eF-site ID 4ubv-A PDB Code 4ubv Chain A click to enlarge Title Structure of the 3-ketoacyl-CoA thiolase FadA5 from M. tuberculosis with an partially acetylated cysteine in complex with acetyl-CoA and CoA Classification TRANSFERASE Compound Acetyl-CoA acetyltransferase FadA5 Source Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (I6XHI4_MYCTU) Sequence A:  MGYPVIVEATRSPIGKRNGWLSGLHATELLGAVQKAVVDK AGIQSGLHAGDVEQVIGGCVTQFGEQSNNISRVAWLTAGL PEHVGATTVDCQCGSGQQANHLIAGLIAAGAIDVGIACGI EAMSRVGLGANAGPDRSLIRAQSWDIDLPNQFEAAERIAK RRGITREDVDVFGLESQRRAQRAWAEGRFDREISPIQAPV LDEQNQPTGERRLVFRDQGLRETTMAGLGELKPVLEGGIH TAGTSSQISDGAAAVLWMDEAVARAHGLTPRARIVAQALV GAEPYYHLDGPVQSTAKVLEKAGMKIGDIDIVEINEAFAS VVLSWARVHEPDMDRVNVNGGAIALGHPVGCTGSRLITTA LHELERTDQSLALITMCAGGALSTGTIIERI Description Functional site 1) chain A residue 28 type sequence E description binding site for residue SO4 A 404 source : AC2 2) chain A residue 196 type sequence I description binding site for residue SO4 A 404 source : AC2 3) chain A residue 197 type sequence Q description binding site for residue SO4 A 404 source : AC2 4) chain A residue 17 type sequence R description binding site for residue DIO A 405 source : AC3 5) chain A residue 18 type sequence N description binding site for residue DIO A 405 source : AC3 6) chain A residue 264 type sequence R description binding site for residue DIO A 406 source : AC4 7) chain A residue 20 type sequence W description binding site for residue GOL A 407 source : AC5 8) chain A residue 212 type sequence R description binding site for residue GOL A 407 source : AC5 9) chain A residue 46 type sequence G description binding site for residue GOL A 408 source : AC6 10) chain A residue 81 type sequence P description binding site for residue GOL A 408 source : AC6 11) chain A residue 82 type sequence E description binding site for residue GOL A 408 source : AC6 12) chain A residue 83 type sequence H description binding site for residue GOL A 408 source : AC6 13) chain A residue 161 type sequence R description binding site for residue GOL A 409 source : AC7 14) chain A residue 162 type sequence R description binding site for residue GOL A 409 source : AC7 15) chain A residue 163 type sequence G description binding site for residue GOL A 409 source : AC7 16) chain A residue 333 type sequence M description binding site for residue GOL A 410 source : AC8 17) chain A residue 190 type sequence D description binding site for residue DIO B 404 source : AD3 18) chain A residue 20 type sequence W description binding site for residue DIO B 406 source : AD5 19) chain A residue 215 type sequence F description binding site for residue DIO B 406 source : AD5 20) chain A residue 216 type sequence R description binding site for residue DIO B 406 source : AD5 21) chain A residue 186 type sequence E description binding site for residue GOL B 415 source : AE5 22) chain A residue 337-353 type prosite sequence NVNGGAIALGHPVGCTG description THIOLASE_2 Thiolases signature 2. NvnGGaIAlGHPvGcTG source prosite : PS00737 23) chain A residue 246 type BINDING sequence S description BINDING => ECO:0000269|PubMed:25482540, ECO:0007744|PDB:4UBT, ECO:0007744|PDB:4UBU, ECO:0007744|PDB:4UBV source Swiss-Prot : SWS_FT_FI6 24) chain A residue 93 type ACT_SITE sequence C description Acyl-thioester intermediate => ECO:0000305|PubMed:25482540, ECO:0007744|PDB:4UBV source Swiss-Prot : SWS_FT_FI1 25) chain A residue 347 type ACT_SITE sequence H description Proton acceptor => ECO:0000305|PubMed:25482540, ECO:0007744|PDB:4UBV source Swiss-Prot : SWS_FT_FI2 26) chain A residue 377 type ACT_SITE sequence C description Proton acceptor => ECO:0000305|PubMed:25482540 source Swiss-Prot : SWS_FT_FI3 27) chain A residue 151 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:25482540, ECO:0007744|PDB:4UBT source Swiss-Prot : SWS_FT_FI4 28) chain A residue 379 type BINDING sequence G description BINDING => ECO:0000269|PubMed:25482540, ECO:0007744|PDB:4UBT source Swiss-Prot : SWS_FT_FI4 29) chain A residue 221 type BINDING sequence R description BINDING => ECO:0000269|PubMed:25482540, ECO:0007744|PDB:4UBT, ECO:0007744|PDB:4UBV source Swiss-Prot : SWS_FT_FI5

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