SitesBLAST
Comparing 3608920 FitnessBrowser__Dino:3608920 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)
6x9dA Structure of proline utilization a with trans-4-hydroxy-l-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
47% identity, 99% coverage: 15:1218/1221 of query aligns to 18:1216/1218 of 6x9dA
- active site: N692 (= N686), K715 (= K709), E795 (= E787), C829 (= C821), E925 (= E914), A1007 (= A996)
- binding flavin-adenine dinucleotide: D291 (= D288), A292 (= A289), V323 (= V320), Q325 (= Q322), R352 (= R349), V354 (= V351), K355 (= K352), G356 (= G353), A357 (= A354), Y358 (= Y355), W359 (= W356), F377 (= F374), T378 (= T375), R379 (= R376), K380 (= K377), T383 (= T380), A406 (= A403), T407 (= T404), H408 (= H405), N409 (= N406), Q432 (= Q427), C433 (≠ R428), E477 (= E470), S483 (= S476), F484 (= F477)
- binding 4-hydroxyproline: E659 (= E652), F693 (= F687), I697 (= I691), R828 (= R820), S830 (= S822), G987 (= G976), A988 (= A977), F995 (= F984)
- binding nicotinamide-adenine-dinucleotide: I688 (= I682), S689 (= S683), P690 (= P684), W691 (= W685), N692 (= N686), I697 (= I691), K715 (= K709), A717 (= A711), E718 (= E712), G748 (= G742), G751 (= G746), A752 (≠ G747), T766 (= T761), G767 (= G762), S768 (= S763), V771 (= V766), E795 (= E787), T796 (= T788), C829 (= C821), E925 (= E914), F927 (= F916), F995 (= F984)
7mybA Structure of proline utilization a with tetrahydrothiophene-2- carboxylate bound in the proline dehydrogenase active site (see paper)
46% identity, 99% coverage: 15:1218/1221 of query aligns to 18:1215/1217 of 7mybA
- binding flavin-adenine dinucleotide: D290 (= D288), A291 (= A289), V322 (= V320), Q324 (= Q322), R351 (= R349), V353 (= V351), K354 (= K352), G355 (= G353), A356 (= A354), Y357 (= Y355), W358 (= W356), F376 (= F374), T377 (= T375), R378 (= R376), K379 (= K377), T382 (= T380), A405 (= A403), T406 (= T404), H407 (= H405), N408 (= N406), C432 (≠ R428), L433 (= L429), E476 (= E470), S482 (= S476), F483 (= F477)
- binding nicotinamide-adenine-dinucleotide: I687 (= I682), S688 (= S683), P689 (= P684), W690 (= W685), N691 (= N686), I696 (= I691), K714 (= K709), E717 (= E712), G747 (= G742), G750 (= G746), T765 (= T761), G766 (= G762), S767 (= S763), V770 (= V766), I774 (= I770), E794 (= E787), T795 (= T788), C828 (= C821), E924 (= E914), F926 (= F916), F994 (= F984)
- binding (2S)-thiolane-2-carboxylic acid: K249 (= K247), Y457 (= Y451), Y469 (= Y463), R472 (= R466), R473 (= R467)
- binding (2R)-thiolane-2-carboxylic acid: K249 (= K247), D290 (= D288), Y457 (= Y451), Y469 (= Y463), R472 (= R466), R473 (= R467)
7myaA Structure of proline utilization a with the fad covalently-modified by 1,3-dithiolane (see paper)
46% identity, 99% coverage: 15:1218/1221 of query aligns to 18:1215/1217 of 7myaA
- binding nicotinamide-adenine-dinucleotide: I687 (= I682), S688 (= S683), P689 (= P684), W690 (= W685), N691 (= N686), I696 (= I691), K714 (= K709), A716 (= A711), E717 (= E712), G747 (= G742), G750 (= G746), A751 (≠ G747), T765 (= T761), G766 (= G762), S767 (= S763), V770 (= V766), E794 (= E787), T795 (= T788), C828 (= C821), E924 (= E914), F926 (= F916), F994 (= F984)
- binding [(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl (2R,3S,4S)-5-[5-(1,3-dithiolan-2-yl)-7,8-dimethyl-2,4-dioxo-1,3,4,5-tetrahydrobenzo[g]pteridin-10(2H)-yl]-2,3,4-trihydroxypentyl dihydrogen diphosphate: D290 (= D288), A291 (= A289), V322 (= V320), Q324 (= Q322), V353 (= V351), K354 (= K352), G355 (= G353), A356 (= A354), W358 (= W356), F376 (= F374), T377 (= T375), R378 (= R376), K379 (= K377), T382 (= T380), A405 (= A403), T406 (= T404), H407 (= H405), N408 (= N406), Q431 (= Q427), C432 (≠ R428), L433 (= L429), Y457 (= Y451), E476 (= E470)
Sites not aligning to the query:
- binding [(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl (2R,3S,4S)-5-[5-(1,3-dithiolan-2-yl)-7,8-dimethyl-2,4-dioxo-1,3,4,5-tetrahydrobenzo[g]pteridin-10(2H)-yl]-2,3,4-trihydroxypentyl dihydrogen diphosphate: 1217
7mycA Structure of proline utilization a with the fad covalently modified by tetrahydrothiophene (see paper)
46% identity, 99% coverage: 15:1218/1221 of query aligns to 18:1215/1216 of 7mycA
- binding 1,4-dihydronicotinamide adenine dinucleotide: I687 (= I682), S688 (= S683), P689 (= P684), W690 (= W685), N691 (= N686), K714 (= K709), E717 (= E712), G747 (= G742), G750 (= G746), A751 (≠ G747), F764 (= F760), G766 (= G762), S767 (= S763), V770 (= V766), T795 (= T788), G796 (= G789), C828 (= C821), E924 (= E914), F926 (= F916)
- binding [(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl (2R,3S,4S)-5-{7,8-dimethyl-2,4-dioxo-5-[(2R)-tetrahydrothiophen-2-yl]-1,3,4,5-tetrahydrobenzo[g]pteridin-10(2H)-yl}-2,3,4-trihydroxypentyl dihydrogen diphosphate (non-preferred name): K249 (= K247), D290 (= D288), A291 (= A289), V322 (= V320), Q324 (= Q322), R351 (= R349), V353 (= V351), K354 (= K352), G355 (= G353), A356 (= A354), Y357 (= Y355), W358 (= W356), F376 (= F374), T377 (= T375), R378 (= R376), K379 (= K377), T382 (= T380), A405 (= A403), T406 (= T404), H407 (= H405), N408 (= N406), Q431 (= Q427), C432 (≠ R428), L433 (= L429), Y457 (= Y451), S482 (= S476), F483 (= F477)
6x99A Structure of proline utilization a with d-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
47% identity, 99% coverage: 15:1218/1221 of query aligns to 18:1214/1216 of 6x99A
- active site: N690 (= N686), K713 (= K709), E793 (= E787), C827 (= C821), E923 (= E914), A1005 (= A996)
- binding d-proline: W557 (= W551), T558 (≠ H552), E657 (= E652), F691 (= F687), R727 (≠ Q723), R826 (= R820), S828 (= S822), G985 (= G976), A986 (= A977), F993 (= F984)
- binding flavin-adenine dinucleotide: D289 (= D288), A290 (= A289), V321 (= V320), R350 (= R349), V352 (= V351), K353 (= K352), G354 (= G353), A355 (= A354), Y356 (= Y355), W357 (= W356), F375 (= F374), T376 (= T375), R377 (= R376), K378 (= K377), T381 (= T380), A404 (= A403), T405 (= T404), H406 (= H405), N407 (= N406), Q430 (= Q427), C431 (≠ R428), Y456 (= Y451), E475 (= E470), S481 (= S476), F482 (= F477)
7my9A Structure of proline utilization a with 1,3-dithiolane-2-carboxylate bound in the proline dehydrogenase active site (see paper)
46% identity, 99% coverage: 15:1218/1221 of query aligns to 18:1214/1216 of 7my9A
- binding flavin-adenine dinucleotide: D289 (= D288), A290 (= A289), V321 (= V320), Q323 (= Q322), R350 (= R349), V352 (= V351), K353 (= K352), G354 (= G353), A355 (= A354), Y356 (= Y355), W357 (= W356), F375 (= F374), T376 (= T375), R377 (= R376), K378 (= K377), T381 (= T380), A404 (= A403), T405 (= T404), H406 (= H405), N407 (= N406), C431 (≠ R428), L432 (= L429), E475 (= E470), S481 (= S476), F482 (= F477)
- binding nicotinamide-adenine-dinucleotide: I686 (= I682), S687 (= S683), P688 (= P684), W689 (= W685), N690 (= N686), I695 (= I691), K713 (= K709), A715 (= A711), E716 (= E712), G746 (= G742), G749 (= G746), A750 (≠ G747), T764 (= T761), G765 (= G762), S766 (= S763), V769 (= V766), E793 (= E787), T794 (= T788), C827 (= C821), E923 (= E914), F925 (= F916), F993 (= F984)
- binding 1,3-dithiolane-2-carboxylic acid: Y456 (= Y451), Y468 (= Y463), R471 (= R466), R472 (= R467)
6x9aA Structure of proline utilization a with trans-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
46% identity, 99% coverage: 15:1218/1221 of query aligns to 18:1212/1214 of 6x9aA
- active site: N688 (= N686), K711 (= K709), E791 (= E787), C825 (= C821), E921 (= E914), A1003 (= A996)
- binding flavin-adenine dinucleotide: D287 (= D288), A288 (= A289), V319 (= V320), R348 (= R349), V350 (= V351), K351 (= K352), G352 (= G353), A353 (= A354), Y354 (= Y355), W355 (= W356), F373 (= F374), T374 (= T375), R375 (= R376), K376 (= K377), T379 (= T380), A402 (= A403), T403 (= T404), H404 (= H405), N405 (= N406), C429 (≠ R428), E473 (= E470), S479 (= S476), F480 (= F477)
- binding (4S)-4-hydroxy-D-proline: W555 (= W551), T556 (≠ H552), E655 (= E652), F689 (= F687), R725 (≠ Q723), S826 (= S822), G983 (= G976), A984 (= A977), F991 (= F984)
6x9bA Structure of proline utilization a with cis-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
46% identity, 99% coverage: 15:1218/1221 of query aligns to 18:1212/1214 of 6x9bA
- active site: N688 (= N686), K711 (= K709), E791 (= E787), C825 (= C821), E921 (= E914), A1003 (= A996)
- binding flavin-adenine dinucleotide: D287 (= D288), A288 (= A289), V319 (= V320), R348 (= R349), V350 (= V351), K351 (= K352), G352 (= G353), A353 (= A354), Y354 (= Y355), W355 (= W356), F373 (= F374), T374 (= T375), R375 (= R376), K376 (= K377), T379 (= T380), A402 (= A403), T403 (= T404), H404 (= H405), N405 (= N406), Q428 (= Q427), C429 (≠ R428), Y454 (= Y451), E473 (= E470), S479 (= S476), F480 (= F477)
- binding nicotinamide-adenine-dinucleotide: I684 (= I682), S685 (= S683), P686 (= P684), W687 (= W685), N688 (= N686), I693 (= I691), K711 (= K709), A713 (= A711), E714 (= E712), G744 (= G742), G747 (= G746), A748 (≠ G747), T762 (= T761), G763 (= G762), S764 (= S763), V767 (= V766), I771 (= I770), E791 (= E787), T792 (= T788), C825 (= C821), E921 (= E914), F923 (= F916)
- binding (4R)-4-hydroxy-D-proline: E655 (= E652), F689 (= F687), S826 (= S822), G983 (= G976), A984 (= A977), F991 (= F984)
6x9cA Structure of proline utilization a with l-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
46% identity, 98% coverage: 15:1216/1221 of query aligns to 17:1209/1209 of 6x9cA
- active site: N687 (= N686), K710 (= K709), E790 (= E787), C824 (= C821), E920 (= E914), A1002 (= A996)
- binding dihydroflavine-adenine dinucleotide: D286 (= D288), A287 (= A289), V318 (= V320), Q320 (= Q322), R347 (= R349), V349 (= V351), K350 (= K352), G351 (= G353), A352 (= A354), Y353 (= Y355), W354 (= W356), F372 (= F374), T373 (= T375), R374 (= R376), K375 (= K377), T378 (= T380), A401 (= A403), T402 (= T404), H403 (= H405), N404 (= N406), Q427 (= Q427), C428 (≠ R428), E472 (= E470), S478 (= S476), F479 (= F477)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I683 (= I682), S684 (= S683), P685 (= P684), W686 (= W685), N687 (= N686), K710 (= K709), E713 (= E712), G743 (= G742), G746 (= G746), A747 (≠ G747), F760 (= F760), G762 (= G762), S763 (= S763), V766 (= V766), E920 (= E914), F922 (= F916)
- binding proline: R823 (= R820), C824 (= C821), S825 (= S822), G982 (= G976), A983 (= A977), F990 (= F984)
5kf6A Structure of proline utilization a from sinorhizobium meliloti complexed with l-tetrahydrofuroic acid and NAD+ in space group p21 (see paper)
46% identity, 99% coverage: 15:1218/1221 of query aligns to 18:1207/1207 of 5kf6A
- active site: N683 (= N686), K706 (= K709), E786 (= E787), C820 (= C821), E916 (= E914), A998 (= A996)
- binding flavin-adenine dinucleotide: D282 (= D288), A283 (= A289), V314 (= V320), Q316 (= Q322), R343 (= R349), V345 (= V351), K346 (= K352), G347 (= G353), A348 (= A354), Y349 (= Y355), W350 (= W356), F368 (= F374), T369 (= T375), R370 (= R376), K371 (= K377), T374 (= T380), A397 (= A403), T398 (= T404), H399 (= H405), N400 (= N406), Q423 (= Q427), C424 (≠ R428), L425 (= L429), E468 (= E470), S474 (= S476), F475 (= F477)
- binding nicotinamide-adenine-dinucleotide: I679 (= I682), S680 (= S683), P681 (= P684), W682 (= W685), N683 (= N686), I688 (= I691), K706 (= K709), A708 (= A711), E709 (= E712), G739 (= G742), G742 (= G746), A743 (≠ G747), F756 (= F760), T757 (= T761), G758 (= G762), S759 (= S763), V762 (= V766), I766 (= I770), E786 (= E787), T787 (= T788), C820 (= C821), E916 (= E914), F918 (= F916), F986 (= F984)
- binding tetrahydrofuran-2-carboxylic acid: K241 (= K247), D282 (= D288), Y449 (= Y451), R464 (= R466), R465 (= R467)
6ufpA Structure of proline utilization a with the fad covalently modified by l-thiazolidine-2-carboxylate and three cysteines (cys46, cys470, cys638) modified to s,s-(2-hydroxyethyl)thiocysteine (see paper)
46% identity, 99% coverage: 15:1218/1221 of query aligns to 18:1197/1197 of 6ufpA
- active site: N673 (= N686), K696 (= K709), E776 (= E787), C810 (= C821), E906 (= E914), A988 (= A996)
- binding dihydroflavine-adenine dinucleotide: D285 (= D288), A286 (= A289), V317 (= V320), Q319 (= Q322), R346 (= R349), V348 (= V351), K349 (= K352), G350 (= G353), A351 (= A354), W353 (= W356), F371 (= F374), T372 (= T375), R373 (= R376), K374 (= K377), T377 (= T380), A400 (= A403), T401 (= T404), H402 (= H405), N403 (= N406), Q426 (= Q427), C427 (≠ R428), L428 (= L429), S464 (= S476)
- binding nicotinamide-adenine-dinucleotide: I669 (= I682), P671 (= P684), W672 (= W685), N673 (= N686), I678 (= I691), K696 (= K709), E699 (= E712), G729 (= G742), G732 (= G746), F746 (= F760), T747 (= T761), G748 (= G762), S749 (= S763), V752 (= V766), E776 (= E787), T777 (= T788), C810 (= C821), E906 (= E914), F908 (= F916)
- binding (2S)-1,3-thiazolidine-2-carboxylic acid: K244 (= K247), D285 (= D288), Y439 (= Y451), Y451 (= Y463), R454 (= R466), R455 (= R467)
6bsnA Structure of proline utilization a (puta) with proline bound in remote sites (see paper)
49% identity, 80% coverage: 34:1005/1221 of query aligns to 19:960/973 of 6bsnA
- active site: N643 (= N686), E743 (= E787), A777 (≠ C821), A951 (= A996)
- binding dihydroflavine-adenine dinucleotide: D269 (= D288), A270 (= A289), Q303 (= Q322), R330 (= R349), V332 (= V351), K333 (= K352), G334 (= G353), A335 (= A354), Y336 (= Y355), W337 (= W356), F355 (= F374), T356 (= T375), R357 (= R376), K358 (= K377), T361 (= T380), A384 (= A403), T385 (= T404), H386 (= H405), N387 (= N406), Y432 (= Y451), S457 (= S476), F458 (= F477)
- binding proline: M630 (vs. gap), W642 (= W685), F644 (= F687), G718 (= G762), R776 (= R820), S778 (= S822), F871 (= F916), I930 (= I975), G931 (= G976), A932 (= A977), F939 (= F984), A958 (≠ T1003), R959 (= R1004)
Sites not aligning to the query:
3hazA Crystal structure of bifunctional proline utilization a (puta) protein (see paper)
49% identity, 80% coverage: 34:1005/1221 of query aligns to 19:969/983 of 3hazA
- active site: N652 (= N686), K675 (= K709), E752 (= E787), C786 (= C821), E878 (= E914), A960 (= A996)
- binding flavin-adenine dinucleotide: D272 (= D288), A273 (= A289), Q306 (= Q322), R333 (= R349), V335 (= V351), K336 (= K352), G337 (= G353), A338 (= A354), Y339 (= Y355), W340 (= W356), F358 (= F374), T359 (= T375), R360 (= R376), K361 (= K377), T364 (= T380), A387 (= A403), T388 (= T404), H389 (= H405), N390 (= N406), Y435 (= Y451), S460 (= S476), F461 (= F477)
- binding nicotinamide-adenine-dinucleotide: I648 (= I682), S649 (= S683), P650 (= P684), W651 (= W685), N652 (= N686), I657 (= I691), K675 (= K709), P676 (= P710), A677 (= A711), G708 (= G742), G711 (= G746), A712 (≠ G747), T726 (= T761), G727 (= G762), S728 (= S763), V731 (= V766), I735 (= I770), E752 (= E787), T753 (= T788), C786 (= C821), E878 (= E914), F880 (= F916), F948 (= F984)
7sqnA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with (2s)-oxetane-2-carboxylic acid (see paper)
48% identity, 41% coverage: 16:516/1221 of query aligns to 5:503/503 of 7sqnA
- binding (2S)-oxetane-2-carboxylic acid: K222 (= K247), Y433 (= Y451), R448 (= R466), R449 (= R467)
- binding flavin-adenine dinucleotide: D263 (= D288), A264 (= A289), V295 (= V320), Q297 (= Q322), R324 (= R349), V326 (= V351), K327 (= K352), G328 (= G353), A329 (= A354), Y330 (= Y355), W331 (= W356), Y349 (≠ F374), T350 (= T375), R351 (= R376), K352 (= K377), T355 (= T380), A378 (= A403), T379 (= T404), H380 (= H405), N381 (= N406), C405 (≠ R428), L406 (= L429), E452 (= E470), S458 (= S476)
7mwvA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclopropanecarboxylic acid (see paper)
48% identity, 41% coverage: 16:516/1221 of query aligns to 5:499/499 of 7mwvA
- binding flavin-adenine dinucleotide: D259 (= D288), A260 (= A289), V291 (= V320), Q293 (= Q322), R320 (= R349), V322 (= V351), K323 (= K352), G324 (= G353), A325 (= A354), Y326 (= Y355), W327 (= W356), Y345 (≠ F374), T346 (= T375), R347 (= R376), K348 (= K377), T351 (= T380), A374 (= A403), T375 (= T404), H376 (= H405), N377 (= N406), C401 (≠ R428), L402 (= L429), E448 (= E470), S454 (= S476)
- binding cyclopropanecarboxylic acid: K218 (= K247), Y429 (= Y451), Y441 (= Y463), R444 (= R466), R445 (= R467)
7mwuA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclobutanecarboxylic acid (see paper)
48% identity, 41% coverage: 16:516/1221 of query aligns to 5:499/499 of 7mwuA
- binding flavin-adenine dinucleotide: D259 (= D288), A260 (= A289), V291 (= V320), Q293 (= Q322), R320 (= R349), V322 (= V351), K323 (= K352), G324 (= G353), A325 (= A354), Y326 (= Y355), W327 (= W356), Y345 (≠ F374), T346 (= T375), R347 (= R376), K348 (= K377), T351 (= T380), A374 (= A403), T375 (= T404), H376 (= H405), N377 (= N406), C401 (≠ R428), L402 (= L429), E448 (= E470), S454 (= S476)
- binding cyclobutanecarboxylic acid: K218 (= K247), L402 (= L429), Y429 (= Y451), Y441 (= Y463), R444 (= R466), R445 (= R467)
7mwtA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with 1,1-cyclobutanedicarboxylate (see paper)
48% identity, 41% coverage: 16:516/1221 of query aligns to 5:499/499 of 7mwtA
- binding flavin-adenine dinucleotide: D259 (= D288), A260 (= A289), V291 (= V320), Q293 (= Q322), R320 (= R349), V322 (= V351), K323 (= K352), G324 (= G353), A325 (= A354), Y326 (= Y355), W327 (= W356), Y345 (≠ F374), T346 (= T375), R347 (= R376), K348 (= K377), T351 (= T380), A374 (= A403), T375 (= T404), H376 (= H405), N377 (= N406), C401 (≠ R428), L402 (= L429), E448 (= E470), S454 (= S476)
- binding cyclobutane-1,1-dicarboxylic acid: K218 (= K247), Y326 (= Y355), Y429 (= Y451), Y441 (= Y463), R444 (= R466), R445 (= R467)
4jnyA Crystal structure of puta86-630 mutant d370a complexed with l- tetrahydro-2-furoic acid (see paper)
47% identity, 41% coverage: 16:516/1221 of query aligns to 6:491/491 of 4jnyA
- binding flavin-adenine dinucleotide: A252 (= A289), V283 (= V320), Q285 (= Q322), R312 (= R349), V314 (= V351), K315 (= K352), G316 (= G353), A317 (= A354), Y318 (= Y355), W319 (= W356), Y337 (≠ F374), T338 (= T375), R339 (= R376), K340 (= K377), T343 (= T380), A366 (= A403), T367 (= T404), H368 (= H405), N369 (= N406), C393 (≠ R428), L394 (= L429), E440 (= E470), S446 (= S476), F447 (= F477)
- binding tetrahydrofuran-2-carboxylic acid: K210 (= K247), Y421 (= Y451), R436 (= R466), R437 (= R467)
5ur2B Crystal structure of proline utilization a (puta) from bdellovibrio bacteriovorus inactivated by n-propargylglycine (see paper)
31% identity, 70% coverage: 154:1005/1221 of query aligns to 69:940/959 of 5ur2B
- active site: N618 (= N686), K641 (= K709), E722 (= E787), C756 (= C821), E851 (= E914), T931 (≠ A996)
- binding N-propargylglycine-modified flavin adenine dinucleotide: K174 (= K247), D215 (= D288), M216 (≠ A289), Q249 (= Q322), V278 (= V351), K279 (= K352), G280 (= G353), A281 (= A354), W283 (= W356), Y300 (≠ F374), T301 (= T375), N302 (≠ R376), K303 (= K377), S306 (≠ T380), A329 (= A403), S330 (≠ T404), H331 (= H405), N332 (= N406), Q356 (= Q427), M357 (≠ R428), L358 (= L429), Y379 (= Y451), E398 (= E470), E403 (≠ S475), W405 (≠ F477)
3e2sA Crystal structure reduced puta86-630 mutant y540s complexed with l- proline (see paper)
46% identity, 41% coverage: 16:516/1221 of query aligns to 5:468/468 of 3e2sA
- binding flavin-adenine dinucleotide: D228 (= D288), A229 (= A289), V260 (= V320), Q262 (= Q322), V291 (= V351), K292 (= K352), G293 (= G353), A294 (= A354), Y295 (= Y355), W296 (= W356), Y314 (≠ F374), T315 (= T375), R316 (= R376), K317 (= K377), T320 (= T380), A343 (= A403), T344 (= T404), H345 (= H405), N346 (= N406), C370 (≠ R428), L371 (= L429), E417 (= E470), S423 (= S476), F424 (= F477)
- binding proline: K187 (= K247), L371 (= L429), Y410 (= Y463), R413 (= R466), R414 (= R467)
Query Sequence
>3608920 FitnessBrowser__Dino:3608920
MNRAFDISSQIDNPFRAQVRAHYTAEETALLKSLAARIKLSAHEREKAAAAGARYVTRVR
NETRPSMMEAFLAEYGLSTSEGVGLMCLAEALLRVPDADTIDDLIEDKVAPSNWGAHLGH
SSSSLVNASTWALMLTGKVLDEDPRGPARALRGLVKRLGEPVVRTAVGQSMKVLGRQFVL
GQTIEEGLKNARELEKKGFTYSYDMLGEAARTDADARRYHAAYAQAITAIARQATGDVRS
SPGISVKLSALHPRYEYTHRHSVMADLVPRAAALVKQAAQAGIGFNVDAEEQDRLDLSLD
VIEAMMSDPDLDGWDGFGVVVQAYGRRAGPVIETLYDMAERYDRKIMVRLVKGAYWDTEI
KLAQELGVERFPVFTRKNNTDVSYMACAQMLLDRRDRIYPQFATHNAHTCAAVLQMAGNA
RDCFEFQRLHGMGASLHQIVKETEGTRCRIYAPVGAHQDLLAYLVRRLLENGANSSFVNQ
IVDPDIPAEAISADPVSEMEKLGDQIPNPAIRQPSDLFAPDRRNSRGYRVNEPASILPLM
TAREAFAETTWHARPMLAGGRDPTGPTREVHSPADKTRLVGTVQEASAEDVACALDAAET
GFRDWSARPVSERADMLRKLADMYEDNIAELTAITTREAGKTVLDGIAEVREAVDFLRFY
ANEAERLEEEDPGRPRGIFVCISPWNFPLAIFTGQIAAALVMGNAVLAKPAEQTPIIAAR
AVQMMRDCGLPDAALQLLPGDGPMVGGPLTSDPRIAGVCFTGSTEVAMIIHKALAKNAGP
EAVLVAETGGLNAMIVDSTALHEQAVRDILISSFQSAGQRCSALRILYVQEDVHDKLMEM
LSGALDALVIGDSWNLDVDVSPVIDADAQSDILGYIDQHRKAGTLIKTLAAPDSGTYVTP
AIVKVGGIADMEREIFGPVLHVATFKANEIDQVVDAINARRYGLTFGLHTRIDDRVEQIV
ERIQVGNVYVNRNQIGAIVGSQPFGGEGLSGTGPKAGGPLYLTRFRKVGKSTSHPAPQGA
VLGKAALNTALSSLDARNWAARPDRVHILRMALSGSTGVVRRALSETAAFDMSPQTLPGP
TGESNRLSMVPRGTVLCLGPTPEIAMAQAVQALGAGCAVVIALPGSTPLSQPLSDAGAPV
VTLDGTVDCVTLTELTGIEVVAAAGASDWTRTLRVALSQRDGPIIPLIVDEIAPERYVLE
RHLCIDTTAAGGNAKLLAASS
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