SitesBLAST
Comparing H281DRAFT_02404 FitnessBrowser__Burk376:H281DRAFT_02404 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)
6x9dA Structure of proline utilization a with trans-4-hydroxy-l-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
63% identity, 94% coverage: 75:1312/1312 of query aligns to 1:1218/1218 of 6x9dA
- active site: N692 (= N773), K715 (= K796), E795 (= E877), C829 (= C911), E925 (= E1007), A1007 (= A1089)
- binding flavin-adenine dinucleotide: D291 (= D367), A292 (= A368), V323 (= V399), Q325 (= Q401), R352 (= R428), V354 (= V430), K355 (= K431), G356 (= G432), A357 (= A433), Y358 (= Y434), W359 (= W435), F377 (≠ Y453), T378 (= T454), R379 (= R455), K380 (= K456), T383 (= T459), A406 (= A482), T407 (= T483), H408 (= H484), N409 (= N485), Q432 (= Q508), C433 (= C509), E477 (= E556), S483 (= S562), F484 (= F563)
- binding 4-hydroxyproline: E659 (= E739), F693 (= F774), I697 (= I778), R828 (= R910), S830 (= S912), G987 (= G1069), A988 (= A1070), F995 (= F1077)
- binding nicotinamide-adenine-dinucleotide: I688 (= I769), S689 (= S770), P690 (= P771), W691 (= W772), N692 (= N773), I697 (= I778), K715 (= K796), A717 (= A798), E718 (= E799), G748 (= G829), G751 (= G833), A752 (= A834), T766 (= T848), G767 (= G849), S768 (= S850), V771 (= V853), E795 (= E877), T796 (= T878), C829 (= C911), E925 (= E1007), F927 (= F1009), F995 (= F1077)
7mybA Structure of proline utilization a with tetrahydrothiophene-2- carboxylate bound in the proline dehydrogenase active site (see paper)
63% identity, 94% coverage: 75:1312/1312 of query aligns to 1:1217/1217 of 7mybA
- binding flavin-adenine dinucleotide: D290 (= D367), A291 (= A368), V322 (= V399), Q324 (= Q401), R351 (= R428), V353 (= V430), K354 (= K431), G355 (= G432), A356 (= A433), Y357 (= Y434), W358 (= W435), F376 (≠ Y453), T377 (= T454), R378 (= R455), K379 (= K456), T382 (= T459), A405 (= A482), T406 (= T483), H407 (= H484), N408 (= N485), C432 (= C509), L433 (= L510), E476 (= E556), S482 (= S562), F483 (= F563)
- binding nicotinamide-adenine-dinucleotide: I687 (= I769), S688 (= S770), P689 (= P771), W690 (= W772), N691 (= N773), I696 (= I778), K714 (= K796), E717 (= E799), G747 (= G829), G750 (= G833), T765 (= T848), G766 (= G849), S767 (= S850), V770 (= V853), I774 (= I857), E794 (= E877), T795 (= T878), C828 (= C911), E924 (= E1007), F926 (= F1009), F994 (= F1077)
- binding (2S)-thiolane-2-carboxylic acid: K249 (= K326), Y457 (= Y537), Y469 (= Y549), R472 (= R552), R473 (= R553)
- binding (2R)-thiolane-2-carboxylic acid: K249 (= K326), D290 (= D367), Y457 (= Y537), Y469 (= Y549), R472 (= R552), R473 (= R553)
7myaA Structure of proline utilization a with the fad covalently-modified by 1,3-dithiolane (see paper)
63% identity, 94% coverage: 75:1312/1312 of query aligns to 1:1217/1217 of 7myaA
- binding nicotinamide-adenine-dinucleotide: I687 (= I769), S688 (= S770), P689 (= P771), W690 (= W772), N691 (= N773), I696 (= I778), K714 (= K796), A716 (= A798), E717 (= E799), G747 (= G829), G750 (= G833), A751 (= A834), T765 (= T848), G766 (= G849), S767 (= S850), V770 (= V853), E794 (= E877), T795 (= T878), C828 (= C911), E924 (= E1007), F926 (= F1009), F994 (= F1077)
- 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 (= D367), A291 (= A368), V322 (= V399), Q324 (= Q401), V353 (= V430), K354 (= K431), G355 (= G432), A356 (= A433), W358 (= W435), F376 (≠ Y453), T377 (= T454), R378 (= R455), K379 (= K456), T382 (= T459), A405 (= A482), T406 (= T483), H407 (= H484), N408 (= N485), Q431 (= Q508), C432 (= C509), L433 (= L510), Y457 (= Y537), E476 (= E556), G1217 (= G1312)
7my9A Structure of proline utilization a with 1,3-dithiolane-2-carboxylate bound in the proline dehydrogenase active site (see paper)
63% identity, 94% coverage: 75:1312/1312 of query aligns to 1:1216/1216 of 7my9A
- binding flavin-adenine dinucleotide: D289 (= D367), A290 (= A368), V321 (= V399), Q323 (= Q401), R350 (= R428), V352 (= V430), K353 (= K431), G354 (= G432), A355 (= A433), Y356 (= Y434), W357 (= W435), F375 (≠ Y453), T376 (= T454), R377 (= R455), K378 (= K456), T381 (= T459), A404 (= A482), T405 (= T483), H406 (= H484), N407 (= N485), C431 (= C509), L432 (= L510), E475 (= E556), S481 (= S562), F482 (= F563)
- binding nicotinamide-adenine-dinucleotide: I686 (= I769), S687 (= S770), P688 (= P771), W689 (= W772), N690 (= N773), I695 (= I778), K713 (= K796), A715 (= A798), E716 (= E799), G746 (= G829), G749 (= G833), A750 (= A834), T764 (= T848), G765 (= G849), S766 (= S850), V769 (= V853), E793 (= E877), T794 (= T878), C827 (= C911), E923 (= E1007), F925 (= F1009), F993 (= F1077)
- binding 1,3-dithiolane-2-carboxylic acid: Y456 (= Y537), Y468 (= Y549), R471 (= R552), R472 (= R553)
7mycA Structure of proline utilization a with the fad covalently modified by tetrahydrothiophene (see paper)
63% identity, 94% coverage: 75:1311/1312 of query aligns to 1:1216/1216 of 7mycA
- binding 1,4-dihydronicotinamide adenine dinucleotide: I687 (= I769), S688 (= S770), P689 (= P771), W690 (= W772), N691 (= N773), K714 (= K796), E717 (= E799), G747 (= G829), G750 (= G833), A751 (= A834), F764 (= F847), G766 (= G849), S767 (= S850), V770 (= V853), T795 (= T878), G796 (= G879), C828 (= C911), E924 (= E1007), F926 (= F1009)
- 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 (= K326), D290 (= D367), A291 (= A368), V322 (= V399), Q324 (= Q401), R351 (= R428), V353 (= V430), K354 (= K431), G355 (= G432), A356 (= A433), Y357 (= Y434), W358 (= W435), F376 (≠ Y453), T377 (= T454), R378 (= R455), K379 (= K456), T382 (= T459), A405 (= A482), T406 (= T483), H407 (= H484), N408 (= N485), Q431 (= Q508), C432 (= C509), L433 (= L510), Y457 (= Y537), S482 (= S562), F483 (= F563)
6x99A Structure of proline utilization a with d-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
63% identity, 94% coverage: 75:1312/1312 of query aligns to 1:1216/1216 of 6x99A
- active site: N690 (= N773), K713 (= K796), E793 (= E877), C827 (= C911), E923 (= E1007), A1005 (= A1089)
- binding d-proline: W557 (= W638), T558 (≠ R639), E657 (= E739), F691 (= F774), R727 (= R810), R826 (= R910), S828 (= S912), G985 (= G1069), A986 (= A1070), F993 (= F1077)
- binding flavin-adenine dinucleotide: D289 (= D367), A290 (= A368), V321 (= V399), R350 (= R428), V352 (= V430), K353 (= K431), G354 (= G432), A355 (= A433), Y356 (= Y434), W357 (= W435), F375 (≠ Y453), T376 (= T454), R377 (= R455), K378 (= K456), T381 (= T459), A404 (= A482), T405 (= T483), H406 (= H484), N407 (= N485), Q430 (= Q508), C431 (= C509), Y456 (= Y537), E475 (= E556), S481 (= S562), F482 (= F563)
6x9bA Structure of proline utilization a with cis-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
63% identity, 94% coverage: 75:1312/1312 of query aligns to 1:1214/1214 of 6x9bA
- active site: N688 (= N773), K711 (= K796), E791 (= E877), C825 (= C911), E921 (= E1007), A1003 (= A1089)
- binding flavin-adenine dinucleotide: D287 (= D367), A288 (= A368), V319 (= V399), R348 (= R428), V350 (= V430), K351 (= K431), G352 (= G432), A353 (= A433), Y354 (= Y434), W355 (= W435), F373 (≠ Y453), T374 (= T454), R375 (= R455), K376 (= K456), T379 (= T459), A402 (= A482), T403 (= T483), H404 (= H484), N405 (= N485), Q428 (= Q508), C429 (= C509), Y454 (= Y537), E473 (= E556), S479 (= S562), F480 (= F563)
- binding nicotinamide-adenine-dinucleotide: I684 (= I769), S685 (= S770), P686 (= P771), W687 (= W772), N688 (= N773), I693 (= I778), K711 (= K796), A713 (= A798), E714 (= E799), G744 (= G829), G747 (= G833), A748 (= A834), T762 (= T848), G763 (= G849), S764 (= S850), V767 (= V853), I771 (= I857), E791 (= E877), T792 (= T878), C825 (= C911), E921 (= E1007), F923 (= F1009)
- binding (4R)-4-hydroxy-D-proline: E655 (= E739), F689 (= F774), S826 (= S912), G983 (= G1069), A984 (= A1070), F991 (= F1077)
6x9aA Structure of proline utilization a with trans-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
63% identity, 94% coverage: 75:1312/1312 of query aligns to 1:1214/1214 of 6x9aA
- active site: N688 (= N773), K711 (= K796), E791 (= E877), C825 (= C911), E921 (= E1007), A1003 (= A1089)
- binding flavin-adenine dinucleotide: D287 (= D367), A288 (= A368), V319 (= V399), R348 (= R428), V350 (= V430), K351 (= K431), G352 (= G432), A353 (= A433), Y354 (= Y434), W355 (= W435), F373 (≠ Y453), T374 (= T454), R375 (= R455), K376 (= K456), T379 (= T459), A402 (= A482), T403 (= T483), H404 (= H484), N405 (= N485), C429 (= C509), E473 (= E556), S479 (= S562), F480 (= F563)
- binding (4S)-4-hydroxy-D-proline: W555 (= W638), T556 (≠ R639), E655 (= E739), F689 (= F774), R725 (= R810), S826 (= S912), G983 (= G1069), A984 (= A1070), F991 (= F1077)
6x9cA Structure of proline utilization a with l-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
63% identity, 94% coverage: 78:1308/1312 of query aligns to 3:1209/1209 of 6x9cA
- active site: N687 (= N773), K710 (= K796), E790 (= E877), C824 (= C911), E920 (= E1007), A1002 (= A1089)
- binding dihydroflavine-adenine dinucleotide: D286 (= D367), A287 (= A368), V318 (= V399), Q320 (= Q401), R347 (= R428), V349 (= V430), K350 (= K431), G351 (= G432), A352 (= A433), Y353 (= Y434), W354 (= W435), F372 (≠ Y453), T373 (= T454), R374 (= R455), K375 (= K456), T378 (= T459), A401 (= A482), T402 (= T483), H403 (= H484), N404 (= N485), Q427 (= Q508), C428 (= C509), E472 (= E556), S478 (= S562), F479 (= F563)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I683 (= I769), S684 (= S770), P685 (= P771), W686 (= W772), N687 (= N773), K710 (= K796), E713 (= E799), G743 (= G829), G746 (= G833), A747 (= A834), F760 (= F847), G762 (= G849), S763 (= S850), V766 (= V853), E920 (= E1007), F922 (= F1009)
- binding proline: R823 (= R910), C824 (= C911), S825 (= S912), G982 (= G1069), A983 (= A1070), F990 (= F1077)
5kf6A Structure of proline utilization a from sinorhizobium meliloti complexed with l-tetrahydrofuroic acid and NAD+ in space group p21 (see paper)
63% identity, 94% coverage: 75:1309/1312 of query aligns to 1:1206/1207 of 5kf6A
- active site: N683 (= N773), K706 (= K796), E786 (= E877), C820 (= C911), E916 (= E1007), A998 (= A1089)
- binding flavin-adenine dinucleotide: D282 (= D367), A283 (= A368), V314 (= V399), Q316 (= Q401), R343 (= R428), V345 (= V430), K346 (= K431), G347 (= G432), A348 (= A433), Y349 (= Y434), W350 (= W435), F368 (≠ Y453), T369 (= T454), R370 (= R455), K371 (= K456), T374 (= T459), A397 (= A482), T398 (= T483), H399 (= H484), N400 (= N485), Q423 (= Q508), C424 (= C509), L425 (= L510), E468 (= E556), S474 (= S562), F475 (= F563)
- binding nicotinamide-adenine-dinucleotide: I679 (= I769), S680 (= S770), P681 (= P771), W682 (= W772), N683 (= N773), I688 (= I778), K706 (= K796), A708 (= A798), E709 (= E799), G739 (= G829), G742 (= G833), A743 (= A834), F756 (= F847), T757 (= T848), G758 (= G849), S759 (= S850), V762 (= V853), I766 (= I857), E786 (= E877), T787 (= T878), C820 (= C911), E916 (= E1007), F918 (= F1009), F986 (= F1077)
- binding tetrahydrofuran-2-carboxylic acid: K241 (= K326), D282 (= D367), Y449 (= Y537), R464 (= R552), R465 (= R553)
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)
62% identity, 94% coverage: 75:1309/1312 of query aligns to 1:1196/1197 of 6ufpA
- active site: N673 (= N773), K696 (= K796), E776 (= E877), C810 (= C911), E906 (= E1007), A988 (= A1089)
- binding dihydroflavine-adenine dinucleotide: D285 (= D367), A286 (= A368), V317 (= V399), Q319 (= Q401), R346 (= R428), V348 (= V430), K349 (= K431), G350 (= G432), A351 (= A433), W353 (= W435), F371 (≠ Y453), T372 (= T454), R373 (= R455), K374 (= K456), T377 (= T459), A400 (= A482), T401 (= T483), H402 (= H484), N403 (= N485), Q426 (= Q508), C427 (= C509), L428 (= L510), S464 (= S562)
- binding nicotinamide-adenine-dinucleotide: I669 (= I769), P671 (= P771), W672 (= W772), N673 (= N773), I678 (= I778), K696 (= K796), E699 (= E799), G729 (= G829), G732 (= G833), F746 (= F847), T747 (= T848), G748 (= G849), S749 (= S850), V752 (= V853), E776 (= E877), T777 (= T878), C810 (= C911), E906 (= E1007), F908 (= F1009)
- binding (2S)-1,3-thiazolidine-2-carboxylic acid: K244 (= K326), D285 (= D367), Y439 (= Y537), Y451 (= Y549), R454 (= R552), R455 (= R553)
3hazA Crystal structure of bifunctional proline utilization a (puta) protein (see paper)
49% identity, 76% coverage: 96:1098/1312 of query aligns to 8:969/983 of 3hazA
- active site: N652 (= N773), K675 (= K796), E752 (= E877), C786 (= C911), E878 (= E1007), A960 (= A1089)
- binding flavin-adenine dinucleotide: D272 (= D367), A273 (= A368), Q306 (= Q401), R333 (= R428), V335 (= V430), K336 (= K431), G337 (= G432), A338 (= A433), Y339 (= Y434), W340 (= W435), F358 (≠ Y453), T359 (= T454), R360 (= R455), K361 (= K456), T364 (= T459), A387 (= A482), T388 (= T483), H389 (= H484), N390 (= N485), Y435 (= Y537), S460 (= S562), F461 (= F563)
- binding nicotinamide-adenine-dinucleotide: I648 (= I769), S649 (= S770), P650 (= P771), W651 (= W772), N652 (= N773), I657 (= I778), K675 (= K796), P676 (= P797), A677 (= A798), G708 (= G829), G711 (= G833), A712 (= A834), T726 (= T848), G727 (= G849), S728 (= S850), V731 (= V853), I735 (= I857), E752 (= E877), T753 (= T878), C786 (= C911), E878 (= E1007), F880 (= F1009), F948 (= F1077)
6bsnA Structure of proline utilization a (puta) with proline bound in remote sites (see paper)
48% identity, 76% coverage: 96:1098/1312 of query aligns to 8:960/973 of 6bsnA
- active site: N643 (= N773), E743 (= E877), A777 (≠ C911), A951 (= A1089)
- binding dihydroflavine-adenine dinucleotide: D269 (= D367), A270 (= A368), Q303 (= Q401), R330 (= R428), V332 (= V430), K333 (= K431), G334 (= G432), A335 (= A433), Y336 (= Y434), W337 (= W435), F355 (≠ Y453), T356 (= T454), R357 (= R455), K358 (= K456), T361 (= T459), A384 (= A482), T385 (= T483), H386 (= H484), N387 (= N485), Y432 (= Y537), S457 (= S562), F458 (= F563)
- binding proline: M630 (vs. gap), W642 (= W772), F644 (= F774), G718 (= G849), R776 (= R910), S778 (= S912), F871 (= F1009), I930 (= I1068), G931 (= G1069), A932 (= A1070), F939 (= F1077), A958 (≠ Q1096), R959 (= R1097)
Sites not aligning to the query:
7sqnA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with (2s)-oxetane-2-carboxylic acid (see paper)
73% identity, 39% coverage: 89:603/1312 of query aligns to 1:503/503 of 7sqnA
- binding (2S)-oxetane-2-carboxylic acid: K222 (= K326), Y433 (= Y537), R448 (= R552), R449 (= R553)
- binding flavin-adenine dinucleotide: D263 (= D367), A264 (= A368), V295 (= V399), Q297 (= Q401), R324 (= R428), V326 (= V430), K327 (= K431), G328 (= G432), A329 (= A433), Y330 (= Y434), W331 (= W435), Y349 (= Y453), T350 (= T454), R351 (= R455), K352 (= K456), T355 (= T459), A378 (= A482), T379 (= T483), H380 (= H484), N381 (= N485), C405 (= C509), L406 (= L510), E452 (= E556), S458 (= S562)
7mwvA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclopropanecarboxylic acid (see paper)
72% identity, 39% coverage: 89:603/1312 of query aligns to 1:499/499 of 7mwvA
- binding flavin-adenine dinucleotide: D259 (= D367), A260 (= A368), V291 (= V399), Q293 (= Q401), R320 (= R428), V322 (= V430), K323 (= K431), G324 (= G432), A325 (= A433), Y326 (= Y434), W327 (= W435), Y345 (= Y453), T346 (= T454), R347 (= R455), K348 (= K456), T351 (= T459), A374 (= A482), T375 (= T483), H376 (= H484), N377 (= N485), C401 (= C509), L402 (= L510), E448 (= E556), S454 (= S562)
- binding cyclopropanecarboxylic acid: K218 (= K326), Y429 (= Y537), Y441 (= Y549), R444 (= R552), R445 (= R553)
7mwuA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclobutanecarboxylic acid (see paper)
72% identity, 39% coverage: 89:603/1312 of query aligns to 1:499/499 of 7mwuA
- binding flavin-adenine dinucleotide: D259 (= D367), A260 (= A368), V291 (= V399), Q293 (= Q401), R320 (= R428), V322 (= V430), K323 (= K431), G324 (= G432), A325 (= A433), Y326 (= Y434), W327 (= W435), Y345 (= Y453), T346 (= T454), R347 (= R455), K348 (= K456), T351 (= T459), A374 (= A482), T375 (= T483), H376 (= H484), N377 (= N485), C401 (= C509), L402 (= L510), E448 (= E556), S454 (= S562)
- binding cyclobutanecarboxylic acid: K218 (= K326), L402 (= L510), Y429 (= Y537), Y441 (= Y549), R444 (= R552), R445 (= R553)
7mwtA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with 1,1-cyclobutanedicarboxylate (see paper)
72% identity, 39% coverage: 89:603/1312 of query aligns to 1:499/499 of 7mwtA
- binding flavin-adenine dinucleotide: D259 (= D367), A260 (= A368), V291 (= V399), Q293 (= Q401), R320 (= R428), V322 (= V430), K323 (= K431), G324 (= G432), A325 (= A433), Y326 (= Y434), W327 (= W435), Y345 (= Y453), T346 (= T454), R347 (= R455), K348 (= K456), T351 (= T459), A374 (= A482), T375 (= T483), H376 (= H484), N377 (= N485), C401 (= C509), L402 (= L510), E448 (= E556), S454 (= S562)
- binding cyclobutane-1,1-dicarboxylic acid: K218 (= K326), Y326 (= Y434), Y429 (= Y537), Y441 (= Y549), R444 (= R552), R445 (= R553)
4jnyA Crystal structure of puta86-630 mutant d370a complexed with l- tetrahydro-2-furoic acid (see paper)
71% identity, 39% coverage: 88:603/1312 of query aligns to 1:491/491 of 4jnyA
- binding flavin-adenine dinucleotide: A252 (= A368), V283 (= V399), Q285 (= Q401), R312 (= R428), V314 (= V430), K315 (= K431), G316 (= G432), A317 (= A433), Y318 (= Y434), W319 (= W435), Y337 (= Y453), T338 (= T454), R339 (= R455), K340 (= K456), T343 (= T459), A366 (= A482), T367 (= T483), H368 (= H484), N369 (= N485), C393 (= C509), L394 (= L510), E440 (= E556), S446 (= S562), F447 (= F563)
- binding tetrahydrofuran-2-carboxylic acid: K210 (= K326), Y421 (= Y537), R436 (= R552), R437 (= R553)
1tj0A Crystal structure of e. Coli puta proline dehydrogenase domain (residues 86-669) co-crystallized with l-lactate (see paper)
68% identity, 39% coverage: 89:603/1312 of query aligns to 1:469/469 of 1tj0A
- binding flavin-adenine dinucleotide: D229 (= D367), A230 (= A368), V261 (= V399), Q263 (= Q401), R290 (= R428), V292 (= V430), K293 (= K431), G294 (= G432), A295 (= A433), Y296 (= Y434), W297 (= W435), Y315 (= Y453), T316 (= T454), R317 (= R455), K318 (= K456), T321 (= T459), A344 (= A482), T345 (= T483), H346 (= H484), N347 (= N485), Q370 (= Q508), C371 (= C509), L372 (= L510), E418 (= E556), S424 (= S562)
3e2sA Crystal structure reduced puta86-630 mutant y540s complexed with l- proline (see paper)
67% identity, 39% coverage: 89:603/1312 of query aligns to 1:468/468 of 3e2sA
- binding flavin-adenine dinucleotide: D228 (= D367), A229 (= A368), V260 (= V399), Q262 (= Q401), V291 (= V430), K292 (= K431), G293 (= G432), A294 (= A433), Y295 (= Y434), W296 (= W435), Y314 (= Y453), T315 (= T454), R316 (= R455), K317 (= K456), T320 (= T459), A343 (= A482), T344 (= T483), H345 (= H484), N346 (= N485), C370 (= C509), L371 (= L510), E417 (= E556), S423 (= S562), F424 (= F563)
- binding proline: K187 (= K326), L371 (= L510), Y410 (= Y549), R413 (= R552), R414 (= R553)
Query Sequence
>H281DRAFT_02404 FitnessBrowser__Burk376:H281DRAFT_02404
MASTTLGVKVDDLLRSRLRDAATRLERTPHWLIKQAIFAYLEKIEQGQLPPELSGVAGSA
DMADGASVEPDEDGAAHPFLDFAQNVQPQSVLRAAITAAYRRPEPECVPFLLGQARLPAN
LAGDVQALAAKLVETLRGKSKGGGVEGLIHEFSLSSQEGVALMCLAEALLRIPDRATRDA
LIRDKISKGDWKSHVGQAPSLFVNAATWGLMITGKLVTTNSETNLSSALTRLIGKGGEPL
IRKGVDMAMRLMGEQFVTGENISEALANSRKYEARGFRYSYDMLGEAATTEADAQRYYAS
YEQAIHAIGKAAGGRGIYEGPGISIKLSALHPRYSRSQQERTMSELLPRVRSLAILARRY
DIGLNIDAEEADRLEISLDLLEALCFDPELAGWNGIGFVVQAYQKRCPFVIEYIVDLARR
SRHRIMVRLVKGAYWDTEIKRAQVDGLEGYPVYTRKIYTDVSYLACAKKLLGAPDAVYPQ
FATHNAHTLSAIYHLAGNNYYPGQYEFQCLHGMGEPLYEEVTGPLSAGKLNRPCRVYAPV
GTHETLLAYLVRRLLENGANTSFVNRIADENVAIQDLIADPVEEASKIVPLGAPHAKIPL
PRNLYGAERLNSMGLDLSNEHRLASLSSALLASANHPWRAAPMLADDQIVLGNARDVRNP
ADHRDLVGTVVEASAEHVSAALAHAVAAAPIWQATPVEARADCLARAADLLEAQMHTLMG
LVVREAGKSLANAVSEIREAIDFLRYYSTQIRSEFSNDTHRPLGPVVCISPWNFPLAIFM
GQVAAALAAGNTVLAKPAEQTPLIAAQAVRILREAGVPAGAVQLLPGDGETVGAALVADP
RTRAVMFTGSTEVARLINKTLSGRLDPEGKPIPLIAETGGQNAMIVDSSALAEQVVADVM
QSSFDSAGQRCSALRVLCLQDDVADRTLEMLTGAMRELTVGNPDRLSTDVGPVIDVDAKR
GIDAHIAAMREKGRKVEQLPMPEGCAQGTFVPPTLIELDSIDELKREVFGPVLHVVRYRR
SQLDQLLEQIRTTGYGLTLGIHTRIDETIAHVISRAHVGNIYVNRNVIGAVVGVQPFGGE
GLSGTGPKAGGALYLQRLLATRPAGLPKSLAQALIVDVPQAAEKGDNPSAALTALRDWLI
AEREPQLAARCDGYLSHMPAGATAVLSGPTGERNTYTLGARGTVLCIASTASGARAQFAA
VLATGNRALFEGAAGEQLVTQLPASLKSYASVRKNAETPFDAVLFEGDSDELLTLVKEVA
KRPGPIVSVQGVASRALESGDEDYALERLLTERSVSVNTAAAGGNANLMTIG
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