SitesBLAST
Comparing WP_010960298.1 NCBI__GCF_000008325.1:WP_010960298.1 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)
2q5qA X-ray structure of phenylpyruvate decarboxylase in complex with 3- deaza-thdp and 5-phenyl-2-oxo-valeric acid (see paper)
37% identity, 96% coverage: 9:537/549 of query aligns to 5:530/533 of 2q5qA
- active site: I24 (≠ V28), G26 (= G30), D27 (= D31), F28 (≠ Y32), A29 (≠ V33), E50 (= E53), T73 (= T75), H114 (= H116), H115 (= H117), G117 (≠ F119), R118 (≠ G120), T119 (≠ P121), L120 (≠ F122), R167 (≠ A169), V259 (≠ A263), N286 (≠ D290), M378 (≠ V382), A400 (≠ T407), M402 (= M409), D427 (= D434), N454 (= N461), S456 (≠ G463), W457 (≠ Y464), M459 (≠ T466), L460 (≠ E467), F463 (= F469), R520 (≠ P527)
- binding 5-phenyl-2-keto-valeric acid: G26 (= G30), D27 (= D31), R62 (= R65), H114 (= H116), H115 (= H117), R216 (≠ H220), R217 (= R221), M240 (≠ T244), R242 (≠ K246), D284 (= D288), T285 (≠ V289), L373 (≠ I377), L393 (≠ F400), M394 (≠ L401), A395 (= A402), A400 (≠ T407), M459 (≠ T466), F530 (≠ L537)
- binding magnesium ion: D427 (= D434), N454 (= N461), S456 (≠ G463)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: P25 (= P29), E50 (= E53), A76 (≠ V78), D380 (= D384), M402 (= M409), G426 (= G433), D427 (= D434), G428 (= G435), A429 (= A436), N454 (= N461), S456 (≠ G463), W457 (≠ Y464), E458 (≠ S465), M459 (≠ T466), L460 (≠ E467)
2q5oA X-ray structure of phenylpyruvate decarboxylase in complex with 3- deaza-thdp and phenylpyruvate (see paper)
37% identity, 96% coverage: 9:537/549 of query aligns to 4:525/529 of 2q5oA
- active site: I23 (≠ V28), G25 (= G30), D26 (= D31), F27 (≠ Y32), A28 (≠ V33), E49 (= E53), T72 (= T75), H113 (= H116), H114 (= H117), G116 (≠ F119), R117 (≠ G120), T118 (≠ P121), L119 (≠ F122), R166 (≠ A169), V258 (≠ A263), N285 (≠ D290), M373 (≠ V382), A395 (≠ T407), M397 (= M409), D422 (= D434), N449 (= N461), S451 (≠ G463), W452 (≠ Y464), M454 (≠ T466), L455 (≠ E467), F458 (= F469), R515 (≠ P527)
- binding magnesium ion: D422 (= D434), N449 (= N461), S451 (≠ G463)
- binding 3-phenylpyruvic acid: G25 (= G30), D26 (= D31), R61 (= R65), H113 (= H116), H114 (= H117), R215 (≠ H220), R216 (= R221), M239 (≠ T244), G242 (≠ S247), T284 (≠ V289), L388 (≠ F400), M389 (≠ L401), A390 (= A402), M454 (≠ T466), F525 (≠ L537)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: P24 (= P29), E49 (= E53), A75 (≠ V78), D375 (= D384), M397 (= M409), G421 (= G433), D422 (= D434), G423 (= G435), A424 (= A436), N449 (= N461), S451 (≠ G463), W452 (≠ Y464), E453 (≠ S465), M454 (≠ T466), L455 (≠ E467)
6vgsBBB Alpha-keto acid decarboxylase (see paper)
31% identity, 97% coverage: 8:537/549 of query aligns to 3:533/543 of 6vgsBBB
- active site: V23 (= V28), G25 (= G30), D26 (= D31), Y27 (= Y32), N28 (≠ V33), E49 (= E53), T71 (= T75), H112 (= H116), H113 (= H117), L115 (≠ F119), A116 (vs. gap), V166 (≠ A169), S282 (≠ D290), Q372 (≠ V382), G397 (≠ T407), I399 (≠ M409), D424 (= D434), N451 (= N461), G453 (= G463), Y454 (= Y464), V456 (≠ T466), E457 (= E467)
- binding magnesium ion: D424 (= D434), N451 (= N461), G453 (= G463)
- binding thiamine diphosphate: P24 (= P29), E49 (= E53), V74 (= V78), T374 (≠ D384), I399 (≠ M409), G423 (= G433), G425 (= G435), S426 (≠ A436), N451 (= N461), G453 (= G463), Y454 (= Y464), T455 (≠ S465), V456 (≠ T466), E457 (= E467)
2q5lA X-ray structure of phenylpyruvate decarboxylase in complex with 2-(1- hydroxyethyl)-3-deaza-thdp (see paper)
36% identity, 96% coverage: 9:537/549 of query aligns to 9:533/538 of 2q5lA
- active site: I28 (≠ V28), G30 (= G30), D31 (= D31), F32 (≠ Y32), A33 (≠ V33), E54 (= E53), T77 (= T75), T118 (≠ H116), L119 (≠ F122), R166 (≠ A169), V258 (≠ A263), N285 (≠ D290), M381 (≠ V382), A403 (≠ T407), M405 (= M409), D430 (= D434), N457 (= N461), S459 (≠ G463), W460 (≠ Y464), M462 (≠ T466), L463 (≠ E467), F466 (= F469), R523 (≠ P527)
- binding magnesium ion: D430 (= D434), N457 (= N461), S459 (≠ G463)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-[(1r)-1-hydroxyethyl]-3-methyl-2-thienyl}ethyl trihydrogen diphosphate: P29 (= P29), D31 (= D31), E54 (= E53), D383 (= D384), A403 (≠ T407), M405 (= M409), D430 (= D434), G431 (= G435), N457 (= N461), S459 (≠ G463), W460 (≠ Y464), E461 (≠ S465), M462 (≠ T466), L463 (≠ E467)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-[(1s)-1-hydroxyethyl]-3-methyl-2-thienyl}ethyl trihydrogen diphosphate: P29 (= P29), D31 (= D31), E54 (= E53), D383 (= D384), A403 (≠ T407), M405 (= M409), G429 (= G433), D430 (= D434), G431 (= G435), A432 (= A436), N457 (= N461), S459 (≠ G463), W460 (≠ Y464), E461 (≠ S465), M462 (≠ T466), L463 (≠ E467)
Q92345 Probable pyruvate decarboxylase C1F8.07c; EC 4.1.1.1 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
32% identity, 95% coverage: 9:531/549 of query aligns to 11:547/569 of Q92345
- S233 (≠ D226) modified: Phosphoserine
- T521 (≠ E505) modified: Phosphothreonine
- S522 (≠ N506) modified: Phosphoserine
2q5jA X-ray structure of phenylpyruvate decarboxylase in complex with 3- deaza-thdp (see paper)
36% identity, 96% coverage: 9:537/549 of query aligns to 3:517/523 of 2q5jA
- active site: I22 (≠ V28), G24 (= G30), D25 (= D31), F26 (≠ Y32), A27 (≠ V33), E48 (= E53), T71 (= T75), R150 (≠ A169), V242 (≠ A263), N269 (≠ D290), M365 (≠ V382), A387 (≠ T407), M389 (= M409), D414 (= D434), N441 (= N461), S443 (≠ G463), W444 (≠ Y464), M446 (≠ T466), L447 (≠ E467), F450 (= F469), R507 (≠ P527)
- binding magnesium ion: D414 (= D434), N441 (= N461), S443 (≠ G463)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-3-methylthiophen-2-yl}ethyl trihydrogen diphosphate: P23 (= P29), E48 (= E53), G366 (= G383), D367 (= D384), A387 (≠ T407), G388 (≠ S408), M389 (= M409), G413 (= G433), D414 (= D434), G415 (= G435), A416 (= A436), N441 (= N461), W444 (≠ Y464), E445 (≠ S465), M446 (≠ T466), L447 (≠ E467)
2vbgA The complex structure of the branched-chain keto acid decarboxylase (kdca) from lactococcus lactis with 2r-1-hydroxyethyl-deazathdp (see paper)
31% identity, 97% coverage: 8:537/549 of query aligns to 8:537/546 of 2vbgA
- active site: V28 (= V28), G30 (= G30), D31 (= D31), Y32 (= Y32), N33 (≠ V33), N53 (≠ R52), E54 (= E53), T76 (= T75), F115 (≠ L114), V116 (≠ I115), H117 (= H116), H118 (= H117), L120 (≠ F119), A121 (vs. gap), V171 (≠ A169), K259 (≠ A263), S286 (≠ D290), E375 (≠ D381), Q376 (≠ V382), G401 (≠ T407), I403 (≠ M409), D428 (= D434), N455 (= N461), G457 (= G463), Y458 (= Y464), V460 (≠ T466), E461 (= E467), K527 (≠ P527)
- binding magnesium ion: D428 (= D434), N455 (= N461), G457 (= G463)
- binding 2-{4-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-[(1r)-1-hydroxyethyl]-3-methyl-2-thienyl}ethyl trihydrogen diphosphate: P29 (= P29), E54 (= E53), V79 (= V78), H118 (= H117), G377 (= G383), T378 (≠ D384), G401 (≠ T407), S402 (= S408), I403 (≠ M409), G427 (= G433), G429 (= G435), S430 (≠ A436), N455 (= N461), G457 (= G463), Y458 (= Y464), T459 (≠ S465), V460 (≠ T466), E461 (= E467)
2vbfB The holostructure of the branched-chain keto acid decarboxylase (kdca) from lactococcus lactis (see paper)
31% identity, 97% coverage: 8:537/549 of query aligns to 8:537/546 of 2vbfB
- active site: V28 (= V28), G30 (= G30), D31 (= D31), Y32 (= Y32), N33 (≠ V33), N53 (≠ R52), E54 (= E53), T76 (= T75), F115 (≠ L114), V116 (≠ I115), H117 (= H116), H118 (= H117), L120 (≠ F119), A121 (vs. gap), V171 (≠ A169), K259 (≠ A263), S286 (≠ D290), E375 (≠ D381), Q376 (≠ V382), G401 (≠ T407), I403 (≠ M409), D428 (= D434), N455 (= N461), G457 (= G463), Y458 (= Y464), V460 (≠ T466), E461 (= E467), K527 (≠ P527)
- binding magnesium ion: D428 (= D434), N455 (= N461), G457 (= G463)
- binding thiamine diphosphate: P29 (= P29), E54 (= E53), V79 (= V78), G377 (= G383), T378 (≠ D384), G401 (≠ T407), S402 (= S408), I403 (≠ M409), G427 (= G433), G429 (= G435), S430 (≠ A436), N455 (= N461), G457 (= G463), Y458 (= Y464), T459 (≠ S465), V460 (≠ T466), E461 (= E467)
2nxwA Crystal structure of phenylpyruvate decarboxylase of azospirillum brasilense (see paper)
36% identity, 96% coverage: 9:537/549 of query aligns to 10:530/537 of 2nxwA
- active site: I29 (≠ V28), G31 (= G30), D32 (= D31), F33 (≠ Y32), A34 (≠ V33), E55 (= E53), T78 (= T75), R163 (≠ A169), V255 (≠ A263), N282 (≠ D290), M378 (≠ V382), A400 (≠ T407), M402 (= M409), D427 (= D434), N454 (= N461), S456 (≠ G463), W457 (≠ Y464), M459 (≠ T466), L460 (≠ E467), F463 (= F469), R520 (≠ P527)
- binding magnesium ion: D427 (= D434), N454 (= N461), S456 (≠ G463)
- binding thiamine diphosphate: P30 (= P29), E55 (= E53), D380 (= D384), M402 (= M409), G426 (= G433), D427 (= D434), G428 (= G435), A429 (= A436), N454 (= N461), S456 (≠ G463), W457 (≠ Y464), E458 (≠ S465), M459 (≠ T466), L460 (≠ E467)
5npuA Inferred ancestral pyruvate decarboxylase (see paper)
32% identity, 95% coverage: 9:531/549 of query aligns to 4:526/547 of 5npuA
- binding magnesium ion: D425 (= D434), N452 (= N461)
- binding thiamine diphosphate: D375 (= D384), G398 (≠ T407), H399 (≠ S408), I400 (≠ M409), G424 (= G433), D425 (= D434), S427 (≠ A436), N452 (= N461), G454 (= G463), Y455 (= Y464), T456 (≠ S465), I457 (≠ T466), E458 (= E467)
P23234 Indole-3-pyruvate decarboxylase; Indolepyruvate decarboxylase; EC 4.1.1.74 from Enterobacter cloacae (see paper)
32% identity, 95% coverage: 6:529/549 of query aligns to 4:534/552 of P23234
- E52 (= E53) binding thiamine diphosphate
- D435 (= D434) binding Mg(2+)
- N462 (= N461) binding Mg(2+)
1ovmA Crystal structure of indolepyruvate decarboxylase from enterobacter cloacae (see paper)
32% identity, 95% coverage: 6:529/549 of query aligns to 2:518/535 of 1ovmA
- active site: G26 (= G30), D27 (= D31), Y28 (= Y32), N29 (≠ V33), E50 (= E53), T72 (= T75), H113 (= H116), H114 (= H117), L116 (≠ F119), G117 (vs. gap), A167 (= A169), S262 (≠ A263), L289 (≠ D290), Q367 (≠ V382), G392 (≠ T407), I394 (≠ M409), D419 (= D434), N446 (= N461), G448 (= G463), V451 (≠ T466), E452 (= E467), I455 (= I470), K516 (≠ P527)
- binding magnesium ion: D419 (= D434), N446 (= N461), G448 (= G463)
- binding thiamine diphosphate: P25 (= P29), E50 (= E53), V75 (= V78), T369 (≠ D384), G392 (≠ T407), S393 (= S408), I394 (≠ M409), G418 (= G433), G420 (= G435), A421 (= A436), N446 (= N461), G448 (= G463), Y449 (= Y464), T450 (≠ S465), V451 (≠ T466), E452 (= E467)
P06672 Pyruvate decarboxylase; PDC; EC 4.1.1.1 from Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) (see 2 papers)
31% identity, 95% coverage: 9:531/549 of query aligns to 5:545/568 of P06672
- E50 (= E53) mutation to Q: Almost complete loss of activity.
2wvgA Structural insights into the pre-reaction state of pyruvate decarboxylase from zymomonas mobilis (see paper)
31% identity, 95% coverage: 9:531/549 of query aligns to 4:544/565 of 2wvgA
- active site: D26 (= D31), Y27 (= Y32), E49 (= E53), Y72 (= Y76), H112 (= H116), H113 (= H117), L115 (≠ F119), G116 (= G120), C167 (≠ A169), Y289 (≠ V289), T387 (≠ V382), G412 (≠ T407), D439 (= D434), N466 (= N461), G468 (= G463), I471 (≠ T466), E472 (= E467)
- binding fluoride ion: G25 (= G30), D26 (= D31), T71 (= T75), H113 (= H117)
- binding magnesium ion: D439 (= D434), N466 (= N461), G468 (= G463)
- binding 2-{1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-methyl-1h-1,2,3-triazol-4-yl}ethyl trihydrogen diphosphate: A24 (≠ P29), E49 (= E53), V74 (= V78), D389 (= D384), G412 (≠ T407), H413 (≠ S408), I414 (≠ M409), G438 (= G433), D439 (= D434), G440 (= G435), S441 (≠ A436), N466 (= N461), G468 (= G463), Y469 (= Y464), T470 (≠ S465), I471 (≠ T466), E472 (= E467)
2wvaE Structural insights into the pre-reaction state of pyruvate decarboxylase from zymomonas mobilis (see paper)
31% identity, 95% coverage: 9:531/549 of query aligns to 4:544/565 of 2wvaE
- active site: D26 (= D31), Y27 (= Y32), E49 (= E53), Y72 (= Y76), H112 (= H116), H113 (= H117), L115 (≠ F119), G116 (= G120), C167 (≠ A169), Y289 (≠ V289), T387 (≠ V382), G412 (≠ T407), D439 (= D434), N466 (= N461), G468 (= G463), I471 (≠ T466), E472 (= E467)
- binding magnesium ion: D439 (= D434), N466 (= N461), G468 (= G463)
- binding pyruvic acid: D26 (= D31), H113 (= H117)
- binding 2-{1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-methyl-1h-1,2,3-triazol-4-yl}ethyl trihydrogen diphosphate: A24 (≠ P29), E49 (= E53), V74 (= V78), H113 (= H117), G388 (= G383), D389 (= D384), H413 (≠ S408), I414 (≠ M409), G438 (= G433), G440 (= G435), S441 (≠ A436), G468 (= G463), Y469 (= Y464), T470 (≠ S465), I471 (≠ T466), E472 (= E467)
2wvaA Structural insights into the pre-reaction state of pyruvate decarboxylase from zymomonas mobilis (see paper)
31% identity, 95% coverage: 9:531/549 of query aligns to 4:544/565 of 2wvaA
- active site: D26 (= D31), Y27 (= Y32), E49 (= E53), Y72 (= Y76), H112 (= H116), H113 (= H117), L115 (≠ F119), G116 (= G120), C167 (≠ A169), Y289 (≠ V289), T387 (≠ V382), G412 (≠ T407), D439 (= D434), N466 (= N461), G468 (= G463), I471 (≠ T466), E472 (= E467)
- binding magnesium ion: D439 (= D434), N466 (= N461), G468 (= G463)
- binding 2-{1-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-methyl-1h-1,2,3-triazol-4-yl}ethyl trihydrogen diphosphate: A24 (≠ P29), E49 (= E53), V74 (= V78), H113 (= H117), D389 (= D384), G412 (≠ T407), H413 (≠ S408), I414 (≠ M409), G438 (= G433), D439 (= D434), G440 (= G435), S441 (≠ A436), N466 (= N461), G468 (= G463), Y469 (= Y464), T470 (≠ S465), I471 (≠ T466), E472 (= E467)
3oe1A Pyruvate decarboxylase variant glu473asp from z. Mobilis in complex with reaction intermediate 2-lactyl-thdp (see paper)
31% identity, 95% coverage: 9:531/549 of query aligns to 4:544/565 of 3oe1A
- active site: D26 (= D31), Y27 (= Y32), E49 (= E53), Y72 (= Y76), H112 (= H116), H113 (= H117), L115 (≠ F119), G116 (= G120), C167 (≠ A169), Y289 (≠ V289), T387 (≠ V382), G412 (≠ T407), D439 (= D434), N466 (= N461), G468 (= G463), I471 (≠ T466), D472 (≠ E467)
- binding magnesium ion: D439 (= D434), N466 (= N461), G468 (= G463)
- 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: A24 (≠ P29), G25 (= G30), D26 (= D31), E49 (= E53), V74 (= V78), H113 (= H117), G388 (= G383), D389 (= D384), G412 (≠ T407), H413 (≠ S408), I414 (≠ M409), G440 (= G435), S441 (≠ A436), N466 (= N461), G468 (= G463), Y469 (= Y464), T470 (≠ S465), I471 (≠ T466), D472 (≠ E467)
1zpdA Pyruvate decarboxylase from zymomonas mobilis (see paper)
31% identity, 95% coverage: 9:531/549 of query aligns to 4:544/565 of 1zpdA
- active site: D26 (= D31), Y27 (= Y32), E49 (= E53), Y72 (= Y76), H112 (= H116), H113 (= H117), L115 (≠ F119), G116 (= G120), C167 (≠ A169), Y289 (≠ V289), T387 (≠ V382), G412 (≠ T407), I414 (≠ M409), D439 (= D434), N466 (= N461), G468 (= G463), I471 (≠ T466), E472 (= E467)
- binding mono-{4-[(4-amino-2-methyl-pyrimidin-5-ylmethyl)-amino]-2-hydroxy-3-mercapto-pent-3-enyl-phosphono} ester: A24 (≠ P29), E49 (= E53), V74 (= V78), D389 (= D384), G412 (≠ T407), H413 (≠ S408), I414 (≠ M409), G438 (= G433), G440 (= G435), S441 (≠ A436), N466 (= N461), G468 (= G463), Y469 (= Y464), T470 (≠ S465), I471 (≠ T466), E472 (= E467)
- binding magnesium ion: D439 (= D434), N466 (= N461), G468 (= G463)
2vbiA Holostructure of pyruvate decarboxylase from acetobacter pasteurianus
30% identity, 95% coverage: 9:531/549 of query aligns to 4:536/554 of 2vbiA
- active site: G25 (= G30), D26 (= D31), Y27 (= Y32), N28 (vs. gap), E49 (= E53), T71 (= T75), H112 (= H116), H113 (= H117), I115 (≠ F119), G116 (= G120), C167 (≠ A169), S290 (≠ D290), T383 (≠ V382), G408 (≠ T407), I410 (≠ M409), D435 (= D434), N462 (= N461), G464 (= G463), Y465 (= Y464), I467 (≠ T466), E468 (= E467), R532 (≠ P527)
- binding magnesium ion: D435 (= D434), N462 (= N461), G464 (= G463)
- binding thiamine diphosphate: A24 (≠ P29), E49 (= E53), V74 (= V78), D385 (= D384), G408 (≠ T407), H409 (≠ S408), I410 (≠ M409), G434 (= G433), D435 (= D434), G436 (= G435), S437 (≠ A436), N462 (= N461), G464 (= G463), Y465 (= Y464), V466 (≠ S465), I467 (≠ T466)
5tmaA Zymomonas mobilis pyruvate decarboxylase mutant pdc-2.3 (see paper)
31% identity, 95% coverage: 9:531/549 of query aligns to 5:545/567 of 5tmaA
- active site: D27 (= D31), Y28 (= Y32), E50 (= E53), Y73 (= Y76), H113 (= H116), H114 (= H117), L116 (≠ F119), G117 (= G120), C168 (≠ A169), Y290 (≠ V289), T388 (≠ V382), G413 (≠ T407), D440 (= D434), N467 (= N461), G469 (= G463), I472 (≠ T466), E473 (= E467)
- binding magnesium ion: D440 (= D434), N467 (= N461), G469 (= G463)
- binding thiamine diphosphate: D390 (= D384), G413 (≠ T407), H414 (≠ S408), I415 (≠ M409), G439 (= G433), G441 (= G435), S442 (≠ A436), N467 (= N461), G469 (= G463), Y470 (= Y464), T471 (≠ S465), I472 (≠ T466), E473 (= E467)
Query Sequence
>WP_010960298.1 NCBI__GCF_000008325.1:WP_010960298.1
MGTVEPGAIGQHLLACLYQAGVGHIFGVPGDYVLGFYDLMAKGPVRHIGTTREDTAAFAA
DGYARCRGMGALAVTYGVGALNTVNAVAGAYAESSPVVVISGAPGVREQREDPLIHHRFG
PFRFQREIFERITCAAVVLDDPVIAFRQVERALAAARQHCKPVYIEIPADRVMAPGYPIP
QETPETPSSDDSALAEAVAEAAELLGRAVSPVILAGVELHRRGLQDALVGLVEQARLPVA
ATLTGKSVFAERHPAYLGVYEGAMSTENARYMVEQSDLLLMLGVTLNDVDTGIYTARLDP
QRIVRAAQNEVVIRHHRYPRVLLADFVTALARSVKARGEAFPMPAGPEPWDFPAPDRPMT
IARLVERLDRALTSDMIVVCDVGDCLFAATDLRVHERSEFLASAFYTSMGFAVPAALGAQ
IARPDHRALILVGDGAFQMTGTELSTHARLGLAPIVVVLDNRGYSTERFILDGAFNDIAD
WRFHRLGEVFGPLQGYDAPDEAAFENALSEALVNRNMPSLINVRLSPGDASIAMKRLAGH
LQCRVKGEG
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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