SitesBLAST
Comparing GFF770 FitnessBrowser__Phaeo:GFF770 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
6z1mA Structure of an ancestral glycosidase (family 1) bound to heme (see paper)
45% identity, 97% coverage: 9:439/444 of query aligns to 3:418/423 of 6z1mA
- binding protoporphyrin ix containing fe: P164 (= P169), N165 (≠ W170), L194 (≠ V199), L195 (≠ M200), L218 (≠ F222), L220 (= L224), N244 (= N248), F247 (= F251), K253 (≠ H257), Y256 (= Y260), L288 (≠ V287), R318 (= R337), Y323 (= Y342)
- binding magnesium ion: H346 (≠ E367), K409 (≠ A430)
8ivyA Beta-glucosidase bgla mutant e166q in complex with glucose (see paper)
43% identity, 96% coverage: 5:431/444 of query aligns to 2:435/451 of 8ivyA
5ossB Beta-glucosidase from thermotoga maritima in complex with gluco-1h- imidazole (see paper)
44% identity, 95% coverage: 9:431/444 of query aligns to 4:429/443 of 5ossB
- active site: R75 (= R79), H119 (= H123), E164 (= E168), V167 (≠ C171), N291 (= N293), Y293 (= Y295), E349 (= E352)
- binding (4~{S},5~{S},6~{R},7~{R})-7-(hydroxymethyl)-4,5,6,7-tetrahydro-1~{H}-benzimidazole-4,5,6-triol: Q18 (= Q23), H119 (= H123), E164 (= E168), Y293 (= Y295), E349 (= E352), W396 (= W398), E403 (= E405), W404 (= W406), F412 (= F414)
5n6tA Thermotoga maritima family 1 glycoside hydrolase complexed with a cyclophellitol analogue transition state mimic (see paper)
44% identity, 95% coverage: 9:431/444 of query aligns to 4:429/443 of 5n6tA
- active site: R75 (= R79), H119 (= H123), E164 (= E168), V167 (≠ C171), N291 (= N293), Y293 (= Y295), E349 (= E352)
- binding [(1~{R},2~{R},3~{R},4~{S},5~{R},6~{S})-3,4,5-tris(oxidanyl)-7-oxabicyclo[4.1.0]heptan-2-yl]methanediazonium: Q18 (= Q23), H119 (= H123), N163 (= N167), E164 (= E168), Y293 (= Y295), E349 (= E352), W396 (= W398), E403 (= E405), W404 (= W406), F412 (= F414)
5n6sA Thermotoga maritima family 1 glycoside hydrolase complexed with carba- cyclophellitol transition state mimic (see paper)
44% identity, 95% coverage: 9:431/444 of query aligns to 4:429/443 of 5n6sA
- active site: R75 (= R79), H119 (= H123), E164 (= E168), V167 (≠ C171), N291 (= N293), Y293 (= Y295), E349 (= E352)
- binding azanylidene-[4-[[(1~{S},2~{R},3~{R},4~{R},5~{S},6~{S},7~{S})-2-(hydroxymethyl)-3,4,5-tris(oxidanyl)-7-bicyclo[4.1.0]heptanyl]carbonylamino]butylimino]azanium: Q18 (= Q23), H119 (= H123), W120 (= W124), N163 (= N167), E164 (= E168), W166 (= W170), V167 (≠ C171), E349 (= E352), W396 (= W398), E403 (= E405), W404 (= W406), F412 (= F414)
2wc4A Structure of family 1 beta-glucosidase from thermotoga maritima in complex with 3-imino-2-thia-(+)-castanospermine (see paper)
44% identity, 95% coverage: 9:431/444 of query aligns to 4:429/443 of 2wc4A
- active site: R75 (= R79), H119 (= H123), E164 (= E168), V167 (≠ C171), N291 (= N293), Y293 (= Y295), E349 (= E352)
- binding (3Z,5S,6R,7S,8R,8aS)-3-(octylimino)hexahydro[1,3]thiazolo[3,4-a]pyridine-5,6,7,8-tetrol: Q18 (= Q23), H119 (= H123), N163 (= N167), E164 (= E168), Y293 (= Y295), W322 (= W324), E349 (= E352), W396 (= W398), E403 (= E405), W404 (= W406), F412 (= F414)
2wbgA Structure of family 1 beta-glucosidase from thermotoga maritima in complex with 3-imino-2-oxa-(+)-castanospermine (see paper)
44% identity, 95% coverage: 9:431/444 of query aligns to 4:429/443 of 2wbgA
- active site: R75 (= R79), H119 (= H123), E164 (= E168), V167 (≠ C171), N291 (= N293), Y293 (= Y295), E349 (= E352)
- binding (3Z,5S,6R,7S,8R,8aR)-3-(octylimino)hexahydro[1,3]oxazolo[3,4-a]pyridine-5,6,7,8-tetrol: Q18 (= Q23), H119 (= H123), N163 (= N167), E164 (= E168), Y293 (= Y295), H296 (≠ K298), W322 (= W324), E349 (= E352), W396 (= W398), E403 (= E405), W404 (= W406)
2jalB Beta-glucosidase from thermotoga maritima in complex with cyclophellitol (see paper)
44% identity, 95% coverage: 9:431/444 of query aligns to 5:430/444 of 2jalB
- active site: R76 (= R79), H120 (= H123), E165 (= E168), V168 (≠ C171), N292 (= N293), Y294 (= Y295), E350 (= E352)
- binding calcium ion: D277 (= D278), E281 (≠ T282)
- binding (1r,2s,3s,4s,5r,6r)-6-(hydroxymethyl)cyclohexane-1,2,3,4,5-pentol: Q19 (= Q23), H120 (= H123), E165 (= E168), E350 (= E352), W397 (= W398), E404 (= E405), W405 (= W406), F413 (= F414)
2cbvA Beta-glucosidase from thermotoga maritima in complex with calystegine b2 (see paper)
44% identity, 95% coverage: 9:431/444 of query aligns to 4:428/443 of 2cbvA
- active site: R75 (= R79), H119 (= H123), E164 (= E168), V167 (≠ C171), N290 (= N293), Y292 (= Y295), E348 (= E352)
- binding calystegine b2: Q18 (= Q23), H119 (= H123), W120 (= W124), N163 (= N167), E164 (= E168), E348 (= E352), W395 (= W398), E402 (= E405), W403 (= W406)
1oimA Family 1 b-glucosidase from thermotoga maritima (see paper)
44% identity, 95% coverage: 9:431/444 of query aligns to 4:428/443 of 1oimA
- active site: R75 (= R79), H119 (= H123), E164 (= E168), V167 (≠ C171), N290 (= N293), Y292 (= Y295), E348 (= E352)
- binding 1-deoxynojirimycin: Q18 (= Q23), H119 (= H123), N163 (= N167), E164 (= E168), Y292 (= Y295), E348 (= E352), W395 (= W398), E402 (= E405), W403 (= W406)
1w3jA Family 1 b-glucosidase from thermotoga maritima in complex with tetrahydrooxazine (see paper)
44% identity, 95% coverage: 9:431/444 of query aligns to 3:428/443 of 1w3jA
- active site: R74 (= R79), H118 (= H123), E163 (= E168), V166 (≠ C171), N290 (= N293), Y292 (= Y295), E348 (= E352)
- binding tetrahydrooxazine: Q17 (= Q23), H118 (= H123), E163 (= E168), Y292 (= Y295), E348 (= E352), W395 (= W398), E402 (= E405), W403 (= W406)
1oifA Family 1 b-glucosidase from thermotoga maritima (see paper)
44% identity, 95% coverage: 9:431/444 of query aligns to 4:429/444 of 1oifA
- active site: R75 (= R79), H119 (= H123), E164 (= E168), V167 (≠ C171), N291 (= N293), Y293 (= Y295), E349 (= E352)
- binding 5-hydroxymethyl-3,4-dihydroxypiperidine: Q18 (= Q23), E164 (= E168), Y293 (= Y295), E349 (= E352), W396 (= W398), E403 (= E405), W404 (= W406), F412 (= F414)
2wc3A Structure of family 1 beta-glucosidase from thermotoga maritima in complex with 3-imino-2-oxa-(+)-8-epi-castanospermine (see paper)
44% identity, 95% coverage: 9:431/444 of query aligns to 5:428/442 of 2wc3A
- active site: R76 (= R79), H120 (= H123), E165 (= E168), V168 (≠ C171), N292 (= N293), Y294 (= Y295), E348 (= E352)
- binding (3Z,5S,6R,7S,8S,8aR)-3-(octylimino)hexahydro[1,3]oxazolo[3,4-a]pyridine-5,6,7,8-tetrol: Q19 (= Q23), H120 (= H123), N164 (= N167), E165 (= E168), Y294 (= Y295), H297 (≠ K298), W321 (= W324), E348 (= E352), W395 (= W398), E402 (= E405), W403 (= W406), F411 (= F414)
1oinA Family 1 b-glucosidase from thermotoga maritima (see paper)
44% identity, 95% coverage: 9:431/444 of query aligns to 5:428/442 of 1oinA
- active site: R76 (= R79), H120 (= H123), E165 (= E168), V168 (≠ C171), N292 (= N293), Y294 (= Y295), E348 (= E352)
- binding 2-deoxy-2-fluoro-alpha-D-glucopyranose: Q19 (= Q23), H120 (= H123), N164 (= N167), E165 (= E168), Y294 (= Y295), E348 (= E352), W395 (= W398), E402 (= E405), W403 (= W406)
2j78A Beta-glucosidase from thermotoga maritima in complex with gluco- hydroximolactam (see paper)
44% identity, 95% coverage: 9:431/444 of query aligns to 4:428/443 of 2j78A
- active site: R75 (= R79), H119 (= H123), E164 (= E168), V167 (≠ C171), N291 (= N293), Y293 (= Y295), E348 (= E352)
- binding calcium ion: E64 (≠ D68), E67 (≠ A71), D276 (= D278), S279 (≠ A281)
- binding (2s,3s,4r,5r)-6-(hydroxyamino)-2-(hydroxymethyl)-2,3,4,5-tetrahydropyridine-3,4,5-triol: Q18 (= Q23), H119 (= H123), N163 (= N167), E164 (= E168), Y293 (= Y295), E348 (= E352), W395 (= W398), E402 (= E405), W403 (= W406), F411 (= F414)
1uz1A Family 1 b-glucosidase from thermotoga maritima in complex with isofagomine lactam (see paper)
44% identity, 95% coverage: 9:431/444 of query aligns to 4:425/439 of 1uz1A
- active site: R75 (= R79), H119 (= H123), E164 (= E168), V167 (≠ C171), N290 (= N293), Y292 (= Y295), E345 (= E352)
- binding (3s,4r,5r)-3,4-dihydroxy-5-(hydroxymethyl)piperidin-2-one: Q18 (= Q23), H119 (= H123), N163 (= N167), E164 (= E168), Y292 (= Y295), E345 (= E352), W392 (= W398), E399 (= E405), W400 (= W406), F408 (= F414)
2j7dA Beta-glucosidase from thermotoga maritima in complex with methoxycarbonyl-substituted glucoimidazole (see paper)
44% identity, 95% coverage: 9:431/444 of query aligns to 4:423/437 of 2j7dA
- active site: R75 (= R79), H119 (= H123), E164 (= E168), V167 (≠ C171), N287 (= N293), Y289 (= Y295), E343 (= E352)
- binding methoxycarbonyl-substituted glucoimidazole: Q18 (= Q23), H119 (= H123), E164 (= E168), N220 (= N223), Y289 (= Y295), W316 (= W324), E343 (= E352), W390 (= W398), E397 (= E405), W398 (= W406), F406 (= F414)
2j7cA Beta-glucosidase from thermotoga maritima in complex with phenylaminomethyl-derived glucoimidazole (see paper)
44% identity, 95% coverage: 9:431/444 of query aligns to 4:423/437 of 2j7cA
- active site: R75 (= R79), H119 (= H123), E164 (= E168), V167 (≠ C171), N287 (= N293), Y289 (= Y295), E343 (= E352)
- binding (5r,6r,7s,8s)-3-(anilinomethyl)-5,6,7,8-tetrahydro-5-(hydroxymethyl)-imidazo[1,2-a]pyridine-6,7,8-triol: Q18 (= Q23), H119 (= H123), E164 (= E168), Y289 (= Y295), W316 (= W324), E343 (= E352), W390 (= W398), E397 (= E405), W398 (= W406), F406 (= F414)
2j7bA Beta-glucosidase from thermotoga maritima in complex with gluco- tetrazole (see paper)
44% identity, 95% coverage: 9:431/444 of query aligns to 4:423/437 of 2j7bA
- active site: R75 (= R79), H119 (= H123), E164 (= E168), V167 (≠ C171), N287 (= N293), Y289 (= Y295), E343 (= E352)
- binding nojirimycine tetrazole: Q18 (= Q23), H119 (= H123), N163 (= N167), E164 (= E168), Y289 (= Y295), E343 (= E352), W390 (= W398), E397 (= E405), W398 (= W406), F406 (= F414)
2cesA Beta-glucosidase from thermotoga maritima in complex with glucoimidazole (see paper)
44% identity, 95% coverage: 9:431/444 of query aligns to 4:426/440 of 2cesA
- active site: R75 (= R79), H119 (= H123), E164 (= E168), V167 (≠ C171), N291 (= N293), Y293 (= Y295), E346 (= E352)
- binding glucoimidazole: Q18 (= Q23), H119 (= H123), N163 (= N167), E164 (= E168), Y293 (= Y295), E346 (= E352), W393 (= W398), E400 (= E405), W401 (= W406), F409 (= F414)
Query Sequence
>GFF770 FitnessBrowser__Phaeo:GFF770
MFRNSRADFPKDFLFGTATSAYQIEGHGFGGAGPTHWDSFAATPGNVVRAEHGQRACDHY
HRYAEDLDLAAAAGFDCYRFSTSWARVMPEGRGAPNPEGLDFYDRLTDAILERGLKPCVT
LYHWELPQALADLGGWRNAEIANWFGDYAEVIMGRIGDRMYSAAPINEPWCVGWLSHFLG
HHAPGLRDIRATARAMHHVMLAHGTAIQAMRALGMSNLGGVFNLEWATPVDDSEAAQQAA
ARYDAIYNGFFLGGAFHGRYPDLALEGLEPHLPKGWQDDFATITAPVDWCGLNYYTRKQI
APDAGPWPQYAEVDGPLPKTQMGWEIYPQGLYDFLTRTARDYTGDLPLIVTENGMANADV
VTKGKVEDAARITFVDDHLDAVRRAIADGVPVQGYFLWSLLDNYEWALGYEKRFGLVHVD
FETLKRTPKASYHALRSALTGASK
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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