SitesBLAST
Comparing AZOBR_RS23695 FitnessBrowser__azobra:AZOBR_RS23695 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)
70% identity, 99% coverage: 16:1234/1235 of query aligns to 3:1217/1218 of 6x9dA
- active site: N692 (= N706), K715 (= K729), E795 (= E809), C829 (= C843), E925 (= E939), A1007 (= A1021)
- binding flavin-adenine dinucleotide: D291 (= D306), A292 (= A307), V323 (= V338), Q325 (= Q340), R352 (= R367), V354 (= V369), K355 (= K370), G356 (= G371), A357 (= A372), Y358 (= Y373), W359 (= W374), F377 (≠ Y392), T378 (= T393), R379 (= R394), K380 (= K395), T383 (= T398), A406 (= A421), T407 (= T422), H408 (= H423), N409 (= N424), Q432 (= Q447), C433 (= C448), E477 (= E490), S483 (= S496), F484 (= F497)
- binding 4-hydroxyproline: E659 (= E672), F693 (= F707), I697 (= I711), R828 (= R842), S830 (= S844), G987 (= G1001), A988 (= A1002), F995 (= F1009)
- binding nicotinamide-adenine-dinucleotide: I688 (= I702), S689 (= S703), P690 (= P704), W691 (= W705), N692 (= N706), I697 (= I711), K715 (= K729), A717 (= A731), E718 (= E732), G748 (= G762), G751 (= G765), A752 (= A766), T766 (= T780), G767 (= G781), S768 (= S782), V771 (= V785), E795 (= E809), T796 (= T810), C829 (= C843), E925 (= E939), F927 (= F941), F995 (= F1009)
7mybA Structure of proline utilization a with tetrahydrothiophene-2- carboxylate bound in the proline dehydrogenase active site (see paper)
70% identity, 99% coverage: 16:1234/1235 of query aligns to 3:1216/1217 of 7mybA
- binding flavin-adenine dinucleotide: D290 (= D306), A291 (= A307), V322 (= V338), Q324 (= Q340), R351 (= R367), V353 (= V369), K354 (= K370), G355 (= G371), A356 (= A372), Y357 (= Y373), W358 (= W374), F376 (≠ Y392), T377 (= T393), R378 (= R394), K379 (= K395), T382 (= T398), A405 (= A421), T406 (= T422), H407 (= H423), N408 (= N424), C432 (= C448), L433 (= L449), E476 (= E490), S482 (= S496), F483 (= F497)
- binding nicotinamide-adenine-dinucleotide: I687 (= I702), S688 (= S703), P689 (= P704), W690 (= W705), N691 (= N706), I696 (= I711), K714 (= K729), E717 (= E732), G747 (= G762), G750 (= G765), T765 (= T780), G766 (= G781), S767 (= S782), V770 (= V785), I774 (= I789), E794 (= E809), T795 (= T810), C828 (= C843), E924 (= E939), F926 (= F941), F994 (= F1009)
- binding (2S)-thiolane-2-carboxylic acid: K249 (= K265), Y457 (= Y471), Y469 (= Y483), R472 (= R486), R473 (= R487)
- binding (2R)-thiolane-2-carboxylic acid: K249 (= K265), D290 (= D306), Y457 (= Y471), Y469 (= Y483), R472 (= R486), R473 (= R487)
7myaA Structure of proline utilization a with the fad covalently-modified by 1,3-dithiolane (see paper)
70% identity, 99% coverage: 16:1234/1235 of query aligns to 3:1216/1217 of 7myaA
- binding nicotinamide-adenine-dinucleotide: I687 (= I702), S688 (= S703), P689 (= P704), W690 (= W705), N691 (= N706), I696 (= I711), K714 (= K729), A716 (= A731), E717 (= E732), G747 (= G762), G750 (= G765), A751 (= A766), T765 (= T780), G766 (= G781), S767 (= S782), V770 (= V785), E794 (= E809), T795 (= T810), C828 (= C843), E924 (= E939), F926 (= F941), F994 (= F1009)
- 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 (= D306), A291 (= A307), V322 (= V338), Q324 (= Q340), V353 (= V369), K354 (= K370), G355 (= G371), A356 (= A372), W358 (= W374), F376 (≠ Y392), T377 (= T393), R378 (= R394), K379 (= K395), T382 (= T398), A405 (= A421), T406 (= T422), H407 (= H423), N408 (= N424), Q431 (= Q447), C432 (= C448), L433 (= L449), Y457 (= Y471), E476 (= E490)
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)
70% identity, 99% coverage: 16:1234/1235 of query aligns to 3:1216/1216 of 7mycA
- binding 1,4-dihydronicotinamide adenine dinucleotide: I687 (= I702), S688 (= S703), P689 (= P704), W690 (= W705), N691 (= N706), K714 (= K729), E717 (= E732), G747 (= G762), G750 (= G765), A751 (= A766), F764 (= F779), G766 (= G781), S767 (= S782), V770 (= V785), T795 (= T810), G796 (= G811), C828 (= C843), E924 (= E939), F926 (= F941)
- 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 (= K265), D290 (= D306), A291 (= A307), V322 (= V338), Q324 (= Q340), R351 (= R367), V353 (= V369), K354 (= K370), G355 (= G371), A356 (= A372), Y357 (= Y373), W358 (= W374), F376 (≠ Y392), T377 (= T393), R378 (= R394), K379 (= K395), T382 (= T398), A405 (= A421), T406 (= T422), H407 (= H423), N408 (= N424), Q431 (= Q447), C432 (= C448), L433 (= L449), Y457 (= Y471), S482 (= S496), F483 (= F497)
6x99A Structure of proline utilization a with d-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
70% identity, 99% coverage: 16:1234/1235 of query aligns to 3:1215/1216 of 6x99A
- active site: N690 (= N706), K713 (= K729), E793 (= E809), C827 (= C843), E923 (= E939), A1005 (= A1021)
- binding d-proline: W557 (= W572), T558 (= T573), E657 (= E672), F691 (= F707), R727 (= R743), R826 (= R842), S828 (= S844), G985 (= G1001), A986 (= A1002), F993 (= F1009)
- binding flavin-adenine dinucleotide: D289 (= D306), A290 (= A307), V321 (= V338), R350 (= R367), V352 (= V369), K353 (= K370), G354 (= G371), A355 (= A372), Y356 (= Y373), W357 (= W374), F375 (≠ Y392), T376 (= T393), R377 (= R394), K378 (= K395), T381 (= T398), A404 (= A421), T405 (= T422), H406 (= H423), N407 (= N424), Q430 (= Q447), C431 (= C448), Y456 (= Y471), E475 (= E490), S481 (= S496), F482 (= F497)
7my9A Structure of proline utilization a with 1,3-dithiolane-2-carboxylate bound in the proline dehydrogenase active site (see paper)
70% identity, 99% coverage: 16:1234/1235 of query aligns to 3:1215/1216 of 7my9A
- binding flavin-adenine dinucleotide: D289 (= D306), A290 (= A307), V321 (= V338), Q323 (= Q340), R350 (= R367), V352 (= V369), K353 (= K370), G354 (= G371), A355 (= A372), Y356 (= Y373), W357 (= W374), F375 (≠ Y392), T376 (= T393), R377 (= R394), K378 (= K395), T381 (= T398), A404 (= A421), T405 (= T422), H406 (= H423), N407 (= N424), C431 (= C448), L432 (= L449), E475 (= E490), S481 (= S496), F482 (= F497)
- binding nicotinamide-adenine-dinucleotide: I686 (= I702), S687 (= S703), P688 (= P704), W689 (= W705), N690 (= N706), I695 (= I711), K713 (= K729), A715 (= A731), E716 (= E732), G746 (= G762), G749 (= G765), A750 (= A766), T764 (= T780), G765 (= G781), S766 (= S782), V769 (= V785), E793 (= E809), T794 (= T810), C827 (= C843), E923 (= E939), F925 (= F941), F993 (= F1009)
- binding 1,3-dithiolane-2-carboxylic acid: Y456 (= Y471), Y468 (= Y483), R471 (= R486), R472 (= R487)
6x9aA Structure of proline utilization a with trans-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
70% identity, 99% coverage: 16:1234/1235 of query aligns to 3:1213/1214 of 6x9aA
- active site: N688 (= N706), K711 (= K729), E791 (= E809), C825 (= C843), E921 (= E939), A1003 (= A1021)
- binding flavin-adenine dinucleotide: D287 (= D306), A288 (= A307), V319 (= V338), R348 (= R367), V350 (= V369), K351 (= K370), G352 (= G371), A353 (= A372), Y354 (= Y373), W355 (= W374), F373 (≠ Y392), T374 (= T393), R375 (= R394), K376 (= K395), T379 (= T398), A402 (= A421), T403 (= T422), H404 (= H423), N405 (= N424), C429 (= C448), E473 (= E490), S479 (= S496), F480 (= F497)
- binding (4S)-4-hydroxy-D-proline: W555 (= W572), T556 (= T573), E655 (= E672), F689 (= F707), R725 (= R743), S826 (= S844), G983 (= G1001), A984 (= A1002), F991 (= F1009)
6x9bA Structure of proline utilization a with cis-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
70% identity, 99% coverage: 16:1234/1235 of query aligns to 3:1213/1214 of 6x9bA
- active site: N688 (= N706), K711 (= K729), E791 (= E809), C825 (= C843), E921 (= E939), A1003 (= A1021)
- binding flavin-adenine dinucleotide: D287 (= D306), A288 (= A307), V319 (= V338), R348 (= R367), V350 (= V369), K351 (= K370), G352 (= G371), A353 (= A372), Y354 (= Y373), W355 (= W374), F373 (≠ Y392), T374 (= T393), R375 (= R394), K376 (= K395), T379 (= T398), A402 (= A421), T403 (= T422), H404 (= H423), N405 (= N424), Q428 (= Q447), C429 (= C448), Y454 (= Y471), E473 (= E490), S479 (= S496), F480 (= F497)
- binding nicotinamide-adenine-dinucleotide: I684 (= I702), S685 (= S703), P686 (= P704), W687 (= W705), N688 (= N706), I693 (= I711), K711 (= K729), A713 (= A731), E714 (= E732), G744 (= G762), G747 (= G765), A748 (= A766), T762 (= T780), G763 (= G781), S764 (= S782), V767 (= V785), I771 (= I789), E791 (= E809), T792 (= T810), C825 (= C843), E921 (= E939), F923 (= F941)
- binding (4R)-4-hydroxy-D-proline: E655 (= E672), F689 (= F707), S826 (= S844), G983 (= G1001), A984 (= A1002), F991 (= F1009)
6x9cA Structure of proline utilization a with l-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
70% identity, 98% coverage: 16:1231/1235 of query aligns to 2:1209/1209 of 6x9cA
- active site: N687 (= N706), K710 (= K729), E790 (= E809), C824 (= C843), E920 (= E939), A1002 (= A1021)
- binding dihydroflavine-adenine dinucleotide: D286 (= D306), A287 (= A307), V318 (= V338), Q320 (= Q340), R347 (= R367), V349 (= V369), K350 (= K370), G351 (= G371), A352 (= A372), Y353 (= Y373), W354 (= W374), F372 (≠ Y392), T373 (= T393), R374 (= R394), K375 (= K395), T378 (= T398), A401 (= A421), T402 (= T422), H403 (= H423), N404 (= N424), Q427 (= Q447), C428 (= C448), E472 (= E490), S478 (= S496), F479 (= F497)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I683 (= I702), S684 (= S703), P685 (= P704), W686 (= W705), N687 (= N706), K710 (= K729), E713 (= E732), G743 (= G762), G746 (= G765), A747 (= A766), F760 (= F779), G762 (= G781), S763 (= S782), V766 (= V785), E920 (= E939), F922 (= F941)
- binding proline: R823 (= R842), C824 (= C843), S825 (= S844), G982 (= G1001), A983 (= A1002), F990 (= F1009)
5kf6A Structure of proline utilization a from sinorhizobium meliloti complexed with l-tetrahydrofuroic acid and NAD+ in space group p21 (see paper)
70% identity, 99% coverage: 16:1233/1235 of query aligns to 3:1207/1207 of 5kf6A
- active site: N683 (= N706), K706 (= K729), E786 (= E809), C820 (= C843), E916 (= E939), A998 (= A1021)
- binding flavin-adenine dinucleotide: D282 (= D306), A283 (= A307), V314 (= V338), Q316 (= Q340), R343 (= R367), V345 (= V369), K346 (= K370), G347 (= G371), A348 (= A372), Y349 (= Y373), W350 (= W374), F368 (≠ Y392), T369 (= T393), R370 (= R394), K371 (= K395), T374 (= T398), A397 (= A421), T398 (= T422), H399 (= H423), N400 (= N424), Q423 (= Q447), C424 (= C448), L425 (= L449), E468 (= E490), S474 (= S496), F475 (= F497)
- binding nicotinamide-adenine-dinucleotide: I679 (= I702), S680 (= S703), P681 (= P704), W682 (= W705), N683 (= N706), I688 (= I711), K706 (= K729), A708 (= A731), E709 (= E732), G739 (= G762), G742 (= G765), A743 (= A766), F756 (= F779), T757 (= T780), G758 (= G781), S759 (= S782), V762 (= V785), I766 (= I789), E786 (= E809), T787 (= T810), C820 (= C843), E916 (= E939), F918 (= F941), F986 (= F1009)
- binding tetrahydrofuran-2-carboxylic acid: K241 (= K265), D282 (= D306), Y449 (= Y471), R464 (= R486), R465 (= R487)
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)
69% identity, 99% coverage: 16:1233/1235 of query aligns to 3:1197/1197 of 6ufpA
- active site: N673 (= N706), K696 (= K729), E776 (= E809), C810 (= C843), E906 (= E939), A988 (= A1021)
- binding dihydroflavine-adenine dinucleotide: D285 (= D306), A286 (= A307), V317 (= V338), Q319 (= Q340), R346 (= R367), V348 (= V369), K349 (= K370), G350 (= G371), A351 (= A372), W353 (= W374), F371 (≠ Y392), T372 (= T393), R373 (= R394), K374 (= K395), T377 (= T398), A400 (= A421), T401 (= T422), H402 (= H423), N403 (= N424), Q426 (= Q447), C427 (= C448), L428 (= L449), S464 (= S496)
- binding nicotinamide-adenine-dinucleotide: I669 (= I702), P671 (= P704), W672 (= W705), N673 (= N706), I678 (= I711), K696 (= K729), E699 (= E732), G729 (= G762), G732 (= G765), F746 (= F779), T747 (= T780), G748 (= G781), S749 (= S782), V752 (= V785), E776 (= E809), T777 (= T810), C810 (= C843), E906 (= E939), F908 (= F941)
- binding (2S)-1,3-thiazolidine-2-carboxylic acid: K244 (= K265), D285 (= D306), Y439 (= Y471), Y451 (= Y483), R454 (= R486), R455 (= R487)
3hazA Crystal structure of bifunctional proline utilization a (puta) protein (see paper)
48% identity, 81% coverage: 35:1034/1235 of query aligns to 8:973/983 of 3hazA
- active site: N652 (= N706), K675 (= K729), E752 (= E809), C786 (= C843), E878 (= E939), A960 (= A1021)
- binding flavin-adenine dinucleotide: D272 (= D306), A273 (= A307), Q306 (= Q340), R333 (= R367), V335 (= V369), K336 (= K370), G337 (= G371), A338 (= A372), Y339 (= Y373), W340 (= W374), F358 (≠ Y392), T359 (= T393), R360 (= R394), K361 (= K395), T364 (= T398), A387 (= A421), T388 (= T422), H389 (= H423), N390 (= N424), Y435 (= Y471), S460 (= S496), F461 (= F497)
- binding nicotinamide-adenine-dinucleotide: I648 (= I702), S649 (= S703), P650 (= P704), W651 (= W705), N652 (= N706), I657 (= I711), K675 (= K729), P676 (= P730), A677 (= A731), G708 (= G762), G711 (= G765), A712 (= A766), T726 (= T780), G727 (= G781), S728 (= S782), V731 (= V785), I735 (= I789), E752 (= E809), T753 (= T810), C786 (= C843), E878 (= E939), F880 (= F941), F948 (= F1009)
6bsnA Structure of proline utilization a (puta) with proline bound in remote sites (see paper)
48% identity, 81% coverage: 35:1034/1235 of query aligns to 8:964/973 of 6bsnA
- active site: N643 (= N706), E743 (= E809), A777 (≠ C843), A951 (= A1021)
- binding dihydroflavine-adenine dinucleotide: D269 (= D306), A270 (= A307), Q303 (= Q340), R330 (= R367), V332 (= V369), K333 (= K370), G334 (= G371), A335 (= A372), Y336 (= Y373), W337 (= W374), F355 (≠ Y392), T356 (= T393), R357 (= R394), K358 (= K395), T361 (= T398), A384 (= A421), T385 (= T422), H386 (= H423), N387 (= N424), Y432 (= Y471), S457 (= S496), F458 (= F497)
- binding proline: M630 (vs. gap), W642 (= W705), F644 (= F707), G718 (= G781), R776 (= R842), S778 (= S844), F871 (= F941), I930 (= I1000), G931 (= G1001), A932 (= A1002), F939 (= F1009), A958 (≠ S1028), R959 (= R1029), A961 (≠ L1031)
7sqnA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with (2s)-oxetane-2-carboxylic acid (see paper)
68% identity, 41% coverage: 32:537/1235 of query aligns to 5:503/503 of 7sqnA
- binding (2S)-oxetane-2-carboxylic acid: K222 (= K265), Y433 (= Y471), R448 (= R486), R449 (= R487)
- binding flavin-adenine dinucleotide: D263 (= D306), A264 (= A307), V295 (= V338), Q297 (= Q340), R324 (= R367), V326 (= V369), K327 (= K370), G328 (= G371), A329 (= A372), Y330 (= Y373), W331 (= W374), Y349 (= Y392), T350 (= T393), R351 (= R394), K352 (= K395), T355 (= T398), A378 (= A421), T379 (= T422), H380 (= H423), N381 (= N424), C405 (= C448), L406 (= L449), E452 (= E490), S458 (= S496)
7mwvA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclopropanecarboxylic acid (see paper)
68% identity, 41% coverage: 32:537/1235 of query aligns to 5:499/499 of 7mwvA
- binding flavin-adenine dinucleotide: D259 (= D306), A260 (= A307), V291 (= V338), Q293 (= Q340), R320 (= R367), V322 (= V369), K323 (= K370), G324 (= G371), A325 (= A372), Y326 (= Y373), W327 (= W374), Y345 (= Y392), T346 (= T393), R347 (= R394), K348 (= K395), T351 (= T398), A374 (= A421), T375 (= T422), H376 (= H423), N377 (= N424), C401 (= C448), L402 (= L449), E448 (= E490), S454 (= S496)
- binding cyclopropanecarboxylic acid: K218 (= K265), Y429 (= Y471), Y441 (= Y483), R444 (= R486), R445 (= R487)
7mwuA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclobutanecarboxylic acid (see paper)
68% identity, 41% coverage: 32:537/1235 of query aligns to 5:499/499 of 7mwuA
- binding flavin-adenine dinucleotide: D259 (= D306), A260 (= A307), V291 (= V338), Q293 (= Q340), R320 (= R367), V322 (= V369), K323 (= K370), G324 (= G371), A325 (= A372), Y326 (= Y373), W327 (= W374), Y345 (= Y392), T346 (= T393), R347 (= R394), K348 (= K395), T351 (= T398), A374 (= A421), T375 (= T422), H376 (= H423), N377 (= N424), C401 (= C448), L402 (= L449), E448 (= E490), S454 (= S496)
- binding cyclobutanecarboxylic acid: K218 (= K265), L402 (= L449), Y429 (= Y471), Y441 (= Y483), R444 (= R486), R445 (= R487)
7mwtA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with 1,1-cyclobutanedicarboxylate (see paper)
68% identity, 41% coverage: 32:537/1235 of query aligns to 5:499/499 of 7mwtA
- binding flavin-adenine dinucleotide: D259 (= D306), A260 (= A307), V291 (= V338), Q293 (= Q340), R320 (= R367), V322 (= V369), K323 (= K370), G324 (= G371), A325 (= A372), Y326 (= Y373), W327 (= W374), Y345 (= Y392), T346 (= T393), R347 (= R394), K348 (= K395), T351 (= T398), A374 (= A421), T375 (= T422), H376 (= H423), N377 (= N424), C401 (= C448), L402 (= L449), E448 (= E490), S454 (= S496)
- binding cyclobutane-1,1-dicarboxylic acid: K218 (= K265), Y326 (= Y373), Y429 (= Y471), Y441 (= Y483), R444 (= R486), R445 (= R487)
4jnyA Crystal structure of puta86-630 mutant d370a complexed with l- tetrahydro-2-furoic acid (see paper)
66% identity, 41% coverage: 27:537/1235 of query aligns to 1:491/491 of 4jnyA
- binding flavin-adenine dinucleotide: A252 (= A307), V283 (= V338), Q285 (= Q340), R312 (= R367), V314 (= V369), K315 (= K370), G316 (= G371), A317 (= A372), Y318 (= Y373), W319 (= W374), Y337 (= Y392), T338 (= T393), R339 (= R394), K340 (= K395), T343 (= T398), A366 (= A421), T367 (= T422), H368 (= H423), N369 (= N424), C393 (= C448), L394 (= L449), E440 (= E490), S446 (= S496), F447 (= F497)
- binding tetrahydrofuran-2-carboxylic acid: K210 (= K265), Y421 (= Y471), R436 (= R486), R437 (= R487)
1tj0A Crystal structure of e. Coli puta proline dehydrogenase domain (residues 86-669) co-crystallized with l-lactate (see paper)
64% identity, 41% coverage: 32:537/1235 of query aligns to 5:469/469 of 1tj0A
- binding flavin-adenine dinucleotide: D229 (= D306), A230 (= A307), V261 (= V338), Q263 (= Q340), R290 (= R367), V292 (= V369), K293 (= K370), G294 (= G371), A295 (= A372), Y296 (= Y373), W297 (= W374), Y315 (= Y392), T316 (= T393), R317 (= R394), K318 (= K395), T321 (= T398), A344 (= A421), T345 (= T422), H346 (= H423), N347 (= N424), Q370 (= Q447), C371 (= C448), L372 (= L449), E418 (= E490), S424 (= S496)
1tiwA Crystal structure of e. Coli puta proline dehydrogenase domain (residues 86-669) complexed with l-tetrahydro-2-furoic acid (see paper)
63% identity, 41% coverage: 27:537/1235 of query aligns to 1:459/459 of 1tiwA
- binding flavin-adenine dinucleotide: D219 (= D306), A220 (= A307), V251 (= V338), Q253 (= Q340), R280 (= R367), V282 (= V369), K283 (= K370), G284 (= G371), A285 (= A372), Y286 (= Y373), W287 (= W374), Y305 (= Y392), T306 (= T393), R307 (= R394), K308 (= K395), T311 (= T398), A334 (= A421), T335 (= T422), H336 (= H423), N337 (= N424), Q360 (= Q447), C361 (= C448), L362 (= L449), E408 (= E490), S414 (= S496)
- binding tetrahydrofuran-2-carboxylic acid: K178 (= K265), D219 (= D306), Y389 (= Y471), R404 (= R486), R405 (= R487)
Query Sequence
>AZOBR_RS23695 FitnessBrowser__azobra:AZOBR_RS23695
IDTRTAPPSAAPGEAAPFADFAPPIRPATELRAAITAAYRRPEPECLPFLFEQASLPPGV
ITAAAATARKLITALRAKPRGRGVEGLIHEYSLSSQEGMALMCLAEALLRIPDHATRDAL
IRDKIAGGDWQAHLGKGGSMFVNAATWGLLITGKLTSAGGEQALSSALTRLIARGGEPLI
RRGVDFAMRMMGEQFVTGQTIQEALTNARTMEAEGFRYSYDMLGEAALTAEDAARYYADY
VNAIHAIGTASAGRGVYEGPGISIKLSAIHPRYSRAQADRVMDELLPRVKALALLAKGYD
IGLNIDAEEADRLELSLDLMESLCFDPDLAGWNGIGFVVQAYGKRCPYVIDFLIDLARRS
GHRLMIRLVKGAYWDSEIKRAQLDGLPDFPVYTRKVYTDVSYVACARKLLAAPEAVFPQF
ATHNAQTLATIYEMAGSDFQVGKYEFQCLHGMGEPLYKEVVGPLKRPCRIYAPVGTHETL
LAYLVRRLLENGANSSFVNRIADPAVPVDELVADPVAVARAIAPTGAPHALIALPRNLYA
PERANSAGIDLSDETELARLSAALSASAEMTWTAAPLLADGERAGQAQPVRNPADRRDVV
GSVTEASEALVAEAFGHAVAAASAWAATPPEERAASLFRAADTMQERMPTLLGLIVREAG
KSLPNAIAEVREAIDFLRYYGAQVRDRFDNATHRPLGPVVCISPWNFPLAIFSGQIAAAL
AAGNPVLAKPAEETPLIAAEAVRILHAAGIPAGALQLLPGAGEVGAALVGHEAVRGVMFT
GSTEVARLIQRQLAGRLLPDGAPIPLIAETGGQNAMIVDSSALAEQVVGDVIASAFDSAG
QRCSALRILCLQEDVADRTLAMLKGAMRELRIGNPDRLAVDVGPVISEEARATIAAHIEA
MRAKGRNVEFLPLPAETADGTFIAPTVIEIGGIHELEREVFGPVLHVVRFHRDDLDALVD
SINATGYGLTFGLHTRIDATIERVTGRIGAGNVYVNRNTIGAVVGVQPFGGHGLSGTGPK
AGGPLYLSRLLSRRPKGWLEFRGPDAARAAGLAYGEWLRAKGFTAEASRCAGYVARSAIG
GGAELNGPVGERNLYELHGRGRVLLLPQTRTGLLLQLGAVLATGNSAAVDAPPDLAELLR
GLPPALAARVRTTADWRDVGPLAAVLVEGDRERVTAINRRVADLPGPILLVQAATAEALA
AGRGEGYDLDLLLNERSVSVNTAAAGGNASLVAMS
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