SitesBLAST
Comparing N515DRAFT_1617 FitnessBrowser__Dyella79:N515DRAFT_1617 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)
6efhA Pyruvate decarboxylase from kluyveromyces lactis soaked with pyruvamide
28% identity, 96% coverage: 23:586/590 of query aligns to 1:550/557 of 6efhA
- active site: L24 (≠ I46), G26 (= G48), D27 (= D49), F28 (≠ Y50), N29 (≠ V51), E50 (= E72), T72 (≠ Q94), H113 (= H139), H114 (= H140), L116 (≠ T142), G117 (= G143), A168 (≠ K192), T265 (≠ A288), N292 (≠ Y315), T387 (≠ V417), G412 (≠ Q447), I414 (= I449), D443 (= D473), N470 (= N500), G472 (≠ V502), Y473 (= Y503), I475 (= I505), E476 (= E506), I479 (≠ Y509), T541 (≠ Q577)
- binding magnesium ion: D443 (= D473), N470 (= N500), G472 (≠ V502)
- binding (1S,2S)-1-amino-1,2-dihydroxypropan-1-olate: H91 (≠ R113), C220 (≠ E243), H224 (≠ F247), G285 (= G308), A286 (= A309), H309 (vs. gap), S310 (≠ A329)
- binding thiamine diphosphate: P25 (= P47), E50 (= E72), V75 (= V97), G388 (≠ M418), T389 (= T419), G412 (≠ Q447), I414 (= I449), G444 (= G474), S445 (≠ G475), N470 (= N500), G472 (≠ V502), Y473 (= Y503), T474 (≠ A504), E476 (= E506)
2vjyA Pyruvate decarboxylase from kluyveromyces lactis in complex with the substrate analogue methyl acetylphosphonate (see paper)
28% identity, 95% coverage: 25:586/590 of query aligns to 3:550/562 of 2vjyA
- active site: L24 (≠ I46), G26 (= G48), D27 (= D49), F28 (≠ Y50), N29 (≠ V51), E50 (= E72), T72 (≠ Q94), H113 (= H139), H114 (= H140), L116 (≠ T142), G117 (= G143), A168 (≠ K192), T265 (≠ A288), N292 (≠ Y315), T387 (≠ V417), G412 (≠ Q447), I414 (= I449), D443 (= D473), N470 (= N500), G472 (≠ V502), Y473 (= Y503), I475 (= I505), E476 (= E506), I479 (≠ Y509), T541 (≠ Q577)
- binding methoxy-[(1~{R})-1-oxidanylethyl]phosphinic acid: G26 (= G48), D27 (= D49), H91 (≠ R113), H113 (= H139), H114 (= H140), C220 (≠ E243), H224 (≠ F247), G285 (= G308), A286 (= A309), F291 (≠ D314), H309 (vs. gap), S310 (≠ A329), E476 (= E506), I479 (≠ Y509)
- binding methyl hydrogen (s)-acetylphosphonate: E17 (≠ N39), K64 (≠ R86), Y156 (≠ I180)
- binding magnesium ion: D443 (= D473), N470 (= N500), G472 (≠ V502)
- binding thiamine diphosphate: P25 (= P47), E50 (= E72), V75 (= V97), T389 (= T419), G412 (≠ Q447), S413 (≠ C448), I414 (= I449), G442 (= G472), G444 (= G474), S445 (≠ G475), N470 (= N500), G472 (≠ V502), Y473 (= Y503), T474 (≠ A504), I475 (= I505), E476 (= E506)
P23234 Indole-3-pyruvate decarboxylase; Indolepyruvate decarboxylase; EC 4.1.1.74 from Enterobacter cloacae (see paper)
28% identity, 94% coverage: 25:581/590 of query aligns to 5:536/552 of P23234
- E52 (= E72) binding
- D435 (= D473) binding
- N462 (= N500) binding
2vbgA The complex structure of the branched-chain keto acid decarboxylase (kdca) from lactococcus lactis with 2r-1-hydroxyethyl-deazathdp (see paper)
27% identity, 96% coverage: 25:588/590 of query aligns to 7:538/546 of 2vbgA
- active site: V28 (≠ I46), G30 (= G48), D31 (= D49), Y32 (= Y50), N33 (≠ V51), N53 (= N71), E54 (= E72), T76 (≠ Q94), F115 (= F138), V116 (≠ H139), H117 (= H140), H118 (≠ S141), L120 (vs. gap), A121 (vs. gap), V171 (≠ K192), K259 (≠ A288), S286 (≠ Y315), E375 (≠ T419), Q376 (≠ Y420), G401 (≠ Q447), I403 (= I449), D428 (= D473), N455 (= N500), G457 (≠ V502), Y458 (= Y503), V460 (≠ I505), E461 (= E506), K527 (≠ Q577)
- binding magnesium ion: D428 (= D473), N455 (= N500), G457 (≠ V502)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-[(1r)-1-hydroxyethyl]-3-methyl-2-thienyl}ethyl trihydrogen diphosphate: P29 (= P47), E54 (= E72), V79 (= V97), H118 (≠ S141), G377 (= G421), T378 (≠ S424), G401 (≠ Q447), S402 (≠ C448), I403 (= I449), G427 (= G472), G429 (= G474), S430 (≠ G475), N455 (= N500), G457 (≠ V502), Y458 (= Y503), T459 (≠ A504), V460 (≠ I505), E461 (= E506)
2vbfB The holostructure of the branched-chain keto acid decarboxylase (kdca) from lactococcus lactis (see paper)
27% identity, 96% coverage: 25:588/590 of query aligns to 7:538/546 of 2vbfB
- active site: V28 (≠ I46), G30 (= G48), D31 (= D49), Y32 (= Y50), N33 (≠ V51), N53 (= N71), E54 (= E72), T76 (≠ Q94), F115 (= F138), V116 (≠ H139), H117 (= H140), H118 (≠ S141), L120 (vs. gap), A121 (vs. gap), V171 (≠ K192), K259 (≠ A288), S286 (≠ Y315), E375 (≠ T419), Q376 (≠ Y420), G401 (≠ Q447), I403 (= I449), D428 (= D473), N455 (= N500), G457 (≠ V502), Y458 (= Y503), V460 (≠ I505), E461 (= E506), K527 (≠ Q577)
- binding magnesium ion: D428 (= D473), N455 (= N500), G457 (≠ V502)
- binding thiamine diphosphate: P29 (= P47), E54 (= E72), V79 (= V97), G377 (= G421), T378 (≠ S424), G401 (≠ Q447), S402 (≠ C448), I403 (= I449), G427 (= G472), G429 (= G474), S430 (≠ G475), N455 (= N500), G457 (≠ V502), Y458 (= Y503), T459 (≠ A504), V460 (≠ I505), E461 (= E506)
6vgsBBB Alpha-keto acid decarboxylase (see paper)
25% identity, 96% coverage: 25:588/590 of query aligns to 2:534/543 of 6vgsBBB
- active site: V23 (≠ I46), G25 (= G48), D26 (= D49), Y27 (= Y50), N28 (≠ V51), E49 (= E72), T71 (≠ Q94), H112 (= H139), H113 (= H140), L115 (≠ T142), A116 (vs. gap), V166 (≠ K192), S282 (≠ Y315), Q372 (≠ Y420), G397 (≠ Q447), I399 (= I449), D424 (= D473), N451 (= N500), G453 (≠ V502), Y454 (= Y503), V456 (≠ I505), E457 (= E506)
- binding magnesium ion: D424 (= D473), N451 (= N500), G453 (≠ V502)
- binding thiamine diphosphate: P24 (= P47), E49 (= E72), V74 (= V97), T374 (≠ S424), I399 (= I449), G423 (= G472), G425 (= G474), S426 (≠ G475), N451 (= N500), G453 (≠ V502), Y454 (= Y503), T455 (≠ A504), V456 (≠ I505), E457 (= E506)
P06169 Pyruvate decarboxylase isozyme 1; Thiamine pyrophosphate-dependent 2-oxo-acid decarboxylase; 2ODC; EC 4.1.1.-; EC 4.1.1.43; EC 4.1.1.72; EC 4.1.1.74 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 5 papers)
27% identity, 95% coverage: 25:584/590 of query aligns to 4:549/563 of P06169
- R161 (= R184) modified: Omega-N-methylarginine
- D291 (= D313) mutation to N: In PDC1-8; reduces catalytic activity to 10% but retains autoregulatory activity.
- T390 (≠ V417) binding
- GSI 413:415 (≠ QCI 447:449) binding
- D444 (= D473) binding
- GS 445:446 (≠ GG 474:475) binding
- N471 (= N500) binding
- NDGYTI 471:476 (≠ NQVYAI 500:505) binding
- G473 (≠ V502) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylserine
1qpbA Pyruvate decarboyxlase from yeast (form b) complexed with pyruvamide (see paper)
27% identity, 95% coverage: 23:584/590 of query aligns to 1:548/555 of 1qpbA
- active site: L24 (≠ I46), G26 (= G48), D27 (= D49), F28 (≠ Y50), N29 (≠ V51), E50 (= E72), T72 (≠ Q94), H113 (= H139), H114 (= H140), L116 (≠ T142), G117 (= G143), A168 (≠ K192), T265 (≠ A288), N292 (≠ Y315), T387 (≠ D415), G412 (≠ Q447), I414 (= I449), D443 (= D473), N470 (= N500), G472 (≠ V502), Y473 (= Y503), I475 (= I505), E476 (= E506), I479 (≠ Y509), V541 (≠ Q577)
- binding magnesium ion: D443 (= D473), N470 (= N500), G472 (≠ V502)
- binding pyruvamide: Y156 (≠ I180), H224 (≠ F247), D225 (≠ G248)
- binding thiamine diphosphate: P25 (= P47), E50 (= E72), V75 (= V97), T389 (≠ V417), I414 (= I449), G442 (= G472), G444 (= G474), S445 (≠ G475), N470 (= N500), G472 (≠ V502), Y473 (= Y503), T474 (≠ A504), I475 (= I505), E476 (= E506)
1ovmA Crystal structure of indolepyruvate decarboxylase from enterobacter cloacae (see paper)
27% identity, 94% coverage: 25:581/590 of query aligns to 3:520/535 of 1ovmA
- active site: G26 (= G48), D27 (= D49), Y28 (= Y50), N29 (≠ V51), E50 (= E72), T72 (≠ Q94), H113 (= H139), H114 (= H140), L116 (≠ T142), G117 (= G143), A167 (≠ K192), S262 (≠ A288), L289 (≠ F318), Q367 (≠ Y420), G392 (≠ Q447), I394 (= I449), D419 (= D473), N446 (= N500), G448 (≠ V502), V451 (≠ I505), E452 (= E506), I455 (≠ Y509), K516 (≠ Q577)
- binding magnesium ion: D419 (= D473), N446 (= N500), G448 (≠ V502)
- binding thiamine diphosphate: P25 (= P47), E50 (= E72), V75 (= V97), T369 (≠ V422), G392 (≠ Q447), S393 (≠ C448), I394 (= I449), G418 (= G472), G420 (= G474), A421 (≠ G475), N446 (= N500), G448 (≠ V502), Y449 (= Y503), T450 (≠ A504), V451 (≠ I505), E452 (= E506)
2w93A Crystal structure of the saccharomyces cerevisiae pyruvate decarboxylase variant e477q in complex with the surrogate pyruvamide
28% identity, 95% coverage: 25:584/590 of query aligns to 3:534/544 of 2w93A
- active site: L24 (≠ I46), G26 (= G48), D27 (= D49), F28 (≠ Y50), N29 (≠ V51), E50 (= E72), T72 (≠ Q94), H113 (= H139), H114 (= H140), L116 (≠ T142), G117 (= G143), A168 (≠ K192), T265 (≠ A288), T373 (≠ D415), G398 (≠ Q447), I400 (= I449), D429 (= D473), N456 (= N500), G458 (≠ V502), Y459 (= Y503), I461 (= I505), Q462 (≠ E506), I465 (≠ Y509), V527 (≠ Q577)
- binding magnesium ion: D429 (= D473), N456 (= N500), G458 (≠ V502)
- binding (1S,2S)-1-amino-1,2-dihydroxypropan-1-olate: D27 (= D49), H114 (= H140), C220 (≠ E243), H224 (≠ F247), G285 (= G308), A286 (= A309), H295 (≠ L328), S296 (≠ A329)
- binding thiamine diphosphate: P25 (= P47), E50 (= E72), V75 (= V97), T375 (≠ V417), S399 (≠ C448), I400 (= I449), G428 (= G472), G430 (= G474), S431 (≠ G475), N456 (= N500), G458 (≠ V502), Y459 (= Y503), T460 (≠ A504), I461 (= I505), Q462 (≠ E506)
6efgD Pyruvate decarboxylase from kluyveromyces lactis
28% identity, 95% coverage: 25:586/590 of query aligns to 3:529/537 of 6efgD
- active site: L24 (≠ I46), G26 (= G48), D27 (= D49), F28 (≠ Y50), N29 (≠ V51), E50 (= E72), T72 (≠ Q94), H104 (≠ D126), L106 (≠ R128), G107 (≠ D129), A158 (≠ K192), T255 (≠ A288), T366 (≠ V417), G391 (≠ Q447), I393 (= I449), D422 (= D473), N449 (= N500), G451 (≠ V502), Y452 (= Y503), I454 (= I505), E455 (= E506), I458 (≠ Y509), T520 (≠ Q577)
- binding magnesium ion: D422 (= D473), N449 (= N500), G451 (≠ V502)
- binding thiamine diphosphate: P25 (= P47), E50 (= E72), V75 (= V97), T368 (= T419), I393 (= I449), G421 (= G472), G423 (= G474), S424 (≠ G475), N449 (= N500), G451 (≠ V502), Y452 (= Y503), T453 (≠ A504), I454 (= I505), E455 (= E506)
Q92345 Probable pyruvate decarboxylase C1F8.07c; EC 4.1.1.1 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
27% identity, 96% coverage: 23:588/590 of query aligns to 7:554/569 of Q92345
- S233 (≠ G251) modified: Phosphoserine
- T521 (≠ N555) modified: Phosphothreonine
- S522 (≠ A556) modified: Phosphoserine
2vk1A Crystal structure of the saccharomyces cerevisiae pyruvate decarboxylase variant d28a in complex with its substrate (see paper)
27% identity, 95% coverage: 25:584/590 of query aligns to 3:548/562 of 2vk1A
- active site: L24 (≠ I46), G26 (= G48), A27 (≠ D49), F28 (≠ Y50), N29 (≠ V51), E50 (= E72), T72 (≠ Q94), H113 (= H139), H114 (= H140), L116 (≠ T142), G117 (= G143), A168 (≠ K192), T265 (≠ A288), N292 (≠ Y315), T387 (≠ D415), G412 (≠ Q447), I414 (= I449), D443 (= D473), N470 (= N500), G472 (≠ V502), Y473 (= Y503), I475 (= I505), E476 (= E506), I479 (≠ Y509), V541 (≠ Q577)
- binding magnesium ion: D443 (= D473), N470 (= N500), G472 (≠ V502)
- binding pyruvic acid: A27 (≠ D49), H114 (= H140), C220 (≠ E243), G285 (= G308), A286 (= A309), H309 (vs. gap), S310 (≠ A329)
- binding thiamine diphosphate: P25 (= P47), E50 (= E72), V75 (= V97), G388 (≠ I416), T389 (≠ V417), I414 (= I449), G442 (= G472), G444 (= G474), S445 (≠ G475), N470 (= N500), G472 (≠ V502), Y473 (= Y503), T474 (≠ A504), I475 (= I505), E476 (= E506)
8hp4A Ctpdc complex
28% identity, 95% coverage: 23:584/590 of query aligns to 1:529/540 of 8hp4A
- binding magnesium ion: D423 (= D473), N451 (= N500), G453 (≠ V502)
- binding thiamine diphosphate: P25 (= P47), E50 (= E72), V77 (= V97), T369 (= T430), S393 (≠ C448), I394 (= I449), G422 (= G472), G424 (= G474), S425 (≠ G475), N451 (= N500), G453 (≠ V502), Y454 (= Y503), T455 (≠ A504), I456 (= I505)
5npuA Inferred ancestral pyruvate decarboxylase (see paper)
26% identity, 96% coverage: 24:590/590 of query aligns to 1:535/547 of 5npuA
- binding magnesium ion: D425 (= D473), N452 (= N500)
- binding thiamine diphosphate: D375 (≠ S425), G398 (≠ Q447), H399 (≠ C448), I400 (= I449), G424 (= G472), D425 (= D473), S427 (≠ G475), N452 (= N500), G454 (≠ V502), Y455 (= Y503), T456 (≠ A504), I457 (= I505), E458 (= E506)
2vbiA Holostructure of pyruvate decarboxylase from acetobacter pasteurianus
26% identity, 96% coverage: 24:590/590 of query aligns to 1:545/554 of 2vbiA
- active site: G25 (= G48), D26 (= D49), Y27 (= Y50), N28 (≠ V51), E49 (= E72), T71 (≠ Q94), H112 (= H139), H113 (= H140), I115 (≠ T142), G116 (= G143), C167 (≠ K192), S290 (≠ L316), T383 (≠ V422), G408 (≠ Q447), I410 (= I449), D435 (= D473), N462 (= N500), G464 (≠ V502), Y465 (= Y503), I467 (= I505), E468 (= E506), R532 (≠ Q577)
- binding magnesium ion: D435 (= D473), N462 (= N500), G464 (≠ V502)
- binding thiamine diphosphate: A24 (≠ P47), E49 (= E72), V74 (= V97), D385 (≠ S424), G408 (≠ Q447), H409 (≠ C448), I410 (= I449), G434 (= G472), D435 (= D473), G436 (= G474), S437 (≠ G475), N462 (= N500), G464 (≠ V502), Y465 (= Y503), V466 (≠ A504), I467 (= I505)
2q5oA X-ray structure of phenylpyruvate decarboxylase in complex with 3- deaza-thdp and phenylpyruvate (see paper)
27% identity, 95% coverage: 27:587/590 of query aligns to 4:525/529 of 2q5oA
- active site: I23 (= I46), G25 (= G48), D26 (= D49), F27 (≠ Y50), A28 (≠ V51), E49 (= E72), T72 (≠ S92), H113 (= H139), H114 (= H140), G116 (≠ T142), R117 (≠ G143), T118 (≠ D144), L119 (= L145), R166 (≠ K192), V258 (≠ A288), N285 (≠ Y315), M373 (≠ L412), A395 (≠ Q447), M397 (≠ I449), D422 (= D473), N449 (= N500), S451 (≠ V502), W452 (≠ Y503), M454 (≠ I505), L455 (≠ M512), F458 (= F515), R515 (≠ Q577)
- binding magnesium ion: D422 (= D473), N449 (= N500), S451 (≠ V502)
- binding 3-phenylpyruvic acid: G25 (= G48), D26 (= D49), R61 (vs. gap), H113 (= H139), H114 (= H140), R215 (≠ L245), R216 (= R246), M239 (≠ L269), G242 (≠ S272), T284 (≠ D314), L388 (≠ F440), M389 (≠ V441), A390 (≠ S442), M454 (≠ I505), F525 (≠ L587)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: P24 (= P47), E49 (= E72), A75 (≠ V97), D375 (≠ S424), M397 (≠ I449), G421 (= G472), D422 (= D473), G423 (= G474), A424 (≠ G475), N449 (= N500), S451 (≠ V502), W452 (≠ Y503), E453 (≠ A504), M454 (≠ I505), L455 (≠ M512)
2q5qA X-ray structure of phenylpyruvate decarboxylase in complex with 3- deaza-thdp and 5-phenyl-2-oxo-valeric acid (see paper)
27% identity, 95% coverage: 27:587/590 of query aligns to 5:530/533 of 2q5qA
- active site: I24 (= I46), G26 (= G48), D27 (= D49), F28 (≠ Y50), A29 (≠ V51), E50 (= E72), T73 (≠ S92), H114 (= H139), H115 (= H140), G117 (≠ T142), R118 (≠ G143), T119 (≠ D144), L120 (= L145), R167 (≠ K192), V259 (≠ A288), N286 (≠ Y315), M378 (≠ L412), A400 (≠ Q447), M402 (≠ I449), D427 (= D473), N454 (= N500), S456 (≠ V502), W457 (≠ Y503), M459 (≠ I505), L460 (≠ M512), F463 (= F515), R520 (≠ Q577)
- binding 5-phenyl-2-keto-valeric acid: G26 (= G48), D27 (= D49), R62 (vs. gap), H114 (= H139), H115 (= H140), R216 (≠ L245), R217 (= R246), M240 (≠ L269), R242 (≠ K271), D284 (= D313), T285 (≠ D314), L373 (= L407), L393 (≠ F440), M394 (≠ V441), A395 (≠ S442), A400 (≠ Q447), M459 (≠ I505), F530 (≠ L587)
- binding magnesium ion: D427 (= D473), N454 (= N500), S456 (≠ V502)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: P25 (= P47), E50 (= E72), A76 (≠ V97), D380 (≠ S424), M402 (≠ I449), G426 (= G472), D427 (= D473), G428 (= G474), A429 (≠ G475), N454 (= N500), S456 (≠ V502), W457 (≠ Y503), E458 (≠ A504), M459 (≠ I505), L460 (≠ M512)
4cokB Functional and structural characterization of pyruvate decarboxylase from gluconoacetobacter diazotrophicus (see paper)
27% identity, 96% coverage: 24:588/590 of query aligns to 2:537/549 of 4cokB
- active site: G26 (= G48), D27 (= D49), Y28 (= Y50), N29 (≠ V51), E50 (= E72), T72 (≠ Q94), H113 (= H139), H114 (= H140), L116 (≠ T142), G117 (= G143), C168 (≠ K192), A284 (≠ L316), E376 (≠ G421), T377 (≠ V422), G402 (≠ Q447), I404 (= I449), D429 (= D473), N456 (= N500), G458 (≠ V502), I461 (= I505), E462 (= E506), R526 (≠ Q577)
- binding magnesium ion: D429 (= D473), N456 (= N500), G458 (≠ V502)
- binding thiamine diphosphate: A25 (≠ P47), E50 (= E72), V75 (= V97), D379 (≠ S424), G402 (≠ Q447), H403 (≠ C448), I404 (= I449), G428 (= G472), G430 (= G474), S431 (≠ G475), N456 (= N500), G458 (≠ V502), Y459 (= Y503), T460 (≠ A504), I461 (= I505), E462 (= E506)
2nxwA Crystal structure of phenylpyruvate decarboxylase of azospirillum brasilense (see paper)
27% identity, 95% coverage: 27:587/590 of query aligns to 10:530/537 of 2nxwA
- active site: I29 (= I46), G31 (= G48), D32 (= D49), F33 (≠ Y50), A34 (≠ V51), E55 (= E72), T78 (≠ S92), R163 (≠ K192), V255 (≠ A288), N282 (≠ Y315), M378 (≠ L412), A400 (≠ Q447), M402 (≠ I449), D427 (= D473), N454 (= N500), S456 (≠ V502), W457 (≠ Y503), M459 (≠ I505), L460 (≠ M512), F463 (= F515), R520 (≠ Q577)
- binding magnesium ion: D427 (= D473), N454 (= N500), S456 (≠ V502)
- binding thiamine diphosphate: P30 (= P47), E55 (= E72), D380 (≠ S424), M402 (≠ I449), G426 (= G472), D427 (= D473), G428 (= G474), A429 (≠ G475), N454 (= N500), S456 (≠ V502), W457 (≠ Y503), E458 (≠ A504), M459 (≠ I505), L460 (≠ M512)
Query Sequence
>N515DRAFT_1617 FitnessBrowser__Dyella79:N515DRAFT_1617
MADSNISNKSRSIATAPASISTATFTVADYLLTRLKQLNVTDVFQIPGDYVKHFTQALEY
FDGVNTIGAINELDAAYAADAYARTRGLAAVSLQFGVSTYSALNAIAGAWVERSPIVVIS
ATPGADMRDITDMYDVLFHHSTGDLNSDRAIYEYVTVKAITLSTNVGAAEQIDELLVDAI
TEKRPVYIACYKEVWGQPCERPPATPLKPRVTRSPELALRNAVDQAWAMITQAKSPLIFA
GVEVLRFGLSGLLQKIIDASGFLYTTTTLGKSVLDEQGDKFIGTYSDAASIEAVREIVMA
SDCVLTLGAIITDDYLTFIEAKYADMVLADTAGVRAGYFKYGDVTMRDFMEALLARFTAS
KAYPIKAKAPPQPKYPQPWAANSDPVYDAQPQIITYNRFFAHTMKFLQDKDLLKDIVMTY
GVSSSMYVATNCYGLKQGSFVSSAAWQCIGFETGAACGAQLGSGKRAWTVAGDGGFMMVC
QSLSTLARNQLNAVIFVMSNQVYAIEQVYVDMSAFKPGPKHKFDAFDILPKWDYLALAKA
FGAEGIRVETVDELNAALPRIAKIKDKPVLVEVVIPQKDLPGQMYRLGSE
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