SitesBLAST
Comparing RR42_RS36655 FitnessBrowser__Cup4G11:RR42_RS36655 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
6a50A Structure of benzoylformate decarboxylases in complex with cofactor tpp
29% identity, 97% coverage: 15:510/512 of query aligns to 16:521/527 of 6a50A
- binding magnesium ion: N117 (≠ G117), L118 (≠ W118), R120 (= R120), D428 (= D411), N455 (= N438), T457 (≠ K440)
- binding thiamine diphosphate: N23 (= N22), P24 (= P23), E47 (= E48), H70 (= H71), T377 (≠ V360), S378 (= S361), G401 (= G384), L403 (≠ I386), G427 (≠ A410), D428 (= D411), G429 (= G412), S430 (= S413), Y433 (= Y416), N455 (= N438), T457 (≠ K440), Y458 (= Y441), G459 (≠ A442), M460 (≠ L444), L461 (= L445)
5deiA Benzoylformate decarboxylase from pseudomonas putida
29% identity, 97% coverage: 15:510/512 of query aligns to 15:520/524 of 5deiA
- active site: N22 (= N22), G24 (= G24), S25 (≠ T25), N26 (≠ S26), E27 (= E27), E46 (= E48), H69 (= H71), L108 (≠ P110), L109 (= L111), T110 (= T112), N111 (vs. gap), Y159 (≠ W164), P253 (vs. gap), H280 (≠ P281), S375 (= S359), G400 (= G384), L402 (≠ I386), D427 (= D411), N454 (= N438), T456 (≠ K440), Y457 (= Y441), A459 (≠ I443), L460 (= L444), F463 (≠ L448)
- binding bicarbonate ion: S25 (≠ T25), H69 (= H71), L109 (= L111)
- binding calcium ion: N185 (≠ L194), D186 (≠ R195), D427 (= D411), N454 (= N438), T456 (≠ K440)
- binding magnesium ion: N116 (≠ G117), L117 (≠ W118), R119 (= R120)
- binding thiamine diphosphate: N22 (= N22), P23 (= P23), E46 (= E48), H69 (= H71), T376 (≠ V360), S377 (= S361), L402 (≠ I386), G426 (≠ A410), D427 (= D411), G428 (= G412), S429 (= S413), Y432 (= Y416), T456 (≠ K440), Y457 (= Y441), G458 (≠ A442), A459 (≠ I443), L460 (= L444)
Sites not aligning to the query:
3fsjX Crystal structure of benzoylformate decarboxylase in complex with the inhibitor mbp (see paper)
29% identity, 97% coverage: 15:510/512 of query aligns to 15:520/524 of 3fsjX
- active site: G24 (= G24), S25 (≠ T25), E27 (= E27), E46 (= E48), H69 (= H71), L108 (≠ P110), L109 (= L111), T110 (= T112), N111 (vs. gap), H280 (≠ P281), G400 (= G384), D427 (= D411), N454 (= N438), T456 (≠ K440), Y457 (= Y441), A459 (≠ I443), L460 (= L444)
- binding calcium ion: D427 (= D411), N454 (= N438), T456 (≠ K440)
- binding 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-{(S)-hydroxy[(R)-hydroxy(methoxy)phosphoryl]phenylmethyl}-5-(2-{[(R)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium: H280 (≠ P281), T376 (≠ V360), S377 (= S361), F396 (≠ Q380), G400 (= G384), L402 (≠ I386), G426 (≠ A410), D427 (= D411), G428 (= G412), S429 (= S413), Y432 (= Y416), T456 (≠ K440), Y457 (= Y441), G458 (≠ A442), A459 (≠ I443), L460 (= L444), F463 (≠ L448)
Sites not aligning to the query:
1mczA Benzoylformate decarboxylase from pseudomonas putida complexed with an inhibitor, r-mandelate (see paper)
29% identity, 97% coverage: 15:510/512 of query aligns to 15:520/524 of 1mczA
- active site: N22 (= N22), G24 (= G24), S25 (≠ T25), N26 (≠ S26), E27 (= E27), E46 (= E48), H69 (= H71), L108 (≠ P110), L109 (= L111), T110 (= T112), N111 (vs. gap), Y159 (≠ W164), P253 (vs. gap), H280 (≠ P281), S375 (= S359), G400 (= G384), L402 (≠ I386), D427 (= D411), N454 (= N438), T456 (≠ K440), Y457 (= Y441), A459 (≠ I443), L460 (= L444), F463 (≠ L448)
- binding magnesium ion: N116 (≠ G117), L117 (≠ W118), R119 (= R120), D427 (= D411), N454 (= N438), T456 (≠ K440)
- binding (r)-mandelic acid: S25 (≠ T25), H69 (= H71), L109 (= L111), H280 (≠ P281), T376 (≠ V360), F463 (≠ L448)
- binding thiamine diphosphate: N22 (= N22), P23 (= P23), E46 (= E48), H69 (= H71), T376 (≠ V360), S377 (= S361), G400 (= G384), L402 (≠ I386), G426 (≠ A410), D427 (= D411), G428 (= G412), S429 (= S413), Y432 (= Y416), Y457 (= Y441), G458 (≠ A442), A459 (≠ I443), L460 (= L444)
Sites not aligning to the query:
3fznA Intermediate analogue in benzoylformate decarboxylase (see paper)
29% identity, 97% coverage: 15:510/512 of query aligns to 15:520/523 of 3fznA
- active site: N22 (= N22), G24 (= G24), S25 (≠ T25), N26 (≠ S26), E27 (= E27), E46 (= E48), H69 (= H71), L108 (≠ P110), L109 (= L111), T110 (= T112), N111 (vs. gap), Y159 (≠ W164), P253 (vs. gap), H280 (≠ P281), S375 (= S359), G400 (= G384), L402 (≠ I386), D427 (= D411), N454 (= N438), T456 (≠ K440), Y457 (= Y441), A459 (≠ I443), L460 (= L444), F463 (≠ L448)
- binding 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-{(S)-hydroxy[(R)-hydroxy(methoxy)phosphoryl]phenylmethyl}-5-(2-{[(R)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium: N22 (= N22), P23 (= P23), G24 (= G24), S25 (≠ T25), E46 (= E48), H69 (= H71), H280 (≠ P281), T376 (≠ V360), S377 (= S361), G400 (= G384), L402 (≠ I386), G426 (≠ A410), D427 (= D411), G428 (= G412), S429 (= S413), Y432 (= Y416), N454 (= N438), T456 (≠ K440), Y457 (= Y441), G458 (≠ A442), A459 (≠ I443)
- binding magnesium ion: D427 (= D411), N454 (= N438), T456 (≠ K440)
- binding phosphate ion: Q286 (≠ P287), L288 (vs. gap), K289 (vs. gap), P290 (= P289)
1bfdA Benzoylformate decarboxylase from pseudomonas putida (see paper)
29% identity, 97% coverage: 15:510/512 of query aligns to 15:520/523 of 1bfdA
- active site: N22 (= N22), G24 (= G24), S25 (≠ T25), N26 (≠ S26), E27 (= E27), E46 (= E48), H69 (= H71), L108 (≠ P110), L109 (= L111), T110 (= T112), N111 (vs. gap), Y159 (≠ W164), P253 (vs. gap), H280 (≠ P281), S375 (= S359), G400 (= G384), L402 (≠ I386), D427 (= D411), N454 (= N438), T456 (≠ K440), Y457 (= Y441), A459 (≠ I443), L460 (= L444), F463 (≠ L448)
- binding calcium ion: D427 (= D411), N454 (= N438), T456 (≠ K440)
- binding magnesium ion: N116 (≠ G117), L117 (≠ W118), R119 (= R120)
- binding thiamine diphosphate: T376 (≠ V360), S377 (= S361), L402 (≠ I386), G426 (≠ A410), D427 (= D411), G428 (= G412), S429 (= S413), Y432 (= Y416), T456 (≠ K440), Y457 (= Y441), G458 (≠ A442), A459 (≠ I443), L460 (= L444)
3f6bX Crystal structure of benzoylformate decarboxylase in complex with the pyridyl inhibitor paa (see paper)
29% identity, 97% coverage: 15:510/512 of query aligns to 15:520/525 of 3f6bX
- active site: G24 (= G24), E46 (= E48), L108 (≠ P110), L109 (= L111), T110 (= T112), N111 (vs. gap), G400 (= G384), D427 (= D411), N454 (= N438), T456 (≠ K440), Y457 (= Y441), A459 (≠ I443), L460 (= L444)
- binding 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-(2-{[(S)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-2-[(1S,2E)-1-hydroxy-3-pyridin-3-ylprop-2-en-1-yl]-4-methyl-1,3-thiazol-3-ium: N22 (= N22), P23 (= P23), G24 (= G24), S25 (≠ T25), E46 (= E48), H69 (= H71)
Sites not aligning to the query:
1pi3A E28q mutant benzoylformate decarboxylase from pseudomonas putida
28% identity, 97% coverage: 15:510/512 of query aligns to 15:520/523 of 1pi3A
- active site: N22 (= N22), G24 (= G24), S25 (≠ T25), N26 (≠ S26), Q27 (≠ E27), E46 (= E48), H69 (= H71), L108 (≠ P110), L109 (= L111), T110 (= T112), N111 (vs. gap), Y159 (≠ W164), P253 (vs. gap), H280 (≠ P281), S375 (= S359), G400 (= G384), L402 (≠ I386), D427 (= D411), N454 (= N438), T456 (≠ K440), Y457 (= Y441), A459 (≠ I443), L460 (= L444), F463 (≠ L448)
- binding calcium ion: D427 (= D411), N454 (= N438), T456 (≠ K440)
- binding magnesium ion: N116 (≠ G117), L117 (≠ W118), R119 (= R120)
- binding 2-{3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4-methyl-2-oxo-2,3-dihydro-1,3-thiazol-5-yl}ethyl trihydrogendiphosphate: T376 (≠ V360), S377 (= S361), L402 (≠ I386), G426 (≠ A410), G428 (= G412), S429 (= S413), Y432 (= Y416), N454 (= N438), T456 (≠ K440), Y457 (= Y441), G458 (≠ A442), A459 (≠ I443), L460 (= L444)
6qsiA Pseudomonas fluorescens pf-5 thiamine diphosphate-dependent 4- hydroxybenzoylformate decarboxylase (see paper)
29% identity, 97% coverage: 15:510/512 of query aligns to 15:520/525 of 6qsiA
- active site: N22 (= N22), G24 (= G24), S25 (≠ T25), N26 (≠ S26), E27 (= E27), E46 (= E48), H69 (= H71), M108 (≠ P110), L109 (= L111), A110 (vs. gap), Y159 (≠ S160), P253 (≠ R257), H280 (≠ P281), S375 (= S359), G400 (= G384), L402 (≠ I386), Y457 (= Y441), A459 (≠ I443), L460 (= L444), F463 (≠ L448)
- binding thiamine diphosphate: N22 (= N22), P23 (= P23), E46 (= E48), H69 (= H71), T376 (≠ V360), S377 (= S361), L402 (≠ I386), G426 (≠ A410), G428 (= G412), S429 (= S413), Y432 (= Y416), N454 (= N438), T456 (≠ K440), Y457 (= Y441), G458 (≠ A442), A459 (≠ I443), L460 (= L444)
7orxCCC jostii RHA1 thiamine diphosphate-dependent 4-hydroxybenzoylformate decarboxylase
28% identity, 99% coverage: 4:510/512 of query aligns to 8:524/531 of 7orxCCC
- active site: N26 (= N22), G28 (= G24), S29 (≠ T25), N30 (≠ S26), E31 (= E27), E50 (= E48), H73 (= H71), M112 (≠ P110), L113 (= L111), S114 (≠ T112), N115 (vs. gap), Y163 (≠ S160), P257 (vs. gap), H284 (≠ P281), S379 (= S359), G404 (= G384), L406 (≠ I386), D431 (= D411), N458 (= N438), T460 (≠ K440), Y461 (= Y441), A463 (≠ I443), L464 (= L444), F467 (vs. gap)
- binding thiamine diphosphate: N26 (= N22), S29 (≠ T25), E50 (= E48), H73 (= H71), T380 (≠ V360), S381 (= S361), G404 (= G384), L406 (≠ I386), G430 (≠ A410), G432 (= G412), S433 (= S413), Y436 (= Y416), N458 (= N438), T460 (≠ K440), Y461 (= Y441), G462 (≠ A442)
4q9dB X-ray structure of a putative thiamin diphosphate-dependent enzyme isolated from mycobacterium smegmatis (see paper)
29% identity, 97% coverage: 11:508/512 of query aligns to 13:513/519 of 4q9dB
- active site: N24 (= N22), G26 (= G24), S27 (≠ T25), T28 (≠ S26), E29 (= E27), Q47 (≠ F47), E48 (= E48), H71 (= H71), V107 (≠ F107), D108 (= D108), Y110 (≠ P110), L111 (= L111), N112 (≠ T112), N113 (vs. gap), L161 (≠ S160), P252 (≠ A256), Y279 (= Y280), M374 (≠ E357), S376 (= S359), G401 (= G384), I403 (= I386), D432 (= D411), N459 (= N438), E461 (≠ K440), Y462 (= Y441), I464 (= I443)
- binding magnesium ion: D432 (= D411), N459 (= N438), E461 (≠ K440)
Sites not aligning to the query:
4k9qA The crystal structure of benzoylformate decarboxylase from polynucleobacter necessarius
24% identity, 97% coverage: 11:508/512 of query aligns to 12:520/531 of 4k9qA
- active site: N23 (= N22), G25 (= G24), S26 (≠ T25), T27 (≠ S26), E28 (= E27), E47 (= E48), H70 (= H71), N106 (≠ D108), E107 (≠ A109), L110 (≠ T112), T111 (≠ A113), L160 (≠ S160), T251 (≠ A256), Y278 (= Y280), V370 (= V356), C373 (≠ S359), G398 (= G384), L400 (≠ I386), D429 (= D411), N456 (= N438), E458 (≠ K440), Y459 (= Y441), G460 (≠ A442), I461 (= I443), L462 (= L445), F465 (≠ L448)
- binding magnesium ion: D429 (= D411), N456 (= N438), E458 (≠ K440)
- binding thiamine diphosphate: P374 (≠ V360), S375 (= S361), L400 (≠ I386), G428 (≠ A410), D429 (= D411), G430 (= G412), S431 (= S413), Y434 (= Y416), N456 (= N438), E458 (≠ K440), Y459 (= Y441), G460 (≠ A442), I461 (= I443), L462 (= L445)
Sites not aligning to the query:
P23234 Indole-3-pyruvate decarboxylase; Indolepyruvate decarboxylase; EC 4.1.1.74 from Enterobacter cloacae (see paper)
25% identity, 86% coverage: 4:443/512 of query aligns to 8:467/552 of P23234
- E52 (= E48) binding
- D435 (= D411) binding
- N462 (= N438) binding
1ovmA Crystal structure of indolepyruvate decarboxylase from enterobacter cloacae (see paper)
26% identity, 86% coverage: 4:443/512 of query aligns to 6:451/535 of 1ovmA
- active site: G26 (= G24), D27 (≠ T25), Y28 (≠ S26), N29 (≠ E27), E50 (= E48), T72 (≠ H71), H113 (≠ Y103), H114 (= H104), L116 (≠ P106), G117 (≠ F107), A167 (≠ S160), S262 (≠ D254), L289 (≠ F277), Q367 (≠ E358), G392 (= G384), I394 (= I386), D419 (= D411), N446 (= N438), G448 (≠ K440), V451 (≠ I443)
- binding magnesium ion: D419 (= D411), N446 (= N438), G448 (≠ K440)
- binding thiamine diphosphate: P25 (= P23), E50 (= E48), V75 (≠ P74), T369 (≠ V360), G392 (= G384), S393 (≠ A385), I394 (= I386), G418 (≠ A410), G420 (= G412), A421 (≠ S413), N446 (= N438), G448 (≠ K440), Y449 (= Y441), T450 (≠ A442), V451 (≠ I443)
Sites not aligning to the query:
6wo1A Hybrid acetohydroxyacid synthase complex structure with cryptococcus neoformans ahas catalytic subunit and saccharomyces cerevisiae ahas regulatory subunit (see paper)
25% identity, 44% coverage: 1:224/512 of query aligns to 9:234/551 of 6wo1A
- active site: Y30 (≠ N22), G32 (= G24), G33 (≠ T25), A34 (≠ S26), I35 (≠ E27), E56 (= E48), T79 (≠ H71), F118 (≠ P110), Q119 (≠ L111), E120 (≠ T112), K168 (≠ S160)
- binding flavin-adenine dinucleotide: D97 (≠ A89), R158 (≠ P150), G208 (= G206), G210 (≠ A208), S213 (≠ E211)
Sites not aligning to the query:
- active site: 255, 282, 398, 424, 426, 451, 478
- binding 2-methylpyrimidin-4-amine: 424, 425, 426
- binding diphosphate: 398, 399, 400, 401, 450, 451, 452, 453
- binding flavin-adenine dinucleotide: 235, 236, 237, 253, 254, 255, 275, 276, 277, 279, 281, 282, 308, 309, 327, 328, 402, 421, 422
- binding magnesium ion: 451, 478
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)
27% identity, 42% coverage: 296:512/512 of query aligns to 419:635/664 of P09114
- W568 (vs. gap) mutation to L: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with A-191.
Sites not aligning to the query:
- 191 P→A: In S4-Hra; highly resistant to sulfonylurea herbicides; when associated with L-568.
7tzzA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase p197t mutant in complex with bispyribac-sodium (see paper)
25% identity, 41% coverage: 2:210/512 of query aligns to 13:227/582 of 7tzzA
Sites not aligning to the query:
- binding 2,6-bis[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid: 266, 292, 489, 568
- 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: 400, 401, 402, 403, 426, 428, 452, 453, 454, 455, 483, 484, 485, 486
- binding flavin-adenine dinucleotide: 246, 247, 248, 263, 264, 266, 267, 286, 288, 293, 310, 311, 329, 330, 405, 423
- binding magnesium ion: 381, 453, 458, 461, 480, 482, 533
P17597 Acetolactate synthase, chloroplastic; AtALS; Acetohydroxy-acid synthase; Protein CHLORSULFURON RESISTANT 1; EC 2.2.1.6 from Arabidopsis thaliana (Mouse-ear cress) (see 8 papers)
38% identity, 19% coverage: 2:98/512 of query aligns to 98:194/670 of P17597
- A122 (≠ S26) mutation to V: Reduced catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides.
- M124 (= M28) mutation to E: Reduced catalytic activity. Resistant to imidazolinone herbicides and reduced sensitivity to sulfonylurea herbicides.; mutation to I: No effect on catalytic activity. Increased resistance to imidazolinone herbicides.
- E144 (= E48) binding
- S186 (≠ Q90) binding
Sites not aligning to the query:
- 197 P→S: In csr1-1/GH50; resistant to sulfonylurea but not to imidazolinone herbicides.
- 199 mutation R->A,E: No effect on catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides.
- 207 binding
- 220 binding
- 246 binding ; binding
- 256 binding
- 308 binding
- 331:332 binding
- 340 modified: Cysteine sulfinic acid (-SO2H)
- 349:352 binding
- 371:375 binding
- 376:377 binding
- 395:396 binding
- 414:415 binding
- 487:488 binding
- 508:509 binding
- 511:513 binding
- 538 binding
- 538:540 binding
- 565 binding
- 565:570 binding
- 567 binding
- 574 binding ; W→L: Increased catalytic activity. Resistant to imidazolinone and sulfonylurea herbicides.; W→S: Slightly decreased catalytic activity. Resistant to imidazolinone and sulfonylurea herbicides.
- 653 binding ; S→A: No effect on catalytic activity or sensitivity to herbicides.; S→F: No effect on catalytic activity. Resistant to imidazolinone herbicides and also slightly sulfonylurea-resistant.; S→N: In csr1-2/GH90; no effect on catalytic activity. Resistant to imidazolinone but not to sulfonylurea herbicides.; S→T: No effect on catalytic activity. Resistant to imidazolinone herbicides but not to sulfonylurea herbicides.
5k3sA Crystal structure of arabidopsis thaliana acetohydroxyacid synthase in complex with a pyrimidinyl-benzoate herbicide, bispyribac-sodium (see paper)
38% identity, 19% coverage: 2:98/512 of query aligns to 13:109/583 of 5k3sA
Sites not aligning to the query:
- active site: 121, 122, 123, 171, 266, 293, 400, 426, 428, 453, 480, 482, 483, 485, 486, 489, 558
- binding 2,6-bis[(4,6-dimethoxypyrimidin-2-yl)oxy]benzoic acid: 292, 485, 489, 569
- binding flavin-adenine dinucleotide: 161, 222, 223, 224, 246, 247, 248, 264, 266, 286, 288, 290, 293, 310, 311, 329, 330, 405, 423
- binding magnesium ion: 453, 480, 482
- binding (3z)-4-{[(4-amino-2-methylpyrimidin-5-yl)methyl]amino}-3-mercaptopent-3-en-1-yl trihydrogen diphosphate: 400, 401, 402, 403, 426, 428, 453, 454, 455, 480, 482, 483, 484, 485, 486
8et4A Crystal structure of wild-type arabidopsis thaliana acetohydroxyacid synthase in complex with amidosulfuron (see paper)
38% identity, 19% coverage: 2:98/512 of query aligns to 13:109/582 of 8et4A
Sites not aligning to the query:
- 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: 400, 401, 402, 403, 426, 428, 452, 453, 454, 455, 458, 480, 482, 483, 484, 485, 486
- binding flavin-adenine dinucleotide: 161, 222, 223, 224, 246, 247, 248, 264, 266, 267, 286, 287, 288, 290, 292, 293, 310, 311, 329, 330, 405, 423
- binding magnesium ion: 370, 453, 458, 461, 480, 482, 533
- binding N-{[(4,6-dimethoxypyrimidin-2-yl)carbamoyl]sulfamoyl}-N-methylmethanesulfonamide: 266, 292, 485, 489, 568
Query Sequence
>RR42_RS36655 FitnessBrowser__Cup4G11:RR42_RS36655
MNGAESLVKTLLACGVDTCFANPGTSEMHFVAALDRIPGMRCVLGLFEGVVTGAADGYAR
MADKPAATLLHCGPGLANGLANLHNARRAQTPVINIVGDQATYHRPFDAPLTADTEGWAR
PVSVWTRTATDAASVGADAATAVQAACAAPGGVASLILPSDVCWDAGGKVGVPLAPLPVP
KVSPDAVQQAARLLRSGQPTLIVLAGTALREVPLADAHRIAAATDARLITPMSNARVSRG
RGRFNVDRVPYSGDVARDKLAGIRNVILVGAPPPVTFFAYPGKSPRPYPEDAEIHVLARP
EQDLAEALARLADELGAPSVSVPASVAPRGIAKGAVTSEAVAQTLTALLPEQAIVVEESV
SFGRAFYPGTVHAAPHDWLQLTGGAIGDGLPLATGAAVAAPGRRVVALQADGSGMYTLQS
LWTMAREKLDVTVVILANRKYAILLGELAGVGANPGKTALDMLDIGNPDLDWVQLANGMG
VEAARAEDMERFAELFGMANGRRGPFVIELVI
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