R description binding site for residue EDO C 405 source : AE2 71) chain C residue 190 type sequence Q description binding site for residue EDO C 406 source : AE3 72) chain F residue 291 type sequence S description binding site for residue EDO C 406 source : AE3 73) chain F residue 293 type sequence D description binding site for residue EDO C 406 source : AE3 74) chain C residue 190 type sequence Q description binding site for residue GOL C 407 source : AE4 75) chain C residue 195 type sequence R description binding site for residue GOL C 407 source : AE4 76) chain D residue 291 type sequence S description binding site for residue GOL C 407 source : AE4 77) chain C residue 195 type sequence R description binding site for residue GOL C 408 source : AE5 78) chain C residue 196 type sequence S description binding site for residue GOL C 408 source : AE5 79) chain C residue 199 type sequence A description binding site for residue GOL C 408 source : AE5 80) chain D residue 298 type sequence V description binding site for residue GOL C 408 source : AE5 81) chain D residue 315 type sequence P description binding site for residue GOL C 408 source : AE5 82) chain C residue 55 type sequence W description binding site for residue ACT C 409 source : AE6 83) chain C residue 56 type sequence Y description binding site for residue ACT C 409 source : AE6 84) chain C residue 139 type sequence S description binding site for residue ACT C 409 source : AE6 85) chain C residue 140 type sequence M description binding site for residue ACT C 409 source : AE6 86) chain C residue 322 type sequence H description binding site for residue ACT C 409 source : AE6 87) chain D residue 169 type sequence S description binding site for residue EDO D 401 source : AE7 88) chain D residue 171 type sequence H description binding site for residue EDO D 401 source : AE7 89) chain D residue 295 type sequence F description binding site for residue EDO D 401 source : AE7 90) chain D residue 300 type sequence D description binding site for residue EDO D 401 source : AE7 91) chain F residue 218 type sequence P description binding site for residue EDO D 401 source : AE7 92) chain F residue 222 type sequence R description binding site for residue EDO D 401 source : AE7 93) chain D residue 303 type sequence S description binding site for residue EDO D 402 source : AE8 94) chain D residue 306 type sequence K description binding site for residue EDO D 402 source : AE8 95) chain F residue 222 type sequence R description binding site for residue EDO D 402 source : AE8 96) chain D residue 222 type sequence R description binding site for residue EDO D 403 source : AE9 97) chain F residue 299 type sequence D description binding site for residue EDO D 403 source : AE9 98) chain D residue 27 type sequence R description binding site for residue GOL D 404 source : AF1 99) chain D residue 105 type sequence P description binding site for residue GOL D 404 source : AF1 100) chain D residue 107 type sequence F description binding site for residue GOL D 404 source : AF1 101) chain D residue 108 type sequence A description binding site for residue GOL D 404 source : AF1 102) chain D residue 109 type sequence N description binding site for residue GOL D 404 source : AF1 103) chain D residue 178 type sequence I description binding site for residue GOL D 405 source : AF2 104) chain D residue 182 type sequence A description binding site for residue GOL D 405 source : AF2 105) chain D residue 210 type sequence L description binding site for residue GOL D 405 source : AF2 106) chain F residue 178 type sequence I description binding site for residue GOL D 405 source : AF2 107) chain F residue 182 type sequence A description binding site for residue GOL D 405 source : AF2 108) chain D residue 55 type sequence W description binding site for residue ACT D 406 source : AF3 109) chain D residue 56 type sequence Y description binding site for residue ACT D 406 source : AF3 110) chain D residue 139 type sequence S description binding site for residue ACT D 406 source : AF3 111) chain D residue 140 type sequence M description binding site for residue ACT D 406 source : AF3 112) chain D residue 322 type sequence H description binding site for residue ACT D 406 source : AF3 113) chain E residue 167 type sequence R description binding site for residue EDO E 401 source : AF4 114) chain E residue 274 type sequence L description binding site for residue EDO E 401 source : AF4 115) chain E residue 304 type sequence E description binding site for residue EDO E 401 source : AF4 116) chain E residue 312 type sequence E description binding site for residue EDO E 402 source : AF5 117) chain E residue 55 type sequence W description binding site for residue ACT E 403 source : AF6 118) chain E residue 56 type sequence Y description binding site for residue ACT E 403 source : AF6 119) chain E residue 139 type sequence S description binding site for residue ACT E 403 source : AF6 120) chain E residue 140 type sequence M description binding site for residue ACT E 403 source : AF6 121) chain E residue 322 type sequence H description binding site for residue ACT E 403 source : AF6 122) chain C residue 178 type sequence I description binding site for residue ACT E 404 source : AF7 123) chain C residue 182 type sequence A description binding site for residue ACT E 404 source : AF7 124) chain E residue 210 type sequence L description binding site for residue ACT E 404 source : AF7 125) chain F residue 167 type sequence R description binding site for residue EDO F 401 source : AF8 126) chain F residue 272 type sequence G description binding site for residue EDO F 401 source : AF8 127) chain F residue 273 type sequence D description binding site for residue EDO F 401 source : AF8 128) chain F residue 274 type sequence L description binding site for residue EDO F 401 source : AF8 129) chain F residue 275 type sequence A description binding site for residue EDO F 401 source : AF8 130) chain F residue 177 type sequence E description binding site for residue EDO F 402 source : AF9 131) chain F residue 167 type sequence R description binding site for residue GOL F 403 source : AG1 132) chain F residue 169 type sequence S description binding site for residue GOL F 403 source : AG1 133) chain F residue 274 type sequence L description binding site for residue GOL F 403 source : AG1 134) chain F residue 300 type sequence D description binding site for residue GOL F 403 source : AG1 135) chain F residue 303 type sequence S description binding site for residue GOL F 403 source : AG1 136) chain F residue 304 type sequence E description binding site for residue GOL F 403 source : AG1 137) chain A residue 47 type sequence S description binding site for residue GOL F 404 source : AG2 138) chain F residue 43 type sequence N description binding site for residue GOL F 404 source : AG2 139) chain F residue 45 type sequence D description binding site for residue GOL F 404 source : AG2 140) chain F residue 47 type sequence S description binding site for residue GOL F 404 source : AG2 141) chain A residue 43 type sequence N description binding site for residue GOL F 405 source : AG3 142) chain A residue 44 type sequence A description binding site for residue GOL F 405 source : AG3 143) chain A residue 45 type sequence D description binding site for residue GOL F 405 source : AG3 144) chain A residue 47 type sequence S description binding site for residue GOL F 405 source : AG3 145) chain F residue 55 type sequence W description binding site for residue ACT F 406 source : AG4 146) chain F residue 56 type sequence Y description binding site for residue ACT F 406 source : AG4 147) chain F residue 139 type sequence S description binding site for residue ACT F 406 source : AG4 148) chain F residue 140 type sequence M description binding site for residue ACT F 406 source : AG4 149) chain F residue 322 type sequence H description binding site for residue ACT F 406 source : AG4 150) chain A residue 139 type ACT_SITE sequence S description Nucleophile => ECO:0000305|PubMed:26787467 source Swiss-Prot : SWS_FT_FI1 151) chain B residue 139 type ACT_SITE sequence S description Nucleophile => ECO:0000305|PubMed:26787467 source Swiss-Prot : SWS_FT_FI1 152) chain C residue 139 type ACT_SITE sequence S description Nucleophile => ECO:0000305|PubMed:26787467 source Swiss-Prot : SWS_FT_FI1 153) chain D residue 139 type ACT_SITE sequence S description Nucleophile => ECO:0000305|PubMed:26787467 source Swiss-Prot : SWS_FT_FI1 154) chain E residue 139 type ACT_SITE sequence S description Nucleophile => ECO:0000305|PubMed:26787467 source Swiss-Prot : SWS_FT_FI1 155) chain F residue 139 type ACT_SITE sequence S description Nucleophile => ECO:0000305|PubMed:26787467 source Swiss-Prot : SWS_FT_FI1 156) chain A residue 293 type ACT_SITE sequence D description ACT_SITE => ECO:0000305|PubMed:26787467 source Swiss-Prot : SWS_FT_FI2 157) chain A residue 322 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:26787467 source Swiss-Prot : SWS_FT_FI2 158) chain B residue 293 type ACT_SITE sequence D description ACT_SITE => ECO:0000305|PubMed:26787467 source Swiss-Prot : SWS_FT_FI2 159) chain B residue 322 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:26787467 source Swiss-Prot : SWS_FT_FI2 160) chain C residue 293 type ACT_SITE sequence D description ACT_SITE => ECO:0000305|PubMed:26787467 source Swiss-Prot : SWS_FT_FI2 161) chain C residue 322 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:26787467 source Swiss-Prot : SWS_FT_FI2 162) chain D residue 293 type ACT_SITE sequence D description ACT_SITE => ECO:0000305|PubMed:26787467 source Swiss-Prot : SWS_FT_FI2 163) chain D residue 322 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:26787467 source Swiss-Prot : SWS_FT_FI2 164) chain E residue 293 type ACT_SITE sequence D description ACT_SITE => ECO:0000305|PubMed:26787467 source Swiss-Prot : SWS_FT_FI2 165) chain E residue 322 type ACT_SITE sequence H description ACT_SITE => ECO:0000305|PubMed:26787467 source Swiss-Prot : SWS_FT_FI2 166) chain F residue 293 type ACT_SITE sequence D description ACT_SITE => ECO:0000305|PubMed:26787467 source Swiss-Prot : SWS_FT_FI2 167) 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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