SitesBLAST
Comparing N515DRAFT_0378 FitnessBrowser__Dyella79:N515DRAFT_0378 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
5d6rB Acetolactate synthase from klebsiella pneumoniae in complex with mechanism-based inhibitor
36% identity, 98% coverage: 2:538/547 of query aligns to 6:544/548 of 5d6rB
- active site: I26 (≠ V22), G28 (= G24), A29 (≠ E25), K30 (≠ E26), I31 (≠ N27), E51 (= E47), T74 (= T70), H113 (≠ F109), Q114 (= Q110), S115 (≠ L111), Q163 (≠ E159), L254 (= L251), E281 (≠ P278), M386 (≠ N380), Q412 (≠ A406), M414 (= M408), D439 (= D433), D466 (= D460), G468 (≠ A462), Y469 (= Y463), M471 (= M465), V472 (≠ I466), Q475 (≠ K469), Y535 (= Y529)
- binding 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-[(Z)-2-fluoro-1-hydroxy-2-phosphonoethenyl]-5-(2-{[(S)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium: M386 (≠ N380), G387 (= G381), S388 (≠ M382), Q412 (≠ A406), M414 (= M408), D439 (= D433), G440 (= G434), G468 (≠ A462), Y469 (= Y463), N470 (≠ G464), M471 (= M465), Y535 (= Y529)
- binding magnesium ion: R63 (= R59), Q212 (≠ R210), D439 (= D433), D466 (= D460), G468 (≠ A462)
1ozgA The crystal structure of klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate (see paper)
35% identity, 98% coverage: 2:538/547 of query aligns to 7:547/549 of 1ozgA
- active site: I27 (≠ V22), G29 (= G24), A30 (≠ E25), K31 (≠ E26), I32 (≠ N27), E52 (= E47), T75 (= T70), H114 (≠ F109), Q115 (= Q110), S116 (≠ L111), Q164 (≠ E159), L257 (= L251), E284 (≠ P278), M389 (≠ N380), Q415 (≠ A406), M417 (= M408), D442 (= D433), D469 (= D460), G471 (≠ A462), Y472 (= Y463), M474 (= M465), V475 (≠ I466), Q478 (≠ K469), Y538 (= Y529)
- binding 2-hydroxyethyl dihydrothiachrome diphosphate: M389 (≠ N380), G390 (= G381), S391 (≠ M382), F392 (≠ Y383), Q415 (≠ A406), M417 (= M408), G441 (= G432), D442 (= D433), G443 (= G434), D469 (= D460), G471 (≠ A462), Y472 (= Y463), N473 (≠ G464), M474 (= M465), V475 (≠ I466), Y538 (= Y529)
- binding magnesium ion: D442 (= D433), D469 (= D460), G471 (≠ A462)
- binding phosphate ion: G253 (= G247), R254 (≠ N248), Q261 (≠ D255), R347 (≠ F335), R398 (= R389), Y401 (vs. gap)
1ozfA The crystal structure of klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactors (see paper)
36% identity, 98% coverage: 2:538/547 of query aligns to 6:543/545 of 1ozfA
- active site: I26 (≠ V22), G28 (= G24), A29 (≠ E25), K30 (≠ E26), I31 (≠ N27), E51 (= E47), T74 (= T70), H113 (≠ F109), Q114 (= Q110), S115 (≠ L111), Q163 (≠ E159), L253 (= L251), E280 (≠ P278), M385 (≠ N380), Q411 (≠ A406), M413 (= M408), D438 (= D433), D465 (= D460), G467 (≠ A462), Y468 (= Y463), M470 (= M465), V471 (≠ I466), Q474 (≠ K469), Y534 (= Y529)
- binding magnesium ion: D438 (= D433), D465 (= D460), G467 (≠ A462)
- binding phosphate ion: G249 (= G247), R250 (≠ N248), Q257 (≠ D255), R343 (≠ F335), R394 (= R389), L396 (vs. gap), Y397 (vs. gap)
- binding thiamine diphosphate: G386 (= G381), S387 (≠ M382), F388 (≠ Y383), Q411 (≠ A406), M413 (= M408), G437 (= G432), D438 (= D433), G439 (= G434), D465 (= D460), G467 (≠ A462), Y468 (= Y463), N469 (≠ G464), M470 (= M465), V471 (≠ I466), Y534 (= Y529)
5dx6B Acetolactate synthase from klebsiella pneumoniae soaked with beta- fluoropyruvate
35% identity, 98% coverage: 2:538/547 of query aligns to 18:550/557 of 5dx6B
- active site: I38 (≠ V22), G40 (= G24), A41 (≠ E25), K42 (≠ E26), I43 (≠ N27), E63 (= E47), T86 (= T70), H125 (≠ F109), Q126 (= Q110), S127 (≠ L111), Q175 (≠ E159), L268 (= L251), E295 (≠ P278), M392 (≠ N380), Q418 (≠ A406), M420 (= M408), D445 (= D433), D472 (= D460), G474 (≠ A462), Y475 (= Y463), M477 (= M465), V478 (≠ I466), Q481 (≠ K469), Y541 (= Y529)
- binding 3-fluoro-2-oxopropanoic acid: G264 (= G247), R265 (≠ N248), Q272 (≠ D255), A400 (= A388), R401 (= R389), Y404 (vs. gap)
- binding magnesium ion: S135 (≠ Q119), T138 (= T122), D445 (= D433), D472 (= D460), G474 (≠ A462)
- binding thiamine diphosphate: G393 (= G381), S394 (≠ M382), F395 (≠ Y383), Q418 (≠ A406), M420 (= M408), G444 (= G432), D445 (= D433), G446 (= G434), D472 (= D460), G474 (≠ A462), Y475 (= Y463), N476 (≠ G464), M477 (= M465), V478 (≠ I466), Y541 (= Y529)
5wdgA Acetolactate synthase from klebsiella pneumoniae in complex with a reaction intermediate
36% identity, 98% coverage: 2:538/547 of query aligns to 7:536/538 of 5wdgA
- active site: I27 (≠ V22), G29 (= G24), A30 (≠ E25), K31 (≠ E26), I32 (≠ N27), E52 (= E47), T75 (= T70), Q157 (≠ E159), L246 (= L251), E273 (≠ P278), M378 (≠ N380), Q404 (≠ A406), M406 (= M408), D431 (= D433), D458 (= D460), G460 (≠ A462), Y461 (= Y463), M463 (= M465), V464 (≠ I466), Q467 (≠ K469), Y527 (= Y529)
- binding (2S,3S)-2,3-dihydroxy-3-[(7S,8R,9aS)-8-(2-{[(R)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-2,7-dimethyl-5,7,8,10-tetrahydro-9aH-pyrimido[4,5-d][1,3]thiazolo[3,2-a]pyrimidin-9a-yl]-2-methylbutanoic acid: M378 (≠ N380), S380 (≠ M382), F381 (≠ Y383), Q404 (≠ A406), M406 (= M408), G430 (= G432), D431 (= D433), G432 (= G434), G433 (= G435), D458 (= D460), G460 (≠ A462), Y461 (= Y463), N462 (≠ G464), M463 (= M465), V464 (≠ I466), Y527 (= Y529)
- binding magnesium ion: R64 (= R59), S117 (≠ Q119), T120 (= T122), Q204 (≠ R210), D431 (= D433), D458 (= D460), G460 (≠ A462)
- binding pyruvic acid: G94 (≠ A89), R147 (= R149)
5dx6A Acetolactate synthase from klebsiella pneumoniae soaked with beta- fluoropyruvate
36% identity, 98% coverage: 2:538/547 of query aligns to 7:539/541 of 5dx6A
- active site: I27 (≠ V22), G29 (= G24), A30 (≠ E25), K31 (≠ E26), I32 (≠ N27), E52 (= E47), T75 (= T70), Q159 (≠ E159), L249 (= L251), E276 (≠ P278), M381 (≠ N380), Q407 (≠ A406), M409 (= M408), D434 (= D433), D461 (= D460), G463 (≠ A462), Y464 (= Y463), M466 (= M465), V467 (≠ I466), Q470 (≠ K469), Y530 (= Y529)
- binding 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-[(1R)-2-fluoro-1-hydroxyethyl]-5-(2-{[(S)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium: M381 (≠ N380), G382 (= G381), S383 (≠ M382), F384 (≠ Y383), Q407 (≠ A406), M409 (= M408), G433 (= G432), D434 (= D433), G435 (= G434), D461 (= D460), G463 (≠ A462), Y464 (= Y463), N465 (≠ G464), Y530 (= Y529)
- binding magnesium ion: S119 (≠ Q119), T122 (= T122), D434 (= D433), D461 (= D460), G463 (≠ A462)
4rjiC Acetolactate synthase from bacillus subtilis bound to thdp - crystal form i (see paper)
33% identity, 99% coverage: 3:542/547 of query aligns to 4:547/555 of 4rjiC
- binding magnesium ion: D438 (= D433), D465 (= D460), T467 (≠ A462)
- binding thiamine diphosphate: P24 (= P23), E48 (= E47), P74 (= P73), S387 (≠ M382), H388 (≠ Y383), Q411 (≠ A406), G437 (= G432), D438 (= D433), G439 (= G434), G440 (= G435), T467 (≠ A462), Y468 (= Y463), D469 (≠ G464), M470 (= M465), V471 (≠ I466), Y534 (= Y529)
4rjkG Acetolactate synthase from bacillus subtilis bound to lthdp - crystal form ii (see paper)
33% identity, 99% coverage: 3:542/547 of query aligns to 3:546/553 of 4rjkG
- binding magnesium ion: D437 (= D433), D464 (= D460), T466 (≠ A462)
- binding 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-(1-carboxy-1-hydroxyethyl)-5-(2-{[hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium: E47 (= E47), Q110 (= Q110)
- binding thiamine diphosphate: I384 (≠ N380), G385 (= G381), S386 (≠ M382), H387 (≠ Y383), Q410 (≠ A406), L412 (≠ M408), G436 (= G432), D437 (= D433), G438 (= G434), G439 (= G435), T466 (≠ A462), Y467 (= Y463), D468 (≠ G464), M469 (= M465), V470 (≠ I466), Y533 (= Y529)
4rjkF Acetolactate synthase from bacillus subtilis bound to lthdp - crystal form ii (see paper)
33% identity, 99% coverage: 3:542/547 of query aligns to 3:546/552 of 4rjkF
- binding magnesium ion: D437 (= D433), D464 (= D460), T466 (≠ A462)
- binding pyruvic acid: A25 (≠ E25), K26 (≠ E26)
- binding thiamine diphosphate: P23 (= P23), E47 (= E47), P73 (= P73), G385 (= G381), S386 (≠ M382), H387 (≠ Y383), Q410 (≠ A406), L412 (≠ M408), G436 (= G432), D437 (= D433), G438 (= G434), G439 (= G435), T466 (≠ A462), Y467 (= Y463), D468 (≠ G464), M469 (= M465), V470 (≠ I466), Y533 (= Y529)
P09342 Acetolactate synthase 1, chloroplastic; ALS I; Acetohydroxy-acid synthase I; Acetolactate synthase I; EC 2.2.1.6 from Nicotiana tabacum (Common tobacco) (see 2 papers)
29% identity, 96% coverage: 6:532/547 of query aligns to 99:643/667 of P09342
- C161 (≠ A67) modified: Disulfide link with 307
- P194 (= P100) mutation to Q: In C3; highly resistant to sulfonylurea herbicides.
- C307 (≠ A208) modified: Disulfide link with 161
P09114 Acetolactate synthase 2, chloroplastic; ALS II; Acetohydroxy-acid synthase II; Acetolactate synthase II; EC 2.2.1.6 from Nicotiana tabacum (Common tobacco) (see paper)
29% identity, 96% coverage: 6:532/547 of query aligns to 96:640/664 of P09114
- P191 (= P100) mutation to A: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with L-568.
- W568 (vs. gap) mutation to L: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with A-191.
1t9aA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, tribenuron methyl (see paper)
29% identity, 97% coverage: 1:528/547 of query aligns to 9:556/597 of 1t9aA
- active site: Y30 (≠ V22), G32 (= G24), G33 (≠ E25), A34 (≠ E26), I35 (≠ N27), E56 (= E47), T79 (= T70), F118 (= F109), Q119 (= Q110), E120 (≠ L111), K168 (≠ E159), R228 (≠ V215), M264 (≠ L251), V291 (≠ P278), V407 (≠ N380), L432 (= L405), G433 (≠ A406), M435 (= M408), D460 (= D433), N487 (≠ D460), E489 (≠ A462), Q490 (≠ Y463), M492 (= M465), V493 (≠ I466), W496 (= W468), L518 (≠ F490), G523 (= G495), L524 (≠ A496)
- binding methyl 2-[4-methoxy-6-methyl-1,3,5-trazin-2-yl(methyl)carbamoylsulfamoyl]benzoate: G33 (≠ E25), V108 (≠ K99), P109 (= P100), F118 (= F109), K168 (≠ E159), M264 (≠ L251), D289 (≠ E276), R290 (≠ K277), M492 (= M465), V493 (≠ I466), W496 (= W468)
- binding flavin-adenine dinucleotide: R158 (= R149), G217 (= G205), A218 (= A206), G219 (≠ A207), N222 (= N209), T244 (= T231), L245 (≠ Q232), Q246 (≠ M233), L262 (≠ A249), M264 (≠ L251), H265 (≠ S252), G284 (= G271), A285 (≠ H272), R286 (≠ D273), D288 (≠ V275), R290 (≠ K277), V291 (≠ P278), E317 (≠ N293), V318 (≠ F294), N322 (≠ E298), G335 (= G311), D336 (= D312), A337 (≠ I313), Q411 (≠ K384), M412 (≠ I385), G430 (≠ N403), G431 (≠ A404)
- binding magnesium ion: D460 (= D433), N487 (≠ D460), E489 (≠ A462)
- binding propyl trihydrogen diphosphate: V407 (≠ N380), G408 (= G381), Q409 (≠ M382), H410 (≠ Y383), M435 (= M408), G459 (= G432), D460 (= D433), A461 (≠ G434), S462 (≠ G435), N487 (≠ D460), E489 (≠ A462), Q490 (≠ Y463), G491 (= G464), M492 (= M465)
- binding 5-{[ethyl(methyl)amino]methyl}-2-methyl-5,6-dihydropyrimidin-4-amine: G433 (≠ A406), M435 (= M408), M465 (= M438)
Sites not aligning to the query:
1t9dA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, metsulfuron methyl (see paper)
29% identity, 97% coverage: 1:528/547 of query aligns to 8:555/596 of 1t9dA
- active site: Y29 (≠ V22), G31 (= G24), G32 (≠ E25), A33 (≠ E26), I34 (≠ N27), E55 (= E47), T78 (= T70), F117 (= F109), Q118 (= Q110), E119 (≠ L111), K167 (≠ E159), R227 (≠ V215), M263 (≠ L251), V290 (≠ P278), V406 (≠ N380), L431 (= L405), G432 (≠ A406), M434 (= M408), D459 (= D433), N486 (≠ D460), E488 (≠ A462), Q489 (≠ Y463), M491 (= M465), V492 (≠ I466), W495 (= W468), L517 (≠ F490), G522 (= G495), L523 (≠ A496)
- binding methyl 2-[({[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)amino]carbonyl}amino)sulfonyl]benzoate: G32 (≠ E25), A33 (≠ E26), V107 (≠ K99), P108 (= P100), F117 (= F109), K167 (≠ E159), M263 (≠ L251), D288 (≠ E276), R289 (≠ K277), W495 (= W468)
- binding flavin-adenine dinucleotide: R157 (= R149), G216 (= G205), A217 (= A206), G218 (≠ A207), N221 (= N209), T243 (= T231), L244 (≠ Q232), Q245 (≠ M233), M260 (≠ N248), L261 (≠ A249), H264 (≠ S252), G283 (= G271), A284 (≠ H272), R285 (≠ D273), D287 (≠ V275), R289 (≠ K277), V290 (≠ P278), E316 (≠ N293), V317 (≠ F294), N321 (≠ E298), G334 (= G311), D335 (= D312), A336 (≠ I313), Q410 (≠ K384), M411 (≠ I385), G429 (≠ N403), G430 (≠ A404)
- binding magnesium ion: D459 (= D433), N486 (≠ D460), E488 (≠ A462)
- binding 2,5-dimethyl-pyrimidin-4-ylamine: E55 (= E47), P81 (= P73), Q118 (= Q110), G432 (≠ A406), M434 (= M408), M464 (= M438)
Sites not aligning to the query:
1t9cA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, sulfometuron methyl (see paper)
29% identity, 97% coverage: 1:528/547 of query aligns to 8:555/596 of 1t9cA
- active site: Y29 (≠ V22), G31 (= G24), G32 (≠ E25), A33 (≠ E26), I34 (≠ N27), E55 (= E47), T78 (= T70), F117 (= F109), Q118 (= Q110), E119 (≠ L111), K167 (≠ E159), R227 (≠ V215), M263 (≠ L251), V290 (≠ P278), V406 (≠ N380), L431 (= L405), G432 (≠ A406), M434 (= M408), D459 (= D433), N486 (≠ D460), E488 (≠ A462), Q489 (≠ Y463), M491 (= M465), V492 (≠ I466), W495 (= W468), L517 (≠ F490), G522 (= G495), L523 (≠ A496)
- binding methyl 2-[({[(4,6-dimethylpyrimidin-2-yl)amino]carbonyl}amino)sulfonyl]benzoate: G32 (≠ E25), V107 (≠ K99), P108 (= P100), F117 (= F109), K167 (≠ E159), D288 (≠ E276), R289 (≠ K277), W495 (= W468)
- binding flavin-adenine dinucleotide: R157 (= R149), G216 (= G205), A217 (= A206), G218 (≠ A207), N221 (= N209), T243 (= T231), L244 (≠ Q232), Q245 (≠ M233), L261 (≠ A249), M263 (≠ L251), H264 (≠ S252), G283 (= G271), A284 (≠ H272), R285 (≠ D273), D287 (≠ V275), R289 (≠ K277), V290 (≠ P278), E316 (≠ N293), V317 (≠ F294), N321 (≠ E298), G334 (= G311), D335 (= D312), A336 (≠ I313), M411 (≠ I385), G429 (≠ N403), G430 (≠ A404)
- binding magnesium ion: D459 (= D433), N486 (≠ D460), E488 (≠ A462)
Sites not aligning to the query:
1n0hA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, chlorimuron ethyl (see paper)
29% identity, 97% coverage: 1:528/547 of query aligns to 10:558/599 of 1n0hA
- active site: Y31 (≠ V22), G33 (= G24), G34 (≠ E25), A35 (≠ E26), I36 (≠ N27), E57 (= E47), T80 (= T70), F119 (= F109), Q120 (= Q110), E121 (≠ L111), K169 (≠ E159), R230 (≠ V215), M266 (≠ L251), V293 (≠ P278), V409 (≠ N380), L434 (= L405), G435 (≠ A406), M437 (= M408), D462 (= D433), N489 (≠ D460), E491 (≠ A462), Q492 (≠ Y463), M494 (= M465), V495 (≠ I466), W498 (= W468), L520 (≠ F490), G525 (= G495), L526 (≠ A496)
- binding 4-{[(4'-amino-2'-methylpyrimidin-5'-yl)methyl]amino}pent-3-enyl diphosphate: V409 (≠ N380), G410 (= G381), Q411 (≠ M382), H412 (≠ Y383), G435 (≠ A406), M437 (= M408), G461 (= G432), D462 (= D433), A463 (≠ G434), S464 (≠ G435), M467 (= M438), N489 (≠ D460), E491 (≠ A462), Q492 (≠ Y463), G493 (= G464), V495 (≠ I466)
- binding 2-[[[[(4-chloro-6-methoxy-2-pyrimidinyl)amino]carbonyl]amino]sulfonyl]benzoic acid ethyl ester: G34 (≠ E25), A35 (≠ E26), V109 (≠ K99), P110 (= P100), F119 (= F109), K169 (≠ E159), M266 (≠ L251), D291 (≠ E276), R292 (≠ K277), V495 (≠ I466), W498 (= W468)
- binding flavin-adenine dinucleotide: R159 (= R149), G219 (= G205), A220 (= A206), G221 (≠ A207), N224 (= N209), T246 (= T231), L247 (≠ Q232), Q248 (≠ M233), L264 (≠ A249), G265 (≠ A250), M266 (≠ L251), H267 (≠ S252), G286 (= G271), A287 (≠ H272), R288 (≠ D273), D290 (≠ V275), R292 (≠ K277), V293 (≠ P278), E319 (≠ N293), V320 (≠ F294), N324 (≠ E298), G337 (= G311), D338 (= D312), A339 (≠ I313), M414 (≠ I385), G432 (≠ N403), G433 (≠ A404)
- binding magnesium ion: D462 (= D433), N489 (≠ D460), E491 (≠ A462)
- binding thiamine diphosphate: Y31 (≠ V22), E57 (= E47), P83 (= P73)
Sites not aligning to the query:
5wkcA Saccharomyces cerevisiae acetohydroxyacid synthase in complex with the herbicide penoxsulam (see paper)
29% identity, 97% coverage: 1:528/547 of query aligns to 8:550/591 of 5wkcA
- active site: Y29 (≠ V22), G31 (= G24), G32 (≠ E25), A33 (≠ E26), I34 (≠ N27), E55 (= E47), T78 (= T70), F117 (= F109), Q118 (= Q110), E119 (≠ L111), K167 (≠ E159), R222 (≠ V215), M258 (≠ L251), V285 (≠ P278), V401 (≠ N380), L426 (= L405), G427 (≠ A406), M429 (= M408), D454 (= D433), N481 (≠ D460), E483 (≠ A462), Q484 (≠ Y463), M486 (= M465), V487 (≠ I466), W490 (= W468), L512 (≠ F490), G517 (= G495), L518 (≠ A496)
- binding 2-[3-[(4-azanyl-2-methyl-pyrimidin-5-yl)methyl]-2-[(1~{S})-1-(dioxidanyl)-1-oxidanyl-ethyl]-4-methyl-1,3-thiazol-5-yl]ethyl phosphono hydrogen phosphate: V401 (≠ N380), G402 (= G381), Q403 (≠ M382), H404 (≠ Y383), G427 (≠ A406), M429 (= M408), G453 (= G432), D454 (= D433), A455 (≠ G434), S456 (≠ G435), M459 (= M438), N481 (≠ D460), E483 (≠ A462), Q484 (≠ Y463), G485 (= G464), M486 (= M465), V487 (≠ I466)
- binding ethaneperoxoic acid: G32 (≠ E25), Q118 (= Q110)
- binding flavin-adenine dinucleotide: R157 (= R149), G211 (= G205), A212 (= A206), G213 (≠ A207), N216 (= N209), T238 (= T231), L239 (≠ Q232), Q240 (≠ M233), L256 (≠ A249), M258 (≠ L251), G278 (= G271), A279 (≠ H272), R280 (≠ D273), R284 (≠ K277), V285 (≠ P278), E311 (≠ N293), V312 (≠ F294), N316 (≠ E298), D330 (= D312), A331 (≠ I313), M406 (≠ I385), G424 (≠ N403)
- binding magnesium ion: D454 (= D433), N481 (≠ D460), E483 (≠ A462)
- binding 2-(2,2-difluoroethoxy)-N-(5,8-dimethoxy[1,2,4]triazolo[1,5-c]pyrimidin-2-yl)-6-(trifluoromethyl)benzenesulfonamide: G32 (≠ E25), A33 (≠ E26), V107 (≠ K99), F117 (= F109), K167 (≠ E159), M258 (≠ L251), R284 (≠ K277), M486 (= M465), W490 (= W468)
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: P30 (= P23), E55 (= E47)
Sites not aligning to the query:
1t9bB Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, chlorsulfuron (see paper)
30% identity, 97% coverage: 1:528/547 of query aligns to 8:554/595 of 1t9bB
- active site: Y29 (≠ V22), G31 (= G24), G32 (≠ E25), A33 (≠ E26), I34 (≠ N27), E55 (= E47), T78 (= T70), F117 (= F109), Q118 (= Q110), E119 (≠ L111), K167 (≠ E159), R226 (≠ V215), M262 (≠ L251), V289 (≠ P278), V405 (≠ N380), L430 (= L405), G431 (≠ A406), M433 (= M408), D458 (= D433), N485 (≠ D460), E487 (≠ A462), Q488 (≠ Y463), M490 (= M465), V491 (≠ I466), W494 (= W468), L516 (≠ F490), G521 (= G495), L522 (≠ A496)
- binding 1-(2-chlorophenylsulfonyl)-3-(4-methoxy-6-methyl-l,3,5-triazin-2-yl)urea: V107 (≠ K99), P108 (= P100), D287 (≠ E276), R288 (≠ K277), M490 (= M465), W494 (= W468)
- binding flavin-adenine dinucleotide: R157 (= R149), G215 (= G205), A216 (= A206), G217 (≠ A207), N220 (= N209), T242 (= T231), L243 (≠ Q232), Q244 (≠ M233), M259 (≠ N248), L260 (≠ A249), M262 (≠ L251), H263 (≠ S252), G282 (= G271), A283 (≠ H272), R284 (≠ D273), D286 (≠ V275), R288 (≠ K277), V289 (≠ P278), E315 (≠ N293), V316 (≠ F294), N320 (≠ E298), G333 (= G311), D334 (= D312), A335 (≠ I313), Q409 (≠ K384), M410 (≠ I385), G428 (≠ N403), G429 (≠ A404)
- binding magnesium ion: D458 (= D433), N485 (≠ D460), E487 (≠ A462)
Sites not aligning to the query:
1t9dB Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, metsulfuron methyl (see paper)
30% identity, 97% coverage: 1:528/547 of query aligns to 7:541/582 of 1t9dB
- active site: Y28 (≠ V22), G30 (= G24), G31 (≠ E25), A32 (≠ E26), I33 (≠ N27), E54 (= E47), T77 (= T70), F116 (= F109), Q117 (= Q110), E118 (≠ L111), K166 (≠ E159), R213 (≠ V215), M249 (≠ L251), V276 (≠ P278), V392 (≠ N380), L417 (= L405), G418 (≠ A406), M420 (= M408), D445 (= D433), N472 (≠ D460), E474 (≠ A462), Q475 (≠ Y463), M477 (= M465), V478 (≠ I466), W481 (= W468), L503 (≠ F490), G508 (= G495), L509 (≠ A496)
- binding methyl 2-[({[(4-methoxy-6-methyl-1,3,5-triazin-2-yl)amino]carbonyl}amino)sulfonyl]benzoate: G31 (≠ E25), A32 (≠ E26), V106 (≠ K99), P107 (= P100), F116 (= F109), K166 (≠ E159), M249 (≠ L251), D274 (≠ E276), R275 (≠ K277), W481 (= W468)
- binding flavin-adenine dinucleotide: R156 (= R149), G202 (= G205), A203 (= A206), G204 (≠ A207), N207 (= N209), T229 (= T231), L230 (≠ Q232), Q231 (≠ M233), L247 (≠ A249), M249 (≠ L251), H250 (≠ S252), G269 (= G271), A270 (≠ H272), R271 (≠ D273), D273 (≠ V275), R275 (≠ K277), V276 (≠ P278), E302 (≠ N293), V303 (≠ F294), N307 (≠ E298), G320 (= G311), D321 (= D312), A322 (≠ I313), Q396 (≠ K384), M397 (≠ I385), G415 (≠ N403), G416 (≠ A404)
- binding magnesium ion: D445 (= D433), N472 (≠ D460), E474 (≠ A462)
- binding 2,5-dimethyl-pyrimidin-4-ylamine: E54 (= E47), P80 (= P73), G418 (≠ A406), M420 (= M408), M450 (= M438)
Sites not aligning to the query:
1t9bA Crystal structure of yeast acetohydroxyacid synthase in complex with a sulfonylurea herbicide, chlorsulfuron (see paper)
30% identity, 97% coverage: 1:528/547 of query aligns to 8:542/583 of 1t9bA
- active site: Y29 (≠ V22), G31 (= G24), G32 (≠ E25), A33 (≠ E26), I34 (≠ N27), E55 (= E47), T78 (= T70), F117 (= F109), Q118 (= Q110), E119 (≠ L111), K167 (≠ E159), R214 (≠ V215), M250 (≠ L251), V277 (≠ P278), V393 (≠ N380), L418 (= L405), G419 (≠ A406), M421 (= M408), D446 (= D433), N473 (≠ D460), E475 (≠ A462), Q476 (≠ Y463), M478 (= M465), V479 (≠ I466), W482 (= W468), L504 (≠ F490), G509 (= G495), L510 (≠ A496)
- binding 1-(2-chlorophenylsulfonyl)-3-(4-methoxy-6-methyl-l,3,5-triazin-2-yl)urea: V107 (≠ K99), P108 (= P100), F117 (= F109), D275 (≠ E276), R276 (≠ K277), M478 (= M465), W482 (= W468)
- binding flavin-adenine dinucleotide: R157 (= R149), G203 (= G205), A204 (= A206), G205 (≠ A207), N208 (= N209), T230 (= T231), L231 (≠ Q232), Q232 (≠ M233), M247 (≠ N248), L248 (≠ A249), M250 (≠ L251), H251 (≠ S252), G270 (= G271), A271 (≠ H272), R272 (≠ D273), D274 (≠ V275), R276 (≠ K277), V277 (≠ P278), E303 (≠ N293), V304 (≠ F294), N308 (≠ E298), D322 (= D312), A323 (≠ I313), Q397 (≠ K384), M398 (≠ I385), G416 (≠ N403), G417 (≠ A404)
- binding magnesium ion: D446 (= D433), N473 (≠ D460), E475 (≠ A462)
Sites not aligning to the query:
P07342 Acetolactate synthase catalytic subunit, mitochondrial; Acetohydroxy-acid synthase catalytic subunit; AHAS; ALS; EC 2.2.1.6 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
29% identity, 97% coverage: 1:528/547 of query aligns to 92:646/687 of P07342
- R241 (= R149) binding
- 355:376 (vs. 252:273, 27% identical) binding
- 407:426 (vs. 293:312, 35% identical) binding
Query Sequence
>N515DRAFT_0378 FitnessBrowser__Dyella79:N515DRAFT_0378
MNAAALFVKALEAEGVRRIFGVPGEENLDLVEALRDSKIELIVTRHEQAAGFMAATWGRL
TGEAGVALSTLGPGATNLVTAAAYAQLGAMPMLMITGQKPIRTHKQGLFQLVDVVDMMQP
LTKYTRQIVSAPTIPARVREAFRRAEEERPGAVHLELPEDIARDSVDEAILLPTEYARRP
SPDDAALVQAGEAITAAKHPILMIGAAANRQRTAVALRTFIDKLGIPFFTTQMGKGVVDE
DHPLWLGNAALSDGDFVHRAIDAADVIVNVGHDVVEKPPFFMHKGRRTVIHINFSSAEVD
TVYFPQIEVVGDIAHTVERLTDALTPQAHWNFKYFDQVREAFHRQLAEHADDPRFPIHPV
RLVADTRRYMPDDGVLCLDNGMYKIWYARYYRARQPNTVLLDNALATMGAGLPSAMAAKL
VYPERKVLAICGDGGFMMNAQELETAVRLKMDLVILLLRDDAYGMIRWKQAEMGYADFGM
QFSNPDFVKFAEAHGAHGHRPESADAFLPTLKRAFEQGGVHLIDLAIDYSDNHRILNEEI
RRLSAAV
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory