eF-site ID 2aqb-ABCD PDB Code 2aqb Chain A, B, C, D click to enlarge Title Structure-activity relationships at the 5-position of thiolactomycin: an intact 5(R)-isoprene unit is required for activity against the condensing enzymes from Mycobacterium tuberculosis and Escherchia coli Classification TRANSFERASE Compound 3-oxoacyl-[acyl-carrier-protein] synthase I Source Escherichia coli (strain K12) (FABB_ECOLI) Sequence A:  MKRAVITGLGIVSSIGNNQQEVLASLREGRSGITFSQELK DSGMRSHVWGNVKLDTTGLIDRKVVRFMSDASIYAFLSME QAIADAGLSPEAYQNNPRVGLIAGSGGGSPRFQVFGADAM RGPRGLKAVGPYVVTKAMASGVSACLATPFKIHGVNYSIS SACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCWEMACE FDAMGALSTKYNDTPEKASRTYDAHRDGFVIAGGGGMVVV EELEHALARGAHIYAEIVGYGATSDGADMVAPSGEGAVRC MKMAMHGVDTPIDYLNSHGTSTPVGDVKELAAIREVFGDK SPAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSIN IEELDEQAAGLNIVTETTDRELTTVMSNSFGFGGTNATLV MRKL B:  KRAVITGLGIVSSIGNNQQEVLASLREGRSGITFSQELKD SGMRSHVWGNVKLDTTGLIDRKVVRFMSDASIYAFLSMEQ AIADAGLSPEAYQNNPRVGLIAGSGGGSPRFQVFGADAMR GPRGLKAVGPYVVTKAMASGVSACLATPFKIHGVNYSISS ACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCWEMACEF DAMGALSTKYNDTPEKASRTYDAHRDGFVIAGGGGMVVVE ELEHALARGAHIYAEIVGYGATSDGADMVAPSGEGAVRCM KMAMHGVDTPIDYLNSHGTSTPVGDVKELAAIREVFGDKS PAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINI EELDEQAAGLNIVTETTDRELTTVMSNSFGFGGTNATLVM RKL C:  KRAVITGLGIVSSIGNNQQEVLASLREGRSGITFSQELKD SGMRSHVWGNVKLDTTGLIDRKVVRFMSDASIYAFLSMEQ AIADAGLSPEAYQNNPRVGLIAGSGGGSPRFQVFGADAMR GPRGLKAVGPYVVTKAMASGVSACLATPFKIHGVNYSISS ACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCWEMACEF DAMGALSTKYNDTPEKASRTYDAHRDGFVIAGGGGMVVVE ELEHALARGAHIYAEIVGYGATSDGADMVAPSGEGAVRCM KMAMHGVDTPIDYLNSHGTSTPVGDVKELAAIREVFGDKS PAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINI EELDEQAAGLNIVTETTDRELTTVMSNSFGFGGTNATLVM RKL D:  KRAVITGLGIVSSIGNNQQEVLASLREGRSGITFSQELKD SGMRSHVWGNVKLDTTGLIDRKVVRFMSDASIYAFLSMEQ AIADAGLSPEAYQNNPRVGLIAGSGGGSPRFQVFGADAMR GPRGLKAVGPYVVTKAMASGVSACLATPFKIHGVNYSISS ACATSAHCIGNAVEQIQLGKQDIVFAGGGEELCWEMACEF DAMGALSTKYNDTPEKASRTYDAHRDGFVIAGGGGMVVVE ELEHALARGAHIYAEIVGYGATSDGADMVAPSGEGAVRCM KMAMHGVDTPIDYLNSHGTSTPVGDVKELAAIREVFGDKS PAISATKAMTGHSLGAAGVQEAIYSLLMLEHGFIAPSINI EELDEQAAGLNIVTETTDRELTTVMSNSFGFGGTNATLVM RKL Description Functional site 1) chain A residue 163 type sequence C description BINDING SITE FOR RESIDUE TL6 A 600 source : AC1 2) chain A residue 229 type sequence F description BINDING SITE FOR RESIDUE TL6 A 600 source : AC1 3) chain A residue 268 type sequence D description BINDING SITE FOR RESIDUE TL6 A 600 source : AC1 4) chain A residue 269 type sequence M description BINDING SITE FOR RESIDUE TL6 A 600 source : AC1 5) chain A residue 270 type sequence V description BINDING SITE FOR RESIDUE TL6 A 600 source : AC1 6) chain A residue 271 type sequence A description BINDING SITE FOR RESIDUE TL6 A 600 source : AC1 7) chain A residue 272 type sequence P description BINDING SITE FOR RESIDUE TL6 A 600 source : AC1 8) chain A residue 298 type sequence H description BINDING SITE FOR RESIDUE TL6 A 600 source : AC1 9) chain A residue 300 type sequence T description BINDING SITE FOR RESIDUE TL6 A 600 source : AC1 10) chain A residue 302 type sequence T description BINDING SITE FOR RESIDUE TL6 A 600 source : AC1 11) chain A residue 333 type sequence H description BINDING SITE FOR RESIDUE TL6 A 600 source : AC1 12) chain A residue 390 type sequence F description BINDING SITE FOR RESIDUE TL6 A 600 source : AC1 13) chain A residue 391 type sequence G description BINDING SITE FOR RESIDUE TL6 A 600 source : AC1 14) chain A residue 392 type sequence F description BINDING SITE FOR RESIDUE TL6 A 600 source : AC1 15) chain A residue 394 type sequence G description BINDING SITE FOR RESIDUE TL6 A 600 source : AC1 16) chain B residue 163 type sequence C description BINDING SITE FOR RESIDUE TL6 B 601 source : AC2 17) chain B residue 229 type sequence F description BINDING SITE FOR RESIDUE TL6 B 601 source : AC2 18) chain B residue 269 type sequence M description BINDING SITE FOR RESIDUE TL6 B 601 source : AC2 19) chain B residue 270 type sequence V description BINDING SITE FOR RESIDUE TL6 B 601 source : AC2 20) chain B residue 271 type sequence A description BINDING SITE FOR RESIDUE TL6 B 601 source : AC2 21) chain B residue 272 type sequence P description BINDING SITE FOR RESIDUE TL6 B 601 source : AC2 22) chain B residue 298 type sequence H description BINDING SITE FOR RESIDUE TL6 B 601 source : AC2 23) chain B residue 300 type sequence T description BINDING SITE FOR RESIDUE TL6 B 601 source : AC2 24) chain B residue 302 type sequence T description BINDING SITE FOR RESIDUE TL6 B 601 source : AC2 25) chain B residue 333 type sequence H description BINDING SITE FOR RESIDUE TL6 B 601 source : AC2 26) chain B residue 390 type sequence F description BINDING SITE FOR RESIDUE TL6 B 601 source : AC2 27) chain B residue 391 type sequence G description BINDING SITE FOR RESIDUE TL6 B 601 source : AC2 28) chain B residue 394 type sequence G description BINDING SITE FOR RESIDUE TL6 B 601 source : AC2 29) chain D residue 163 type sequence C description BINDING SITE FOR RESIDUE TL6 D 602 source : AC3 30) chain D residue 229 type sequence F description BINDING SITE FOR RESIDUE TL6 D 602 source : AC3 31) chain D residue 270 type sequence V description BINDING SITE FOR RESIDUE TL6 D 602 source : AC3 32) chain D residue 271 type sequence A description BINDING SITE FOR RESIDUE TL6 D 602 source : AC3 33) chain D residue 272 type sequence P description BINDING SITE FOR RESIDUE TL6 D 602 source : AC3 34) chain D residue 298 type sequence H description BINDING SITE FOR RESIDUE TL6 D 602 source : AC3 35) chain D residue 300 type sequence T description BINDING SITE FOR RESIDUE TL6 D 602 source : AC3 36) chain D residue 333 type sequence H description BINDING SITE FOR RESIDUE TL6 D 602 source : AC3 37) chain D residue 390 type sequence F description BINDING SITE FOR RESIDUE TL6 D 602 source : AC3 38) chain D residue 391 type sequence G description BINDING SITE FOR RESIDUE TL6 D 602 source : AC3 39) chain D residue 392 type sequence F description BINDING SITE FOR RESIDUE TL6 D 602 source : AC3 40) chain D residue 394 type sequence G description BINDING SITE FOR RESIDUE TL6 D 602 source : AC3 41) chain A residue 163 type catalytic sequence C description 292 source MCSA : MCSA1 42) chain A residue 298 type catalytic sequence H description 292 source MCSA : MCSA1 43) chain A residue 328 type catalytic sequence K description 292 source MCSA : MCSA1 44) chain A residue 333 type catalytic sequence H description 292 source MCSA : MCSA1 45) chain A residue 390 type catalytic sequence F description 292 source MCSA : MCSA1 46) chain A residue 392 type catalytic sequence F description 292 source MCSA : MCSA1 47) chain B residue 163 type catalytic sequence C description 292 source MCSA : MCSA2 48) chain B residue 298 type catalytic sequence H description 292 source MCSA : MCSA2 49) chain B residue 328 type catalytic sequence K description 292 source MCSA : MCSA2 50) chain B residue 333 type catalytic sequence H description 292 source MCSA : MCSA2 51) chain B residue 390 type catalytic sequence F description 292 source MCSA : MCSA2 52) chain B residue 392 type catalytic sequence F description 292 source MCSA : MCSA2 53) chain C residue 163 type catalytic sequence C description 292 source MCSA : MCSA3 54) chain C residue 298 type catalytic sequence H description 292 source MCSA : MCSA3 55) chain C residue 328 type catalytic sequence K description 292 source MCSA : MCSA3 56) chain C residue 333 type catalytic sequence H description 292 source MCSA : MCSA3 57) chain C residue 390 type catalytic sequence F description 292 source MCSA : MCSA3 58) chain C residue 392 type catalytic sequence F description 292 source MCSA : MCSA3 59) chain D residue 163 type catalytic sequence C description 292 source MCSA : MCSA4 60) chain D residue 298 type catalytic sequence H description 292 source MCSA : MCSA4 61) chain D residue 328 type catalytic sequence K description 292 source MCSA : MCSA4 62) chain D residue 333 type catalytic sequence H description 292 source MCSA : MCSA4 63) chain D residue 390 type catalytic sequence F description 292 source MCSA : MCSA4 64) chain D residue 392 type catalytic sequence F description 292 source MCSA : MCSA4 65) chain A residue 154-170 type prosite sequence GVNYSISSACATSAHCI description KS3_1 Ketosynthase family 3 (KS3) active site signature. GVNysISsACATSahCI source prosite : PS00606 66) chain A residue 298 type ACT_SITE sequence H description For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348 source Swiss-Prot : SWS_FT_FI2 67) chain A residue 333 type ACT_SITE sequence H description For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348 source Swiss-Prot : SWS_FT_FI2 68) chain B residue 298 type ACT_SITE sequence H description For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348 source Swiss-Prot : SWS_FT_FI2 69) chain B residue 333 type ACT_SITE sequence H description For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348 source Swiss-Prot : SWS_FT_FI2 70) chain C residue 298 type ACT_SITE sequence H description For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348 source Swiss-Prot : SWS_FT_FI2 71) chain C residue 333 type ACT_SITE sequence H description For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348 source Swiss-Prot : SWS_FT_FI2 72) chain D residue 298 type ACT_SITE sequence H description For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348 source Swiss-Prot : SWS_FT_FI2 73) chain D residue 333 type ACT_SITE sequence H description For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348 source Swiss-Prot : SWS_FT_FI2 74) chain A residue 163 type ACT_SITE sequence C description For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348, ECO:0000305|PubMed:10571059 source Swiss-Prot : SWS_FT_FI1 75) chain B residue 163 type ACT_SITE sequence C description For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348, ECO:0000305|PubMed:10571059 source Swiss-Prot : SWS_FT_FI1 76) chain C residue 163 type ACT_SITE sequence C description For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348, ECO:0000305|PubMed:10571059 source Swiss-Prot : SWS_FT_FI1 77) chain D residue 163 type ACT_SITE sequence C description For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348, ECO:0000305|PubMed:10571059 source Swiss-Prot : SWS_FT_FI1

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