SitesBLAST
Comparing GFF427 FitnessBrowser__WCS417:GFF427 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)
60% identity, 94% coverage: 76:1317/1317 of query aligns to 5:1218/1218 of 6x9dA
- active site: N692 (= N777), K715 (= K800), E795 (= E881), C829 (= C915), E925 (= E1013), A1007 (= A1095)
- binding flavin-adenine dinucleotide: D291 (= D368), A292 (= A369), V323 (= V400), Q325 (= Q402), R352 (= R429), V354 (= V431), K355 (= K432), G356 (= G433), A357 (= A434), Y358 (= Y435), W359 (= W436), F377 (≠ Y454), T378 (= T455), R379 (= R456), K380 (= K457), T383 (= T460), A406 (= A483), T407 (= T484), H408 (= H485), N409 (= N486), Q432 (= Q509), C433 (= C510), E477 (= E557), S483 (= S563), F484 (= F564)
- binding 4-hydroxyproline: E659 (= E743), F693 (= F778), I697 (= I782), R828 (= R914), S830 (= S916), G987 (= G1075), A988 (= A1076), F995 (= F1083)
- binding nicotinamide-adenine-dinucleotide: I688 (= I773), S689 (= S774), P690 (= P775), W691 (= W776), N692 (= N777), I697 (= I782), K715 (= K800), A717 (= A802), E718 (= E803), G748 (= G833), G751 (= G837), A752 (= A838), T766 (= T852), G767 (= G853), S768 (= S854), V771 (= V857), E795 (= E881), T796 (= T882), C829 (= C915), E925 (= E1013), F927 (= F1015), F995 (= F1083)
7mybA Structure of proline utilization a with tetrahydrothiophene-2- carboxylate bound in the proline dehydrogenase active site (see paper)
60% identity, 94% coverage: 76:1317/1317 of query aligns to 5:1217/1217 of 7mybA
- binding flavin-adenine dinucleotide: D290 (= D368), A291 (= A369), V322 (= V400), Q324 (= Q402), R351 (= R429), V353 (= V431), K354 (= K432), G355 (= G433), A356 (= A434), Y357 (= Y435), W358 (= W436), F376 (≠ Y454), T377 (= T455), R378 (= R456), K379 (= K457), T382 (= T460), A405 (= A483), T406 (= T484), H407 (= H485), N408 (= N486), C432 (= C510), L433 (= L511), E476 (= E557), S482 (= S563), F483 (= F564)
- binding nicotinamide-adenine-dinucleotide: I687 (= I773), S688 (= S774), P689 (= P775), W690 (= W776), N691 (= N777), I696 (= I782), K714 (= K800), E717 (= E803), G747 (= G833), G750 (= G837), T765 (= T852), G766 (= G853), S767 (= S854), V770 (= V857), I774 (≠ L861), E794 (= E881), T795 (= T882), C828 (= C915), E924 (= E1013), F926 (= F1015), F994 (= F1083)
- binding (2S)-thiolane-2-carboxylic acid: K249 (= K327), Y457 (= Y538), Y469 (= Y550), R472 (= R553), R473 (= R554)
- binding (2R)-thiolane-2-carboxylic acid: K249 (= K327), D290 (= D368), Y457 (= Y538), Y469 (= Y550), R472 (= R553), R473 (= R554)
7myaA Structure of proline utilization a with the fad covalently-modified by 1,3-dithiolane (see paper)
60% identity, 94% coverage: 76:1317/1317 of query aligns to 5:1217/1217 of 7myaA
- binding nicotinamide-adenine-dinucleotide: I687 (= I773), S688 (= S774), P689 (= P775), W690 (= W776), N691 (= N777), I696 (= I782), K714 (= K800), A716 (= A802), E717 (= E803), G747 (= G833), G750 (= G837), A751 (= A838), T765 (= T852), G766 (= G853), S767 (= S854), V770 (= V857), E794 (= E881), T795 (= T882), C828 (= C915), E924 (= E1013), F926 (= F1015), F994 (= F1083)
- 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 (= D368), A291 (= A369), V322 (= V400), Q324 (= Q402), V353 (= V431), K354 (= K432), G355 (= G433), A356 (= A434), W358 (= W436), F376 (≠ Y454), T377 (= T455), R378 (= R456), K379 (= K457), T382 (= T460), A405 (= A483), T406 (= T484), H407 (= H485), N408 (= N486), Q431 (= Q509), C432 (= C510), L433 (= L511), Y457 (= Y538), E476 (= E557), G1217 (= G1317)
7mycA Structure of proline utilization a with the fad covalently modified by tetrahydrothiophene (see paper)
60% identity, 94% coverage: 76:1316/1317 of query aligns to 5:1216/1216 of 7mycA
- binding 1,4-dihydronicotinamide adenine dinucleotide: I687 (= I773), S688 (= S774), P689 (= P775), W690 (= W776), N691 (= N777), K714 (= K800), E717 (= E803), G747 (= G833), G750 (= G837), A751 (= A838), F764 (= F851), G766 (= G853), S767 (= S854), V770 (= V857), T795 (= T882), G796 (= G883), C828 (= C915), E924 (= E1013), F926 (= F1015)
- 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 (= K327), D290 (= D368), A291 (= A369), V322 (= V400), Q324 (= Q402), R351 (= R429), V353 (= V431), K354 (= K432), G355 (= G433), A356 (= A434), Y357 (= Y435), W358 (= W436), F376 (≠ Y454), T377 (= T455), R378 (= R456), K379 (= K457), T382 (= T460), A405 (= A483), T406 (= T484), H407 (= H485), N408 (= N486), Q431 (= Q509), C432 (= C510), L433 (= L511), Y457 (= Y538), S482 (= S563), F483 (= F564)
6x99A Structure of proline utilization a with d-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
60% identity, 94% coverage: 76:1317/1317 of query aligns to 5:1216/1216 of 6x99A
- active site: N690 (= N777), K713 (= K800), E793 (= E881), C827 (= C915), E923 (= E1013), A1005 (= A1095)
- binding d-proline: W557 (= W643), T558 (≠ K644), E657 (= E743), F691 (= F778), R727 (= R814), R826 (= R914), S828 (= S916), G985 (= G1075), A986 (= A1076), F993 (= F1083)
- binding flavin-adenine dinucleotide: D289 (= D368), A290 (= A369), V321 (= V400), R350 (= R429), V352 (= V431), K353 (= K432), G354 (= G433), A355 (= A434), Y356 (= Y435), W357 (= W436), F375 (≠ Y454), T376 (= T455), R377 (= R456), K378 (= K457), T381 (= T460), A404 (= A483), T405 (= T484), H406 (= H485), N407 (= N486), Q430 (= Q509), C431 (= C510), Y456 (= Y538), E475 (= E557), S481 (= S563), F482 (= F564)
7my9A Structure of proline utilization a with 1,3-dithiolane-2-carboxylate bound in the proline dehydrogenase active site (see paper)
60% identity, 94% coverage: 76:1317/1317 of query aligns to 5:1216/1216 of 7my9A
- binding flavin-adenine dinucleotide: D289 (= D368), A290 (= A369), V321 (= V400), Q323 (= Q402), R350 (= R429), V352 (= V431), K353 (= K432), G354 (= G433), A355 (= A434), Y356 (= Y435), W357 (= W436), F375 (≠ Y454), T376 (= T455), R377 (= R456), K378 (= K457), T381 (= T460), A404 (= A483), T405 (= T484), H406 (= H485), N407 (= N486), C431 (= C510), L432 (= L511), E475 (= E557), S481 (= S563), F482 (= F564)
- binding nicotinamide-adenine-dinucleotide: I686 (= I773), S687 (= S774), P688 (= P775), W689 (= W776), N690 (= N777), I695 (= I782), K713 (= K800), A715 (= A802), E716 (= E803), G746 (= G833), G749 (= G837), A750 (= A838), T764 (= T852), G765 (= G853), S766 (= S854), V769 (= V857), E793 (= E881), T794 (= T882), C827 (= C915), E923 (= E1013), F925 (= F1015), F993 (= F1083)
- binding 1,3-dithiolane-2-carboxylic acid: Y456 (= Y538), Y468 (= Y550), R471 (= R553), R472 (= R554)
6x9aA Structure of proline utilization a with trans-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
60% identity, 94% coverage: 76:1317/1317 of query aligns to 5:1214/1214 of 6x9aA
- active site: N688 (= N777), K711 (= K800), E791 (= E881), C825 (= C915), E921 (= E1013), A1003 (= A1095)
- binding flavin-adenine dinucleotide: D287 (= D368), A288 (= A369), V319 (= V400), R348 (= R429), V350 (= V431), K351 (= K432), G352 (= G433), A353 (= A434), Y354 (= Y435), W355 (= W436), F373 (≠ Y454), T374 (= T455), R375 (= R456), K376 (= K457), T379 (= T460), A402 (= A483), T403 (= T484), H404 (= H485), N405 (= N486), C429 (= C510), E473 (= E557), S479 (= S563), F480 (= F564)
- binding (4S)-4-hydroxy-D-proline: W555 (= W643), T556 (≠ K644), E655 (= E743), F689 (= F778), R725 (= R814), S826 (= S916), G983 (= G1075), A984 (= A1076), F991 (= F1083)
6x9bA Structure of proline utilization a with cis-4-hydroxy-d-proline bound in the l-glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
60% identity, 94% coverage: 76:1317/1317 of query aligns to 5:1214/1214 of 6x9bA
- active site: N688 (= N777), K711 (= K800), E791 (= E881), C825 (= C915), E921 (= E1013), A1003 (= A1095)
- binding flavin-adenine dinucleotide: D287 (= D368), A288 (= A369), V319 (= V400), R348 (= R429), V350 (= V431), K351 (= K432), G352 (= G433), A353 (= A434), Y354 (= Y435), W355 (= W436), F373 (≠ Y454), T374 (= T455), R375 (= R456), K376 (= K457), T379 (= T460), A402 (= A483), T403 (= T484), H404 (= H485), N405 (= N486), Q428 (= Q509), C429 (= C510), Y454 (= Y538), E473 (= E557), S479 (= S563), F480 (= F564)
- binding nicotinamide-adenine-dinucleotide: I684 (= I773), S685 (= S774), P686 (= P775), W687 (= W776), N688 (= N777), I693 (= I782), K711 (= K800), A713 (= A802), E714 (= E803), G744 (= G833), G747 (= G837), A748 (= A838), T762 (= T852), G763 (= G853), S764 (= S854), V767 (= V857), I771 (≠ L861), E791 (= E881), T792 (= T882), C825 (= C915), E921 (= E1013), F923 (= F1015)
- binding (4R)-4-hydroxy-D-proline: E655 (= E743), F689 (= F778), S826 (= S916), G983 (= G1075), A984 (= A1076), F991 (= F1083)
6x9cA Structure of proline utilization a with l-proline bound in the l- glutamate-gamma-semialdehyde dehydrogenase active site (see paper)
60% identity, 94% coverage: 76:1313/1317 of query aligns to 4:1209/1209 of 6x9cA
- active site: N687 (= N777), K710 (= K800), E790 (= E881), C824 (= C915), E920 (= E1013), A1002 (= A1095)
- binding dihydroflavine-adenine dinucleotide: D286 (= D368), A287 (= A369), V318 (= V400), Q320 (= Q402), R347 (= R429), V349 (= V431), K350 (= K432), G351 (= G433), A352 (= A434), Y353 (= Y435), W354 (= W436), F372 (≠ Y454), T373 (= T455), R374 (= R456), K375 (= K457), T378 (= T460), A401 (= A483), T402 (= T484), H403 (= H485), N404 (= N486), Q427 (= Q509), C428 (= C510), E472 (= E557), S478 (= S563), F479 (= F564)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I683 (= I773), S684 (= S774), P685 (= P775), W686 (= W776), N687 (= N777), K710 (= K800), E713 (= E803), G743 (= G833), G746 (= G837), A747 (= A838), F760 (= F851), G762 (= G853), S763 (= S854), V766 (= V857), E920 (= E1013), F922 (= F1015)
- binding proline: R823 (= R914), C824 (= C915), S825 (= S916), G982 (= G1075), A983 (= A1076), F990 (= F1083)
5kf6A Structure of proline utilization a from sinorhizobium meliloti complexed with l-tetrahydrofuroic acid and NAD+ in space group p21 (see paper)
60% identity, 94% coverage: 76:1314/1317 of query aligns to 5:1206/1207 of 5kf6A
- active site: N683 (= N777), K706 (= K800), E786 (= E881), C820 (= C915), E916 (= E1013), A998 (= A1095)
- binding flavin-adenine dinucleotide: D282 (= D368), A283 (= A369), V314 (= V400), Q316 (= Q402), R343 (= R429), V345 (= V431), K346 (= K432), G347 (= G433), A348 (= A434), Y349 (= Y435), W350 (= W436), F368 (≠ Y454), T369 (= T455), R370 (= R456), K371 (= K457), T374 (= T460), A397 (= A483), T398 (= T484), H399 (= H485), N400 (= N486), Q423 (= Q509), C424 (= C510), L425 (= L511), E468 (= E557), S474 (= S563), F475 (= F564)
- binding nicotinamide-adenine-dinucleotide: I679 (= I773), S680 (= S774), P681 (= P775), W682 (= W776), N683 (= N777), I688 (= I782), K706 (= K800), A708 (= A802), E709 (= E803), G739 (= G833), G742 (= G837), A743 (= A838), F756 (= F851), T757 (= T852), G758 (= G853), S759 (= S854), V762 (= V857), I766 (≠ L861), E786 (= E881), T787 (= T882), C820 (= C915), E916 (= E1013), F918 (= F1015), F986 (= F1083)
- binding tetrahydrofuran-2-carboxylic acid: K241 (= K327), D282 (= D368), Y449 (= Y538), R464 (= R553), R465 (= R554)
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)
59% identity, 94% coverage: 76:1314/1317 of query aligns to 5:1196/1197 of 6ufpA
- active site: N673 (= N777), K696 (= K800), E776 (= E881), C810 (= C915), E906 (= E1013), A988 (= A1095)
- binding dihydroflavine-adenine dinucleotide: D285 (= D368), A286 (= A369), V317 (= V400), Q319 (= Q402), R346 (= R429), V348 (= V431), K349 (= K432), G350 (= G433), A351 (= A434), W353 (= W436), F371 (≠ Y454), T372 (= T455), R373 (= R456), K374 (= K457), T377 (= T460), A400 (= A483), T401 (= T484), H402 (= H485), N403 (= N486), Q426 (= Q509), C427 (= C510), L428 (= L511), S464 (= S563)
- binding nicotinamide-adenine-dinucleotide: I669 (= I773), P671 (= P775), W672 (= W776), N673 (= N777), I678 (= I782), K696 (= K800), E699 (= E803), G729 (= G833), G732 (= G837), F746 (= F851), T747 (= T852), G748 (= G853), S749 (= S854), V752 (= V857), E776 (= E881), T777 (= T882), C810 (= C915), E906 (= E1013), F908 (= F1015)
- binding (2S)-1,3-thiazolidine-2-carboxylic acid: K244 (= K327), D285 (= D368), Y439 (= Y538), Y451 (= Y550), R454 (= R553), R455 (= R554)
7sqnA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with (2s)-oxetane-2-carboxylic acid (see paper)
81% identity, 40% coverage: 86:608/1317 of query aligns to 1:503/503 of 7sqnA
- binding (2S)-oxetane-2-carboxylic acid: K222 (= K327), Y433 (= Y538), R448 (= R553), R449 (= R554)
- binding flavin-adenine dinucleotide: D263 (= D368), A264 (= A369), V295 (= V400), Q297 (= Q402), R324 (= R429), V326 (= V431), K327 (= K432), G328 (= G433), A329 (= A434), Y330 (= Y435), W331 (= W436), Y349 (= Y454), T350 (= T455), R351 (= R456), K352 (= K457), T355 (= T460), A378 (= A483), T379 (= T484), H380 (= H485), N381 (= N486), C405 (= C510), L406 (= L511), E452 (= E557), S458 (= S563)
7mwvA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclopropanecarboxylic acid (see paper)
80% identity, 40% coverage: 86:608/1317 of query aligns to 1:499/499 of 7mwvA
- binding flavin-adenine dinucleotide: D259 (= D368), A260 (= A369), V291 (= V400), Q293 (= Q402), R320 (= R429), V322 (= V431), K323 (= K432), G324 (= G433), A325 (= A434), Y326 (= Y435), W327 (= W436), Y345 (= Y454), T346 (= T455), R347 (= R456), K348 (= K457), T351 (= T460), A374 (= A483), T375 (= T484), H376 (= H485), N377 (= N486), C401 (= C510), L402 (= L511), E448 (= E557), S454 (= S563)
- binding cyclopropanecarboxylic acid: K218 (= K327), Y429 (= Y538), Y441 (= Y550), R444 (= R553), R445 (= R554)
7mwuA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclobutanecarboxylic acid (see paper)
80% identity, 40% coverage: 86:608/1317 of query aligns to 1:499/499 of 7mwuA
- binding flavin-adenine dinucleotide: D259 (= D368), A260 (= A369), V291 (= V400), Q293 (= Q402), R320 (= R429), V322 (= V431), K323 (= K432), G324 (= G433), A325 (= A434), Y326 (= Y435), W327 (= W436), Y345 (= Y454), T346 (= T455), R347 (= R456), K348 (= K457), T351 (= T460), A374 (= A483), T375 (= T484), H376 (= H485), N377 (= N486), C401 (= C510), L402 (= L511), E448 (= E557), S454 (= S563)
- binding cyclobutanecarboxylic acid: K218 (= K327), L402 (= L511), Y429 (= Y538), Y441 (= Y550), R444 (= R553), R445 (= R554)
7mwtA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with 1,1-cyclobutanedicarboxylate (see paper)
80% identity, 40% coverage: 86:608/1317 of query aligns to 1:499/499 of 7mwtA
- binding flavin-adenine dinucleotide: D259 (= D368), A260 (= A369), V291 (= V400), Q293 (= Q402), R320 (= R429), V322 (= V431), K323 (= K432), G324 (= G433), A325 (= A434), Y326 (= Y435), W327 (= W436), Y345 (= Y454), T346 (= T455), R347 (= R456), K348 (= K457), T351 (= T460), A374 (= A483), T375 (= T484), H376 (= H485), N377 (= N486), C401 (= C510), L402 (= L511), E448 (= E557), S454 (= S563)
- binding cyclobutane-1,1-dicarboxylic acid: K218 (= K327), Y326 (= Y435), Y429 (= Y538), Y441 (= Y550), R444 (= R553), R445 (= R554)
6bsnA Structure of proline utilization a (puta) with proline bound in remote sites (see paper)
47% identity, 77% coverage: 93:1104/1317 of query aligns to 8:960/973 of 6bsnA
- active site: N643 (= N777), E743 (= E881), A777 (≠ C915), A951 (= A1095)
- binding dihydroflavine-adenine dinucleotide: D269 (= D368), A270 (= A369), Q303 (= Q402), R330 (= R429), V332 (= V431), K333 (= K432), G334 (= G433), A335 (= A434), Y336 (= Y435), W337 (= W436), F355 (≠ Y454), T356 (= T455), R357 (= R456), K358 (= K457), T361 (= T460), A384 (= A483), T385 (= T484), H386 (= H485), N387 (= N486), Y432 (= Y538), S457 (= S563), F458 (= F564)
- binding proline: M630 (vs. gap), W642 (= W776), F644 (= F778), G718 (= G853), R776 (= R914), S778 (= S916), F871 (= F1015), I930 (≠ V1074), G931 (= G1075), A932 (= A1076), F939 (= F1083), A958 (≠ Y1102), R959 (= R1103)
Sites not aligning to the query:
3hazA Crystal structure of bifunctional proline utilization a (puta) protein (see paper)
47% identity, 77% coverage: 93:1104/1317 of query aligns to 8:969/983 of 3hazA
- active site: N652 (= N777), K675 (= K800), E752 (= E881), C786 (= C915), E878 (= E1013), A960 (= A1095)
- binding flavin-adenine dinucleotide: D272 (= D368), A273 (= A369), Q306 (= Q402), R333 (= R429), V335 (= V431), K336 (= K432), G337 (= G433), A338 (= A434), Y339 (= Y435), W340 (= W436), F358 (≠ Y454), T359 (= T455), R360 (= R456), K361 (= K457), T364 (= T460), A387 (= A483), T388 (= T484), H389 (= H485), N390 (= N486), Y435 (= Y538), S460 (= S563), F461 (= F564)
- binding nicotinamide-adenine-dinucleotide: I648 (= I773), S649 (= S774), P650 (= P775), W651 (= W776), N652 (= N777), I657 (= I782), K675 (= K800), P676 (= P801), A677 (= A802), G708 (= G833), G711 (= G837), A712 (= A838), T726 (= T852), G727 (= G853), S728 (= S854), V731 (= V857), I735 (≠ L861), E752 (= E881), T753 (= T882), C786 (= C915), E878 (= E1013), F880 (= F1015), F948 (= F1083)
4jnyA Crystal structure of puta86-630 mutant d370a complexed with l- tetrahydro-2-furoic acid (see paper)
79% identity, 40% coverage: 85:608/1317 of query aligns to 1:491/491 of 4jnyA
- binding flavin-adenine dinucleotide: A252 (= A369), V283 (= V400), Q285 (= Q402), R312 (= R429), V314 (= V431), K315 (= K432), G316 (= G433), A317 (= A434), Y318 (= Y435), W319 (= W436), Y337 (= Y454), T338 (= T455), R339 (= R456), K340 (= K457), T343 (= T460), A366 (= A483), T367 (= T484), H368 (= H485), N369 (= N486), C393 (= C510), L394 (= L511), E440 (= E557), S446 (= S563), F447 (= F564)
- binding tetrahydrofuran-2-carboxylic acid: K210 (= K327), Y421 (= Y538), R436 (= R553), R437 (= R554)
3e2sA Crystal structure reduced puta86-630 mutant y540s complexed with l- proline (see paper)
75% identity, 40% coverage: 86:608/1317 of query aligns to 1:468/468 of 3e2sA
- binding flavin-adenine dinucleotide: D228 (= D368), A229 (= A369), V260 (= V400), Q262 (= Q402), V291 (= V431), K292 (= K432), G293 (= G433), A294 (= A434), Y295 (= Y435), W296 (= W436), Y314 (= Y454), T315 (= T455), R316 (= R456), K317 (= K457), T320 (= T460), A343 (= A483), T344 (= T484), H345 (= H485), N346 (= N486), C370 (= C510), L371 (= L511), E417 (= E557), S423 (= S563), F424 (= F564)
- binding proline: K187 (= K327), L371 (= L511), Y410 (= Y550), R413 (= R553), R414 (= R554)
3e2qA Crystal structure reduced puta86-630 mutant y540s complexed with trans-4-hydroxy-l-proline (see paper)
75% identity, 40% coverage: 86:608/1317 of query aligns to 1:468/468 of 3e2qA
- binding flavin-adenine dinucleotide: D228 (= D368), A229 (= A369), V260 (= V400), Q262 (= Q402), V291 (= V431), K292 (= K432), G293 (= G433), A294 (= A434), Y295 (= Y435), W296 (= W436), Y314 (= Y454), T315 (= T455), R316 (= R456), K317 (= K457), T320 (= T460), A343 (= A483), T344 (= T484), H345 (= H485), N346 (= N486), Q369 (= Q509), C370 (= C510), L371 (= L511), E417 (= E557), S423 (= S563), F424 (= F564)
- binding 4-hydroxyproline: D143 (= D283), K187 (= K327), D228 (= D368), Y410 (= Y550), R413 (= R553), R414 (= R554)
Query Sequence
>GFF427 FitnessBrowser__WCS417:GFF427
MATTTLGVKLDDPTRERLKAAATSIDRTPHWLIKQAIFNYLEKLEGGATLTELNGLSSKD
ADDAGEVQTDHAHQCFLEFAESILPQSVLRASITAAYRRPEPEVVPMLIEQARLPTPMAE
ATNKLAASIAEKLRNQKSAGGRAGIVQGLLQEFSLSSQEGVALMCLAEALLRIPDKGTRD
ALIRDKISTGNWQPHLGNSPSLFVNAATWGLLLTGKLVATHNEAGLTSSLSRIIGKSGEP
MIRKGVDMAMRLMGEQFVTGETIAEALANASKFEAKGFRYSYDMLGEAALTEHDAQKYLA
SYEQAIHSIGKASHGRGIYEGPGISIKLSALHPRYSRAQYERVMDELYPRLLSLTLLAKQ
YDIGLNIDAEEADRLELSLDLLERLCFEPQLTGWNGIGFVIQAYQKRCPYVIDYVIDLAR
RSRHRLMIRLVKGAYWDSEIKRAQVEGLEGYPVYTRKVYTDVSYIACARKLLSVPEVIYP
QFATHNAHTLSAIYHIAGQNYYPGQYEFQCLHGMGEPLYEQVVGKVSDGKLNRPCRVYAP
VGTHETLLAYLVRRLLENGANTSFVNRIADQSISIQELVADPVASIEQMATLEGGFGLPH
PRIPLPRDLYGSDRANSAGIDLANEHRLASLSCALLATAHNNWKAAPMLGCASSEQAAAP
VLNPSDLRDVVGHVQEATVEDVDNAIQCAISAGPIWQATPPAERAAILERAADLMEGEIQ
PLMGLLAREAGKTFANAIAEVREAVDFLRYYAVQARNDFTNDAHRPLGPVVCISPWNFPL
AIFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRILLEAGIPEGVLQLLPGQGETVGARL
VGDDRVKGVMFTGSTEVARLLQRNVAGRLDAQGRPIPLIAETGGQNAMIVDSSALTEQVV
IDVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAECRLGNPERLSVDIGPVIDA
EAKAGIEKHIQAMRDKGRNVYQVAIADGEEIKRGTFVMPTLIELDSFDELQREIFGPVLH
VVRYKRKEIDQLIGQINASGYGLTLGVHTRIDETIAKVIDNVNAGNVYVNRNIVGAVVGV
QPFGGEGLSGTGPKAGGPLYLYRLLSTRPTDAIEQSFVRGDALAAPDVRLRDAMSQPLTA
LKTWADGNKFSDLSALCSQFAAQSQSGITRQLAGPTGERNSYAILPREHVLCLADVEGDL
LTQLAAVLAVGGSAVWPETDLTKALFPRLPKEIQAKIKRVADWTKDEVVFDAVLHHGDSD
QLRAVCQQVAQRGGAIVGVQGLSQGETAVALERLVIERALSVNTAAAGGNASLMTIG
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