SitesBLAST
Comparing PfGW456L13_223 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_223 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: 75:1316/1316 of query aligns to 5:1218/1218 of 6x9dA
- active site: N692 (= N776), K715 (= K799), E795 (= E880), C829 (= C914), E925 (= E1012), A1007 (= A1094)
- 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 (= E742), F693 (= F777), I697 (= I781), R828 (= R913), S830 (= S915), G987 (= G1074), A988 (= A1075), F995 (= F1082)
- binding nicotinamide-adenine-dinucleotide: I688 (= I772), S689 (= S773), P690 (= P774), W691 (= W775), N692 (= N776), I697 (= I781), K715 (= K799), A717 (= A801), E718 (= E802), G748 (= G832), G751 (= G836), A752 (= A837), T766 (= T851), G767 (= G852), S768 (= S853), V771 (= V856), E795 (= E880), T796 (= T881), C829 (= C914), E925 (= E1012), F927 (= F1014), F995 (= F1082)
7mybA Structure of proline utilization a with tetrahydrothiophene-2- carboxylate bound in the proline dehydrogenase active site (see paper)
60% identity, 94% coverage: 75:1316/1316 of query aligns to 5:1217/1217 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 (= I772), S688 (= S773), P689 (= P774), W690 (= W775), N691 (= N776), I696 (= I781), K714 (= K799), E717 (= E802), G747 (= G832), G750 (= G836), T765 (= T851), G766 (= G852), S767 (= S853), V770 (= V856), I774 (≠ L860), E794 (= E880), T795 (= T881), C828 (= C914), E924 (= E1012), F926 (= F1014), F994 (= F1082)
- 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)
60% identity, 94% coverage: 75:1316/1316 of query aligns to 5:1217/1217 of 7myaA
- binding nicotinamide-adenine-dinucleotide: I687 (= I772), S688 (= S773), P689 (= P774), W690 (= W775), N691 (= N776), I696 (= I781), K714 (= K799), A716 (= A801), E717 (= E802), G747 (= G832), G750 (= G836), A751 (= A837), T765 (= T851), G766 (= G852), S767 (= S853), V770 (= V856), E794 (= E880), T795 (= T881), C828 (= C914), E924 (= E1012), F926 (= F1014), F994 (= F1082)
- 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 (= G1316)
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: 75:1316/1316 of query aligns to 5:1216/1216 of 6x99A
- active site: N690 (= N776), K713 (= K799), E793 (= E880), C827 (= C914), E923 (= E1012), A1005 (= A1094)
- binding d-proline: W557 (= W642), T558 (≠ K643), E657 (= E742), F691 (= F777), R727 (= R813), R826 (= R913), S828 (= S915), G985 (= G1074), A986 (= A1075), F993 (= F1082)
- 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)
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: 75:1316/1316 of query aligns to 5:1216/1216 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 (= I772), S687 (= S773), P688 (= P774), W689 (= W775), N690 (= N776), I695 (= I781), K713 (= K799), A715 (= A801), E716 (= E802), G746 (= G832), G749 (= G836), A750 (= A837), T764 (= T851), G765 (= G852), S766 (= S853), V769 (= V856), E793 (= E880), T794 (= T881), C827 (= C914), E923 (= E1012), F925 (= F1014), F993 (= F1082)
- 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)
60% identity, 94% coverage: 75:1315/1316 of query aligns to 5:1216/1216 of 7mycA
- binding 1,4-dihydronicotinamide adenine dinucleotide: I687 (= I772), S688 (= S773), P689 (= P774), W690 (= W775), N691 (= N776), K714 (= K799), E717 (= E802), G747 (= G832), G750 (= G836), A751 (= A837), F764 (= F850), G766 (= G852), S767 (= S853), V770 (= V856), T795 (= T881), G796 (= G882), C828 (= C914), E924 (= E1012), F926 (= F1014)
- 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)
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: 75:1316/1316 of query aligns to 5:1214/1214 of 6x9aA
- active site: N688 (= N776), K711 (= K799), E791 (= E880), C825 (= C914), E921 (= E1012), A1003 (= A1094)
- 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 (= W642), T556 (≠ K643), E655 (= E742), F689 (= F777), R725 (= R813), S826 (= S915), G983 (= G1074), A984 (= A1075), F991 (= F1082)
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: 75:1316/1316 of query aligns to 5:1214/1214 of 6x9bA
- active site: N688 (= N776), K711 (= K799), E791 (= E880), C825 (= C914), E921 (= E1012), A1003 (= A1094)
- 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 (= I772), S685 (= S773), P686 (= P774), W687 (= W775), N688 (= N776), I693 (= I781), K711 (= K799), A713 (= A801), E714 (= E802), G744 (= G832), G747 (= G836), A748 (= A837), T762 (= T851), G763 (= G852), S764 (= S853), V767 (= V856), I771 (≠ L860), E791 (= E880), T792 (= T881), C825 (= C914), E921 (= E1012), F923 (= F1014)
- binding (4R)-4-hydroxy-D-proline: E655 (= E742), F689 (= F777), S826 (= S915), G983 (= G1074), A984 (= A1075), F991 (= F1082)
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: 75:1312/1316 of query aligns to 4:1209/1209 of 6x9cA
- active site: N687 (= N776), K710 (= K799), E790 (= E880), C824 (= C914), E920 (= E1012), A1002 (= A1094)
- 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 (= I772), S684 (= S773), P685 (= P774), W686 (= W775), N687 (= N776), K710 (= K799), E713 (= E802), G743 (= G832), G746 (= G836), A747 (= A837), F760 (= F850), G762 (= G852), S763 (= S853), V766 (= V856), E920 (= E1012), F922 (= F1014)
- binding proline: R823 (= R913), C824 (= C914), S825 (= S915), G982 (= G1074), A983 (= A1075), F990 (= F1082)
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: 75:1313/1316 of query aligns to 5:1206/1207 of 5kf6A
- active site: N683 (= N776), K706 (= K799), E786 (= E880), C820 (= C914), E916 (= E1012), A998 (= A1094)
- 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 (= I772), S680 (= S773), P681 (= P774), W682 (= W775), N683 (= N776), I688 (= I781), K706 (= K799), A708 (= A801), E709 (= E802), G739 (= G832), G742 (= G836), A743 (= A837), F756 (= F850), T757 (= T851), G758 (= G852), S759 (= S853), V762 (= V856), I766 (≠ L860), E786 (= E880), T787 (= T881), C820 (= C914), E916 (= E1012), F918 (= F1014), F986 (= F1082)
- 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)
59% identity, 94% coverage: 75:1313/1316 of query aligns to 5:1196/1197 of 6ufpA
- active site: N673 (= N776), K696 (= K799), E776 (= E880), C810 (= C914), E906 (= E1012), A988 (= A1094)
- 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 (= I772), P671 (= P774), W672 (= W775), N673 (= N776), I678 (= I781), K696 (= K799), E699 (= E802), G729 (= G832), G732 (= G836), F746 (= F850), T747 (= T851), G748 (= G852), S749 (= S853), V752 (= V856), E776 (= E880), T777 (= T881), C810 (= C914), E906 (= E1012), F908 (= F1014)
- binding (2S)-1,3-thiazolidine-2-carboxylic acid: K244 (= K326), D285 (= D367), Y439 (= Y537), Y451 (= Y549), R454 (= R552), R455 (= R553)
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: 85:607/1316 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)
6bsnA Structure of proline utilization a (puta) with proline bound in remote sites (see paper)
46% identity, 78% coverage: 92:1123/1316 of query aligns to 8:973/973 of 6bsnA
- active site: N643 (= N776), E743 (= E880), A777 (≠ C914), A951 (= A1094)
- 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 (= W775), F644 (= F777), G718 (= G852), R776 (= R913), S778 (= S915), F871 (= F1014), I930 (≠ V1073), G931 (= G1074), A932 (= A1075), F939 (= F1082), A958 (≠ Y1101), R959 (= R1102), A961 (= A1111)
3hazA Crystal structure of bifunctional proline utilization a (puta) protein (see paper)
46% identity, 78% coverage: 92:1123/1316 of query aligns to 8:982/983 of 3hazA
- active site: N652 (= N776), K675 (= K799), E752 (= E880), C786 (= C914), E878 (= E1012), A960 (= A1094)
- 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 (= I772), S649 (= S773), P650 (= P774), W651 (= W775), N652 (= N776), I657 (= I781), K675 (= K799), P676 (= P800), A677 (= A801), G708 (= G832), G711 (= G836), A712 (= A837), T726 (= T851), G727 (= G852), S728 (= S853), V731 (= V856), I735 (≠ L860), E752 (= E880), T753 (= T881), C786 (= C914), E878 (= E1012), F880 (= F1014), F948 (= F1082)
7mwvA Structure of the e. Coli puta proline dehydrogenase domain (residues 86-630) complexed with cyclopropanecarboxylic acid (see paper)
80% identity, 40% coverage: 85:607/1316 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)
80% identity, 40% coverage: 85:607/1316 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)
80% identity, 40% coverage: 85:607/1316 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)
78% identity, 40% coverage: 84:607/1316 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)
3e2sA Crystal structure reduced puta86-630 mutant y540s complexed with l- proline (see paper)
74% identity, 40% coverage: 85:607/1316 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)
3e2qA Crystal structure reduced puta86-630 mutant y540s complexed with trans-4-hydroxy-l-proline (see paper)
74% identity, 40% coverage: 85:607/1316 of query aligns to 1:468/468 of 3e2qA
- 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), Q369 (= Q508), C370 (= C509), L371 (= L510), E417 (= E556), S423 (= S562), F424 (= F563)
- binding 4-hydroxyproline: D143 (= D282), K187 (= K326), D228 (= D367), Y410 (= Y549), R413 (= R552), R414 (= R553)
Query Sequence
>PfGW456L13_223 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_223
MATTTLGVKLDDPTRERLKAAATSIDRTPHWLIKQAIFNYLEKLEGGATLSELNGSTKDS
DDSVDAPLDHAHQCFLEFAESILPQSVLRASITAAYRRPEPEVVPMLIEQARLPAPMAEA
TNKLAASIAEKLRNQKSAGGRAGIVQGLLQEFSLSSQEGVALMCLAEALLRIPDKGTRDA
LIRDKISTGNWQPHLGNSPSLFVNAATWGLLLTGKLVSTHNEAGLTSSLSRIIGKSGEPM
IRKGVDMAMRLMGEQFVTGETIAEALANASKFETKGFRYSYDMLGEAALTEHDAQKYLAS
YEQAIHSIGKASHGRGIYEGPGISIKLSALHPRYSRAQYERVMDELYPRLLSLTLLAKQY
DIGLNIDAEEADRLELSLDLLERLCFEPQLTGWNGIGFVIQAYQKRCPYVIDYVIDLARR
SRHRLMIRLVKGAYWDSEIKRAQVEGLEGYPVYTRKVYTDVSYIACARKLLSVPEVIYPQ
FATHNAHTLSAIYHIAGQNYYPGQYEFQCLHGMGEPLYEQVVGKVSEGKLNRPCRVYAPV
GTHETLLAYLVRRLLENGANTSFVNRIADQSISIQELVADPVASIEQMATVEGGFGLPHP
RIPLPRDLYGSERANSSGIDMANEHRLASLSCALLATAHNHWKAAPMLGCASSSEAPAPV
LNPSDLRDVVGHVQEATVEDVDNAIQCALNAAPIWQATPPAERAAILERAADLMEAEIQP
LMGLLAREAGKTFANAIAEVREAVDFLRYYAVQARNDFTNDAHRPLGPVVCISPWNFPLA
IFSGQVAAALAAGNPVLAKPAEQTPLVAAQAVRLMLEAGIPEGVLQLLPGRGETVGAGLV
GDDRVKGVMFTGSTEVARLLQRNIAGRLDSQGRPIPLIAETGGQNAMIVDSSALTEQVVI
DVVSSAFDSAGQRCSALRVLCLQEDSADRVIEMLKGAMAESRLGNPERLSVDIGPVIDAE
AKAGIEKHIQAMRDKGRSVYQVAIADAEEVKRGTFVIPTLIELESFDELQREIFGPVLHV
VRYKRKDIDQLIGQINASGYGLTLGVHTRIDETIAKVIDNVNAGNVYVNRNIVGAVVGVQ
PFGGEGLSGTGPKAGGPLYLYRLLSTRPADAIEQSFARGDAAAAPDVRLRDAMSKPLTAL
KAWADNHKFADLSTLCVQFAAQSQSGITRLLAGPTGERNSYAILPREHVLCLAEVEGDLL
TQLAAVLAVGGSAVWPEADMTKALFARLPKDIQARIKLVSDWNKDEVVFDAVLHHGHSDQ
LRAVCQQIAKRAGAIVGVQGLSQGETNIALERLVIERALSVNTAAAGGNASLMTIG
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