SitesBLAST
Comparing N515DRAFT_4211 FitnessBrowser__Dyella79:N515DRAFT_4211 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)
6jfpA Crystal structure of the beta-glucosidase bgl15 (see paper)
68% identity, 98% coverage: 6:448/450 of query aligns to 2:444/444 of 6jfpA
5gnxA The e171q mutant structure of bgl6 (see paper)
60% identity, 99% coverage: 3:449/450 of query aligns to 3:450/451 of 5gnxA
5ossB Beta-glucosidase from thermotoga maritima in complex with gluco-1h- imidazole (see paper)
50% identity, 98% coverage: 6:445/450 of query aligns to 3:441/443 of 5ossB
- active site: R75 (= R78), H119 (= H122), E164 (= E167), V167 (= V170), N291 (= N292), Y293 (= Y294), 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 (= Q21), H119 (= H122), E164 (= E167), Y293 (= Y294), E349 (= E352), W396 (= W400), E403 (= E407), W404 (= W408), F412 (= F416)
5n6tA Thermotoga maritima family 1 glycoside hydrolase complexed with a cyclophellitol analogue transition state mimic (see paper)
50% identity, 98% coverage: 6:445/450 of query aligns to 3:441/443 of 5n6tA
- active site: R75 (= R78), H119 (= H122), E164 (= E167), V167 (= V170), N291 (= N292), Y293 (= Y294), 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 (= Q21), H119 (= H122), N163 (= N166), E164 (= E167), Y293 (= Y294), E349 (= E352), W396 (= W400), E403 (= E407), W404 (= W408), F412 (= F416)
5n6sA Thermotoga maritima family 1 glycoside hydrolase complexed with carba- cyclophellitol transition state mimic (see paper)
50% identity, 98% coverage: 6:445/450 of query aligns to 3:441/443 of 5n6sA
- active site: R75 (= R78), H119 (= H122), E164 (= E167), V167 (= V170), N291 (= N292), Y293 (= Y294), 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 (= Q21), H119 (= H122), W120 (= W123), N163 (= N166), E164 (= E167), W166 (= W169), V167 (= V170), E349 (= E352), W396 (= W400), E403 (= E407), W404 (= W408), F412 (= F416)
2wc4A Structure of family 1 beta-glucosidase from thermotoga maritima in complex with 3-imino-2-thia-(+)-castanospermine (see paper)
50% identity, 98% coverage: 6:445/450 of query aligns to 3:441/443 of 2wc4A
- active site: R75 (= R78), H119 (= H122), E164 (= E167), V167 (= V170), N291 (= N292), Y293 (= Y294), 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 (= Q21), H119 (= H122), N163 (= N166), E164 (= E167), Y293 (= Y294), W322 (= W325), E349 (= E352), W396 (= W400), E403 (= E407), W404 (= W408), F412 (= F416)
2wbgA Structure of family 1 beta-glucosidase from thermotoga maritima in complex with 3-imino-2-oxa-(+)-castanospermine (see paper)
50% identity, 98% coverage: 6:445/450 of query aligns to 3:441/443 of 2wbgA
- active site: R75 (= R78), H119 (= H122), E164 (= E167), V167 (= V170), N291 (= N292), Y293 (= Y294), 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 (= Q21), H119 (= H122), N163 (= N166), E164 (= E167), Y293 (= Y294), H296 (≠ A297), W322 (= W325), E349 (= E352), W396 (= W400), E403 (= E407), W404 (= W408)
2jalB Beta-glucosidase from thermotoga maritima in complex with cyclophellitol (see paper)
50% identity, 98% coverage: 6:445/450 of query aligns to 4:442/444 of 2jalB
- active site: R76 (= R78), H120 (= H122), E165 (= E167), V168 (= V170), N292 (= N292), Y294 (= Y294), E350 (= E352)
- binding calcium ion: D277 (= D277), E281 (≠ L281)
- binding (1r,2s,3s,4s,5r,6r)-6-(hydroxymethyl)cyclohexane-1,2,3,4,5-pentol: Q19 (= Q21), H120 (= H122), E165 (= E167), E350 (= E352), W397 (= W400), E404 (= E407), W405 (= W408), F413 (= F416)
1oifA Family 1 b-glucosidase from thermotoga maritima (see paper)
50% identity, 98% coverage: 6:445/450 of query aligns to 3:441/444 of 1oifA
- active site: R75 (= R78), H119 (= H122), E164 (= E167), V167 (= V170), N291 (= N292), Y293 (= Y294), E349 (= E352)
- binding 5-hydroxymethyl-3,4-dihydroxypiperidine: Q18 (= Q21), E164 (= E167), Y293 (= Y294), E349 (= E352), W396 (= W400), E403 (= E407), W404 (= W408), F412 (= F416)
1w3jA Family 1 b-glucosidase from thermotoga maritima in complex with tetrahydrooxazine (see paper)
50% identity, 98% coverage: 6:445/450 of query aligns to 2:440/443 of 1w3jA
- active site: R74 (= R78), H118 (= H122), E163 (= E167), V166 (= V170), N290 (= N292), Y292 (= Y294), E348 (= E352)
- binding tetrahydrooxazine: Q17 (= Q21), H118 (= H122), E163 (= E167), Y292 (= Y294), E348 (= E352), W395 (= W400), E402 (= E407), W403 (= W408)
1oinA Family 1 b-glucosidase from thermotoga maritima (see paper)
50% identity, 98% coverage: 6:445/450 of query aligns to 4:440/442 of 1oinA
- active site: R76 (= R78), H120 (= H122), E165 (= E167), V168 (= V170), N292 (= N292), Y294 (= Y294), E348 (= E352)
- binding 2-deoxy-2-fluoro-alpha-D-glucopyranose: Q19 (= Q21), H120 (= H122), N164 (= N166), E165 (= E167), Y294 (= Y294), E348 (= E352), W395 (= W400), E402 (= E407), W403 (= W408)
4ptwA Halothermothrix orenii beta-glucosidase a, 2-deoxy-2-fluoro-glucose complex (see paper)
49% identity, 97% coverage: 7:443/450 of query aligns to 3:442/445 of 4ptwA
- active site: R74 (= R78), H118 (= H122), E163 (= E167), V166 (= V170), N291 (= N292), Y293 (= Y294), E351 (= E352)
- binding 2-deoxy-2-fluoro-alpha-D-glucopyranose: Q17 (= Q21), H118 (= H122), E163 (= E167), Y293 (= Y294), E351 (= E352), W398 (= W400), E405 (= E407), W406 (= W408)
4ptvA Halothermothrix orenii beta-glucosidase a, thiocellobiose complex (see paper)
49% identity, 97% coverage: 7:443/450 of query aligns to 3:442/445 of 4ptvA
- active site: R74 (= R78), H118 (= H122), E163 (= E167), V166 (= V170), N291 (= N292), Y293 (= Y294), E351 (= E352)
- binding beta-D-glucopyranose: W324 (= W325), E405 (= E407), Y408 (≠ L410)
- binding 4-thio-beta-D-glucopyranose: Q17 (= Q21), H118 (= H122), E163 (= E167), Y293 (= Y294), E351 (= E352), W398 (= W400), E405 (= E407), W406 (= W408)
2wc3A Structure of family 1 beta-glucosidase from thermotoga maritima in complex with 3-imino-2-oxa-(+)-8-epi-castanospermine (see paper)
50% identity, 98% coverage: 6:445/450 of query aligns to 4:440/442 of 2wc3A
- active site: R76 (= R78), H120 (= H122), E165 (= E167), V168 (= V170), N292 (= N292), Y294 (= Y294), 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 (= Q21), H120 (= H122), N164 (= N166), E165 (= E167), Y294 (= Y294), H297 (≠ A297), W321 (= W325), E348 (= E352), W395 (= W400), E402 (= E407), W403 (= W408), F411 (= F416)
2j78A Beta-glucosidase from thermotoga maritima in complex with gluco- hydroximolactam (see paper)
50% identity, 98% coverage: 6:445/450 of query aligns to 3:440/443 of 2j78A
- active site: R75 (= R78), H119 (= H122), E164 (= E167), V167 (= V170), N291 (= N292), Y293 (= Y294), E348 (= E352)
- binding calcium ion: E64 (≠ Q67), E67 (≠ K70), D276 (= D277), S279 (≠ K280)
- binding (2s,3s,4r,5r)-6-(hydroxyamino)-2-(hydroxymethyl)-2,3,4,5-tetrahydropyridine-3,4,5-triol: Q18 (= Q21), H119 (= H122), N163 (= N166), E164 (= E167), Y293 (= Y294), E348 (= E352), W395 (= W400), E402 (= E407), W403 (= W408), F411 (= F416)
2cesA Beta-glucosidase from thermotoga maritima in complex with glucoimidazole (see paper)
50% identity, 98% coverage: 6:445/450 of query aligns to 3:438/440 of 2cesA
- active site: R75 (= R78), H119 (= H122), E164 (= E167), V167 (= V170), N291 (= N292), Y293 (= Y294), E346 (= E352)
- binding glucoimidazole: Q18 (= Q21), H119 (= H122), N163 (= N166), E164 (= E167), Y293 (= Y294), E346 (= E352), W393 (= W400), E400 (= E407), W401 (= W408), F409 (= F416)
2cbvA Beta-glucosidase from thermotoga maritima in complex with calystegine b2 (see paper)
50% identity, 98% coverage: 6:445/450 of query aligns to 3:440/443 of 2cbvA
- active site: R75 (= R78), H119 (= H122), E164 (= E167), V167 (= V170), N290 (= N292), Y292 (= Y294), E348 (= E352)
- binding calystegine b2: Q18 (= Q21), H119 (= H122), W120 (= W123), N163 (= N166), E164 (= E167), E348 (= E352), W395 (= W400), E402 (= E407), W403 (= W408)
1oimA Family 1 b-glucosidase from thermotoga maritima (see paper)
50% identity, 98% coverage: 6:445/450 of query aligns to 3:440/443 of 1oimA
- active site: R75 (= R78), H119 (= H122), E164 (= E167), V167 (= V170), N290 (= N292), Y292 (= Y294), E348 (= E352)
- binding 1-deoxynojirimycin: Q18 (= Q21), H119 (= H122), N163 (= N166), E164 (= E167), Y292 (= Y294), E348 (= E352), W395 (= W400), E402 (= E407), W403 (= W408)
2cbuA Beta-glucosidase from thermotoga maritima in complex with castanospermine (see paper)
50% identity, 98% coverage: 6:445/450 of query aligns to 3:437/440 of 2cbuA
- active site: R75 (= R78), H119 (= H122), E164 (= E167), V167 (= V170), N289 (= N292), Y291 (= Y294), E345 (= E352)
- binding castanospermine: Q18 (= Q21), H119 (= H122), N163 (= N166), E164 (= E167), Y291 (= Y294), W318 (= W325), E345 (= E352), W392 (= W400), E399 (= E407), W400 (= W408), F408 (= F416)
1uz1A Family 1 b-glucosidase from thermotoga maritima in complex with isofagomine lactam (see paper)
50% identity, 98% coverage: 6:445/450 of query aligns to 3:437/439 of 1uz1A
- active site: R75 (= R78), H119 (= H122), E164 (= E167), V167 (= V170), N290 (= N292), Y292 (= Y294), E345 (= E352)
- binding (3s,4r,5r)-3,4-dihydroxy-5-(hydroxymethyl)piperidin-2-one: Q18 (= Q21), H119 (= H122), N163 (= N166), E164 (= E167), Y292 (= Y294), E345 (= E352), W392 (= W400), E399 (= E407), W400 (= W408), F408 (= F416)
Query Sequence
>N515DRAFT_4211 FitnessBrowser__Dyella79:N515DRAFT_4211
MTRSYRFPEGFLWGAATSAYQIEGSPLADGAGPSIWERFAHTPGMMVGGDTGDIACDHYR
RYKDDVQLMKALGLHGYRFSIAWARVLPEGTGRVNEKGLDFYKRLVDELLENGIAPNATL
FHWDMPAALDDRGGWLNRDSAHWFAEYAEVMFKALDGRVQRWATLNEPWVVTDGGYLHGA
LAPGHRSKYEAPIAAHNLMRASGAGIQAYRAHGKHEIGVVFNIEPKYPHSQSADDLAATR
RAHAYMNEQFADPALLGSYPPELKEIFGEAWPDFPADDFKLTRQKVDFVGINYYTRAVVK
HDPNQYPLKASPVRQANKTYTETGWEVFEQGLTDTLTWFKDRYGDIPLYITENGSAFYDP
PVAEGEVLDDPLRTGYLRKHLRALHKAIEAGVNLKGYYAWSLLDNLEWSLGFSKRFGLYH
VDFATQKRTPKATAKLYARVIESNGAVLDD
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