SitesBLAST
Comparing BWI76_RS10795 FitnessBrowser__Koxy:BWI76_RS10795 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)
59% identity, 94% coverage: 77:1320/1320 of query aligns to 4:1218/1218 of 6x9dA
- active site: N692 (= N779), K715 (= K802), E795 (= E883), C829 (= C917), E925 (= E1018), A1007 (= A1100)
- binding flavin-adenine dinucleotide: D291 (= D370), A292 (= A371), V323 (= V402), Q325 (= Q404), R352 (= R431), V354 (= V433), K355 (= K434), G356 (= G435), A357 (= A436), Y358 (= Y437), W359 (= W438), F377 (≠ Y456), T378 (= T457), R379 (= R458), K380 (= K459), T383 (= T462), A406 (= A485), T407 (= T486), H408 (= H487), N409 (= N488), Q432 (= Q511), C433 (= C512), E477 (= E559), S483 (= S565), F484 (= F566)
- binding 4-hydroxyproline: E659 (= E745), F693 (= F780), I697 (= I784), R828 (= R916), S830 (= S918), G987 (= G1080), A988 (= A1081), F995 (= F1088)
- binding nicotinamide-adenine-dinucleotide: I688 (= I775), S689 (= S776), P690 (= P777), W691 (= W778), N692 (= N779), I697 (= I784), K715 (= K802), A717 (= A804), E718 (= E805), G748 (= G835), G751 (= G839), A752 (= A840), T766 (= T854), G767 (= G855), S768 (= S856), V771 (= V859), E795 (= E883), T796 (= T884), C829 (= C917), E925 (= E1018), F927 (= F1020), F995 (= F1088)
7mybA Structure of proline utilization a with tetrahydrothiophene-2- carboxylate bound in the proline dehydrogenase active site (see paper)
59% identity, 94% coverage: 77:1320/1320 of query aligns to 4:1217/1217 of 7mybA
- binding flavin-adenine dinucleotide: D290 (= D370), A291 (= A371), V322 (= V402), Q324 (= Q404), R351 (= R431), V353 (= V433), K354 (= K434), G355 (= G435), A356 (= A436), Y357 (= Y437), W358 (= W438), F376 (≠ Y456), T377 (= T457), R378 (= R458), K379 (= K459), T382 (= T462), A405 (= A485), T406 (= T486), H407 (= H487), N408 (= N488), C432 (= C512), L433 (= L513), E476 (= E559), S482 (= S565), F483 (= F566)
- binding nicotinamide-adenine-dinucleotide: I687 (= I775), S688 (= S776), P689 (= P777), W690 (= W778), N691 (= N779), I696 (= I784), K714 (= K802), E717 (= E805), G747 (= G835), G750 (= G839), T765 (= T854), G766 (= G855), S767 (= S856), V770 (= V859), I774 (≠ L863), E794 (= E883), T795 (= T884), C828 (= C917), E924 (= E1018), F926 (= F1020), F994 (= F1088)
- binding (2S)-thiolane-2-carboxylic acid: K249 (= K329), Y457 (= Y540), Y469 (= Y552), R472 (= R555), R473 (= R556)
- binding (2R)-thiolane-2-carboxylic acid: K249 (= K329), D290 (= D370), Y457 (= Y540), Y469 (= Y552), R472 (= R555), R473 (= R556)
7myaA Structure of proline utilization a with the fad covalently-modified by 1,3-dithiolane (see paper)
59% identity, 94% coverage: 77:1320/1320 of query aligns to 4:1217/1217 of 7myaA
- binding nicotinamide-adenine-dinucleotide: I687 (= I775), S688 (= S776), P689 (= P777), W690 (= W778), N691 (= N779), I696 (= I784), K714 (= K802), A716 (= A804), E717 (= E805), G747 (= G835), G750 (= G839), A751 (= A840), T765 (= T854), G766 (= G855), S767 (= S856), V770 (= V859), E794 (= E883), T795 (= T884), C828 (= C917), E924 (= E1018), F926 (= F1020), F994 (= F1088)
- 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 (= D370), A291 (= A371), V322 (= V402), Q324 (= Q404), V353 (= V433), K354 (= K434), G355 (= G435), A356 (= A436), W358 (= W438), F376 (≠ Y456), T377 (= T457), R378 (= R458), K379 (= K459), T382 (= T462), A405 (= A485), T406 (= T486), H407 (= H487), N408 (= N488), Q431 (= Q511), C432 (= C512), L433 (= L513), Y457 (= Y540), E476 (= E559), G1217 (= G1320)
6x99A Structure of proline utilization a with d-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
59% identity, 94% coverage: 77:1320/1320 of query aligns to 4:1216/1216 of 6x99A
- active site: N690 (= N779), K713 (= K802), E793 (= E883), C827 (= C917), E923 (= E1018), A1005 (= A1100)
- binding d-proline: W557 (= W645), T558 (≠ Q646), E657 (= E745), F691 (= F780), R727 (≠ A816), R826 (= R916), S828 (= S918), G985 (= G1080), A986 (= A1081), F993 (= F1088)
- binding flavin-adenine dinucleotide: D289 (= D370), A290 (= A371), V321 (= V402), R350 (= R431), V352 (= V433), K353 (= K434), G354 (= G435), A355 (= A436), Y356 (= Y437), W357 (= W438), F375 (≠ Y456), T376 (= T457), R377 (= R458), K378 (= K459), T381 (= T462), A404 (= A485), T405 (= T486), H406 (= H487), N407 (= N488), Q430 (= Q511), C431 (= C512), Y456 (= Y540), E475 (= E559), S481 (= S565), F482 (= F566)
7my9A Structure of proline utilization a with 1,3-dithiolane-2-carboxylate bound in the proline dehydrogenase active site (see paper)
59% identity, 94% coverage: 77:1320/1320 of query aligns to 4:1216/1216 of 7my9A
- binding flavin-adenine dinucleotide: D289 (= D370), A290 (= A371), V321 (= V402), Q323 (= Q404), R350 (= R431), V352 (= V433), K353 (= K434), G354 (= G435), A355 (= A436), Y356 (= Y437), W357 (= W438), F375 (≠ Y456), T376 (= T457), R377 (= R458), K378 (= K459), T381 (= T462), A404 (= A485), T405 (= T486), H406 (= H487), N407 (= N488), C431 (= C512), L432 (= L513), E475 (= E559), S481 (= S565), F482 (= F566)
- binding nicotinamide-adenine-dinucleotide: I686 (= I775), S687 (= S776), P688 (= P777), W689 (= W778), N690 (= N779), I695 (= I784), K713 (= K802), A715 (= A804), E716 (= E805), G746 (= G835), G749 (= G839), A750 (= A840), T764 (= T854), G765 (= G855), S766 (= S856), V769 (= V859), E793 (= E883), T794 (= T884), C827 (= C917), E923 (= E1018), F925 (= F1020), F993 (= F1088)
- binding 1,3-dithiolane-2-carboxylic acid: Y456 (= Y540), Y468 (= Y552), R471 (= R555), R472 (= R556)
7mycA Structure of proline utilization a with the fad covalently modified by tetrahydrothiophene (see paper)
59% identity, 94% coverage: 77:1319/1320 of query aligns to 4:1216/1216 of 7mycA
- binding 1,4-dihydronicotinamide adenine dinucleotide: I687 (= I775), S688 (= S776), P689 (= P777), W690 (= W778), N691 (= N779), K714 (= K802), E717 (= E805), G747 (= G835), G750 (= G839), A751 (= A840), F764 (= F853), G766 (= G855), S767 (= S856), V770 (= V859), T795 (= T884), G796 (= G885), C828 (= C917), E924 (= E1018), F926 (= F1020)
- 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 (= K329), D290 (= D370), A291 (= A371), V322 (= V402), Q324 (= Q404), R351 (= R431), V353 (= V433), K354 (= K434), G355 (= G435), A356 (= A436), Y357 (= Y437), W358 (= W438), F376 (≠ Y456), T377 (= T457), R378 (= R458), K379 (= K459), T382 (= T462), A405 (= A485), T406 (= T486), H407 (= H487), N408 (= N488), Q431 (= Q511), C432 (= C512), L433 (= L513), Y457 (= Y540), S482 (= S565), F483 (= F566)
6x9aA Structure of proline utilization a with trans-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
59% identity, 94% coverage: 77:1320/1320 of query aligns to 4:1214/1214 of 6x9aA
- active site: N688 (= N779), K711 (= K802), E791 (= E883), C825 (= C917), E921 (= E1018), A1003 (= A1100)
- binding flavin-adenine dinucleotide: D287 (= D370), A288 (= A371), V319 (= V402), R348 (= R431), V350 (= V433), K351 (= K434), G352 (= G435), A353 (= A436), Y354 (= Y437), W355 (= W438), F373 (≠ Y456), T374 (= T457), R375 (= R458), K376 (= K459), T379 (= T462), A402 (= A485), T403 (= T486), H404 (= H487), N405 (= N488), C429 (= C512), E473 (= E559), S479 (= S565), F480 (= F566)
- binding (4S)-4-hydroxy-D-proline: W555 (= W645), T556 (≠ Q646), E655 (= E745), F689 (= F780), R725 (≠ A816), S826 (= S918), G983 (= G1080), A984 (= A1081), F991 (= F1088)
6x9bA Structure of proline utilization a with cis-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
59% identity, 94% coverage: 77:1320/1320 of query aligns to 4:1214/1214 of 6x9bA
- active site: N688 (= N779), K711 (= K802), E791 (= E883), C825 (= C917), E921 (= E1018), A1003 (= A1100)
- binding flavin-adenine dinucleotide: D287 (= D370), A288 (= A371), V319 (= V402), R348 (= R431), V350 (= V433), K351 (= K434), G352 (= G435), A353 (= A436), Y354 (= Y437), W355 (= W438), F373 (≠ Y456), T374 (= T457), R375 (= R458), K376 (= K459), T379 (= T462), A402 (= A485), T403 (= T486), H404 (= H487), N405 (= N488), Q428 (= Q511), C429 (= C512), Y454 (= Y540), E473 (= E559), S479 (= S565), F480 (= F566)
- binding nicotinamide-adenine-dinucleotide: I684 (= I775), S685 (= S776), P686 (= P777), W687 (= W778), N688 (= N779), I693 (= I784), K711 (= K802), A713 (= A804), E714 (= E805), G744 (= G835), G747 (= G839), A748 (= A840), T762 (= T854), G763 (= G855), S764 (= S856), V767 (= V859), I771 (≠ L863), E791 (= E883), T792 (= T884), C825 (= C917), E921 (= E1018), F923 (= F1020)
- binding (4R)-4-hydroxy-D-proline: E655 (= E745), F689 (= F780), S826 (= S918), G983 (= G1080), A984 (= A1081), F991 (= F1088)
6x9cA Structure of proline utilization a with l-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
59% identity, 94% coverage: 77:1316/1320 of query aligns to 3:1209/1209 of 6x9cA
- active site: N687 (= N779), K710 (= K802), E790 (= E883), C824 (= C917), E920 (= E1018), A1002 (= A1100)
- binding dihydroflavine-adenine dinucleotide: D286 (= D370), A287 (= A371), V318 (= V402), Q320 (= Q404), R347 (= R431), V349 (= V433), K350 (= K434), G351 (= G435), A352 (= A436), Y353 (= Y437), W354 (= W438), F372 (≠ Y456), T373 (= T457), R374 (= R458), K375 (= K459), T378 (= T462), A401 (= A485), T402 (= T486), H403 (= H487), N404 (= N488), Q427 (= Q511), C428 (= C512), E472 (= E559), S478 (= S565), F479 (= F566)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I683 (= I775), S684 (= S776), P685 (= P777), W686 (= W778), N687 (= N779), K710 (= K802), E713 (= E805), G743 (= G835), G746 (= G839), A747 (= A840), F760 (= F853), G762 (= G855), S763 (= S856), V766 (= V859), E920 (= E1018), F922 (= F1020)
- binding proline: R823 (= R916), C824 (= C917), S825 (= S918), G982 (= G1080), A983 (= A1081), F990 (= F1088)
5kf6A Structure of proline utilization a from sinorhizobium meliloti complexed with l-tetrahydrofuroic acid and NAD+ in space group p21 (see paper)
58% identity, 94% coverage: 77:1317/1320 of query aligns to 4:1206/1207 of 5kf6A
- active site: N683 (= N779), K706 (= K802), E786 (= E883), C820 (= C917), E916 (= E1018), A998 (= A1100)
- binding flavin-adenine dinucleotide: D282 (= D370), A283 (= A371), V314 (= V402), Q316 (= Q404), R343 (= R431), V345 (= V433), K346 (= K434), G347 (= G435), A348 (= A436), Y349 (= Y437), W350 (= W438), F368 (≠ Y456), T369 (= T457), R370 (= R458), K371 (= K459), T374 (= T462), A397 (= A485), T398 (= T486), H399 (= H487), N400 (= N488), Q423 (= Q511), C424 (= C512), L425 (= L513), E468 (= E559), S474 (= S565), F475 (= F566)
- binding nicotinamide-adenine-dinucleotide: I679 (= I775), S680 (= S776), P681 (= P777), W682 (= W778), N683 (= N779), I688 (= I784), K706 (= K802), A708 (= A804), E709 (= E805), G739 (= G835), G742 (= G839), A743 (= A840), F756 (= F853), T757 (= T854), G758 (= G855), S759 (= S856), V762 (= V859), I766 (≠ L863), E786 (= E883), T787 (= T884), C820 (= C917), E916 (= E1018), F918 (= F1020), F986 (= F1088)
- binding tetrahydrofuran-2-carboxylic acid: K241 (= K329), D282 (= D370), Y449 (= Y540), R464 (= R555), R465 (= R556)
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)
58% identity, 94% coverage: 77:1317/1320 of query aligns to 4:1196/1197 of 6ufpA
- active site: N673 (= N779), K696 (= K802), E776 (= E883), C810 (= C917), E906 (= E1018), A988 (= A1100)
- binding dihydroflavine-adenine dinucleotide: D285 (= D370), A286 (= A371), V317 (= V402), Q319 (= Q404), R346 (= R431), V348 (= V433), K349 (= K434), G350 (= G435), A351 (= A436), W353 (= W438), F371 (≠ Y456), T372 (= T457), R373 (= R458), K374 (= K459), T377 (= T462), A400 (= A485), T401 (= T486), H402 (= H487), N403 (= N488), Q426 (= Q511), C427 (= C512), L428 (= L513), S464 (= S565)
- binding nicotinamide-adenine-dinucleotide: I669 (= I775), P671 (= P777), W672 (= W778), N673 (= N779), I678 (= I784), K696 (= K802), E699 (= E805), G729 (= G835), G732 (= G839), F746 (= F853), T747 (= T854), G748 (= G855), S749 (= S856), V752 (= V859), E776 (= E883), T777 (= T884), C810 (= C917), E906 (= E1018), F908 (= F1020)
- binding (2S)-1,3-thiazolidine-2-carboxylic acid: K244 (= K329), D285 (= D370), Y439 (= Y540), Y451 (= Y552), R454 (= R555), R455 (= R556)
7sqnA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with (2s)-oxetane-2-carboxylic acid (see paper)
92% identity, 40% coverage: 88:610/1320 of query aligns to 1:503/503 of 7sqnA
- binding (2S)-oxetane-2-carboxylic acid: K222 (= K329), Y433 (= Y540), R448 (= R555), R449 (= R556)
- binding flavin-adenine dinucleotide: D263 (= D370), A264 (= A371), V295 (= V402), Q297 (= Q404), R324 (= R431), V326 (= V433), K327 (= K434), G328 (= G435), A329 (= A436), Y330 (= Y437), W331 (= W438), Y349 (= Y456), T350 (= T457), R351 (= R458), K352 (= K459), T355 (= T462), A378 (= A485), T379 (= T486), H380 (= H487), N381 (= N488), C405 (= C512), L406 (= L513), E452 (= E559), S458 (= S565)
7mwvA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclopropanecarboxylic acid (see paper)
91% identity, 40% coverage: 88:610/1320 of query aligns to 1:499/499 of 7mwvA
- binding flavin-adenine dinucleotide: D259 (= D370), A260 (= A371), V291 (= V402), Q293 (= Q404), R320 (= R431), V322 (= V433), K323 (= K434), G324 (= G435), A325 (= A436), Y326 (= Y437), W327 (= W438), Y345 (= Y456), T346 (= T457), R347 (= R458), K348 (= K459), T351 (= T462), A374 (= A485), T375 (= T486), H376 (= H487), N377 (= N488), C401 (= C512), L402 (= L513), E448 (= E559), S454 (= S565)
- binding cyclopropanecarboxylic acid: K218 (= K329), Y429 (= Y540), Y441 (= Y552), R444 (= R555), R445 (= R556)
7mwuA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclobutanecarboxylic acid (see paper)
91% identity, 40% coverage: 88:610/1320 of query aligns to 1:499/499 of 7mwuA
- binding flavin-adenine dinucleotide: D259 (= D370), A260 (= A371), V291 (= V402), Q293 (= Q404), R320 (= R431), V322 (= V433), K323 (= K434), G324 (= G435), A325 (= A436), Y326 (= Y437), W327 (= W438), Y345 (= Y456), T346 (= T457), R347 (= R458), K348 (= K459), T351 (= T462), A374 (= A485), T375 (= T486), H376 (= H487), N377 (= N488), C401 (= C512), L402 (= L513), E448 (= E559), S454 (= S565)
- binding cyclobutanecarboxylic acid: K218 (= K329), L402 (= L513), Y429 (= Y540), Y441 (= Y552), R444 (= R555), R445 (= R556)
7mwtA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with 1,1-cyclobutanedicarboxylate (see paper)
91% identity, 40% coverage: 88:610/1320 of query aligns to 1:499/499 of 7mwtA
- binding flavin-adenine dinucleotide: D259 (= D370), A260 (= A371), V291 (= V402), Q293 (= Q404), R320 (= R431), V322 (= V433), K323 (= K434), G324 (= G435), A325 (= A436), Y326 (= Y437), W327 (= W438), Y345 (= Y456), T346 (= T457), R347 (= R458), K348 (= K459), T351 (= T462), A374 (= A485), T375 (= T486), H376 (= H487), N377 (= N488), C401 (= C512), L402 (= L513), E448 (= E559), S454 (= S565)
- binding cyclobutane-1,1-dicarboxylic acid: K218 (= K329), Y326 (= Y437), Y429 (= Y540), Y441 (= Y552), R444 (= R555), R445 (= R556)
4jnyA Crystal structure of puta86-630 mutant d370a complexed with l- tetrahydro-2-furoic acid (see paper)
89% identity, 40% coverage: 87:610/1320 of query aligns to 1:491/491 of 4jnyA
- binding flavin-adenine dinucleotide: A252 (= A371), V283 (= V402), Q285 (= Q404), R312 (= R431), V314 (= V433), K315 (= K434), G316 (= G435), A317 (= A436), Y318 (= Y437), W319 (= W438), Y337 (= Y456), T338 (= T457), R339 (= R458), K340 (= K459), T343 (= T462), A366 (= A485), T367 (= T486), H368 (= H487), N369 (= N488), C393 (= C512), L394 (= L513), E440 (= E559), S446 (= S565), F447 (= F566)
- binding tetrahydrofuran-2-carboxylic acid: K210 (= K329), Y421 (= Y540), R436 (= R555), R437 (= R556)
3e2sA Crystal structure reduced puta86-630 mutant y540s complexed with l- proline (see paper)
84% identity, 40% coverage: 88:610/1320 of query aligns to 1:468/468 of 3e2sA
- binding flavin-adenine dinucleotide: D228 (= D370), A229 (= A371), V260 (= V402), Q262 (= Q404), V291 (= V433), K292 (= K434), G293 (= G435), A294 (= A436), Y295 (= Y437), W296 (= W438), Y314 (= Y456), T315 (= T457), R316 (= R458), K317 (= K459), T320 (= T462), A343 (= A485), T344 (= T486), H345 (= H487), N346 (= N488), C370 (= C512), L371 (= L513), E417 (= E559), S423 (= S565), F424 (= F566)
- binding proline: K187 (= K329), L371 (= L513), Y410 (= Y552), R413 (= R555), R414 (= R556)
3e2qA Crystal structure reduced puta86-630 mutant y540s complexed with trans-4-hydroxy-l-proline (see paper)
84% identity, 40% coverage: 88:610/1320 of query aligns to 1:468/468 of 3e2qA
- binding flavin-adenine dinucleotide: D228 (= D370), A229 (= A371), V260 (= V402), Q262 (= Q404), V291 (= V433), K292 (= K434), G293 (= G435), A294 (= A436), Y295 (= Y437), W296 (= W438), Y314 (= Y456), T315 (= T457), R316 (= R458), K317 (= K459), T320 (= T462), A343 (= A485), T344 (= T486), H345 (= H487), N346 (= N488), Q369 (= Q511), C370 (= C512), L371 (= L513), E417 (= E559), S423 (= S565), F424 (= F566)
- binding 4-hydroxyproline: D143 (= D285), K187 (= K329), D228 (= D370), Y410 (= Y552), R413 (= R555), R414 (= R556)
1tj0A Crystal structure of e. Coli puta proline dehydrogenase domain (residues 86-669) co-crystallized with l-lactate (see paper)
84% identity, 40% coverage: 88:610/1320 of query aligns to 1:469/469 of 1tj0A
- binding flavin-adenine dinucleotide: D229 (= D370), A230 (= A371), V261 (= V402), Q263 (= Q404), R290 (= R431), V292 (= V433), K293 (= K434), G294 (= G435), A295 (= A436), Y296 (= Y437), W297 (= W438), Y315 (= Y456), T316 (= T457), R317 (= R458), K318 (= K459), T321 (= T462), A344 (= A485), T345 (= T486), H346 (= H487), N347 (= N488), Q370 (= Q511), C371 (= C512), L372 (= L513), E418 (= E559), S424 (= S565)
1tiwA Crystal structure of e. Coli puta proline dehydrogenase domain (residues 86-669) complexed with l-tetrahydro-2-furoic acid (see paper)
83% identity, 40% coverage: 87:610/1320 of query aligns to 1:459/459 of 1tiwA
- binding flavin-adenine dinucleotide: D219 (= D370), A220 (= A371), V251 (= V402), Q253 (= Q404), R280 (= R431), V282 (= V433), K283 (= K434), G284 (= G435), A285 (= A436), Y286 (= Y437), W287 (= W438), Y305 (= Y456), T306 (= T457), R307 (= R458), K308 (= K459), T311 (= T462), A334 (= A485), T335 (= T486), H336 (= H487), N337 (= N488), Q360 (= Q511), C361 (= C512), L362 (= L513), E408 (= E559), S414 (= S565)
- binding tetrahydrofuran-2-carboxylic acid: K178 (= K329), D219 (= D370), Y389 (= Y540), R404 (= R555), R405 (= R556)
Query Sequence
>BWI76_RS10795 FitnessBrowser__Koxy:BWI76_RS10795
MGTTTMGVKLDDATRERIKSAASRIDRTPHWLIKQAIFNYLEKLENDETLPELPALLSGA
ANESDEAGNPADEPYQPFLDFAEQILPQSVSRASITAAWRWAETDAVPMLLEQARLPQTL
GEQAHKLAYQLAEKLRNQKTASGRAGMVQSLLQEFSLSSQEGVALMCLAEALLRIPDKAT
RDALIRDKISNGNWQSHIGRSPSLFVNAATWGLLFTGKLVSPHNETSLSRSLNRIIGKSG
EPLIRKGVDMAMRLMGEQFVTGETIAEALANARKLEDKGFRYSYDMLGEAALTADDAQAY
MVSYQQAIHAIGKASNGRGIYEGPGISIKLSALHPRYSRAQYDRAMEELYPRLKSLTLLA
RQYDIGINIDAEEADRLEISLDLLEKLCFEPELAGWNGIGFVIQAYQKRCPFVIDYLIDL
ATRSRRRLMIRLVKGAYWDSEIKRAQMDGLEGYPVYTRKVYTDVSYLACAKKLLAVPNLI
YPQFATHNAHTLAAIYQLAGQNYYPGQYEFQCLHGMGEPLYEQVTGKIADGKLNRPCRIY
APVGTHETLLAYLVRRLLENGANTSFVNRIADSTLPLDELVADPVAAVEKLAQQEGQVGL
PHPKIPLPRDLYGKGRSNSAGLDLANEHRLASLSSSLLNSALHKWQALPMLEQPVAEGEM
QPVINPAEPKDIVGYVREASDDEVQQALTSAVNNAPIWFATPPQERAAILERAAVLMEGQ
MPTLMGILVREAGKTFSNAIAEVREAVDFLHYYAGQVRNDFDNETHRPLGPVVCISPWNF
PLAIFSGQIAAALAAGNTVLAKPAEQTPLIAAQGVAILLEAGVPPGVIQLLPGRGETVGA
ALTSDERVRGVMFTGSTEVATLLQRNIASRLDAQGRPTPLIAETGGMNAMIVDSSALTEQ
VVIDVLASAFDSAGQRCSALRVLCLQDDIADHTLTMLRGAMAECRMGNPGRLTTDIGPVI
DAEAKENIERHIQTLRAKGRKVFQAVRENGEDSREWASGTFVPPTLIELDSFDELKKEVF
GPVLHVVRYNRNELEGLVEQINASGYGLTLGVHTRIDETIAQVTGSANVGNLYVNRNMVG
AVVGVQPFGGEGLSGTGPKAGGPLYLYRLLSSRPQNAVGITLARQDPEYPLDAQLKTLLE
KPLVALQQWAADRPELQALCQQFSKQAQAGTQRLLPGPTGERNTLTFMPRDRVLCVADNE
QDALTQLAGVTAVGCEVLWPDAPLQRELAKKLPREVSERIHFAKAETLTTEPFDAVIYHG
DSDQLRELCEQVAARDGAIVSVQGFARGESNLLLERLYIERSLSVNTAAAGGNASLMTIG
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