SitesBLAST
Comparing CCNA_02220 FitnessBrowser__Caulo:CCNA_02220 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)
5ns8A Crystal structure of beta-glucosidase bglm-g1 mutant h75r from marine metagenome in complex with inhibitor 1-deoxynojirimycin (see paper)
43% identity, 87% coverage: 45:465/482 of query aligns to 9:429/440 of 5ns8A
1gnxA B-glucosidase from streptomyces sp
45% identity, 91% coverage: 41:479/482 of query aligns to 4:447/447 of 1gnxA
- active site: R75 (= R112), H119 (= H156), E164 (= E201), C167 (≠ V204), N293 (= N326), Y295 (= Y328), E353 (= E386)
- binding beta-D-fructofuranose: Q285 (= Q318), K286 (≠ P319)
- binding alpha-D-glucopyranose: Q204 (= Q241), R281 (≠ K314), Q285 (= Q318)
- binding sulfate ion: R190 (≠ P227), F274 (vs. gap), R276 (= R309)
6z1mA Structure of an ancestral glycosidase (family 1) bound to heme (see paper)
41% identity, 91% coverage: 40:478/482 of query aligns to 2:423/423 of 6z1mA
- binding protoporphyrin ix containing fe: P164 (≠ A202), N165 (≠ A203), L194 (≠ M232), L195 (≠ N233), L218 (≠ M256), L220 (= L258), N244 (= N284), F247 (≠ W287), K253 (= K293), Y256 (= Y296), L288 (≠ V320), R318 (= R372), Y323 (= Y377)
- binding magnesium ion: H346 (≠ D401), K409 (≠ A464)
2cbvA Beta-glucosidase from thermotoga maritima in complex with calystegine b2 (see paper)
39% identity, 91% coverage: 39:478/482 of query aligns to 2:441/443 of 2cbvA
- active site: R75 (= R112), H119 (= H156), E164 (= E201), V167 (= V204), N290 (= N326), Y292 (= Y328), E348 (= E386)
- binding calystegine b2: Q18 (= Q55), H119 (= H156), W120 (= W157), N163 (= N200), E164 (= E201), E348 (= E386), W395 (= W432), E402 (= E439), W403 (= W440)
1oimA Family 1 b-glucosidase from thermotoga maritima (see paper)
39% identity, 91% coverage: 39:478/482 of query aligns to 2:441/443 of 1oimA
- active site: R75 (= R112), H119 (= H156), E164 (= E201), V167 (= V204), N290 (= N326), Y292 (= Y328), E348 (= E386)
- binding 1-deoxynojirimycin: Q18 (= Q55), H119 (= H156), N163 (= N200), E164 (= E201), Y292 (= Y328), E348 (= E386), W395 (= W432), E402 (= E439), W403 (= W440)
2jalB Beta-glucosidase from thermotoga maritima in complex with cyclophellitol (see paper)
38% identity, 91% coverage: 39:478/482 of query aligns to 3:443/444 of 2jalB
- active site: R76 (= R112), H120 (= H156), E165 (= E201), V168 (= V204), N292 (= N326), Y294 (= Y328), E350 (= E386)
- binding calcium ion: D277 (vs. gap), E281 (≠ T315)
- binding (1r,2s,3s,4s,5r,6r)-6-(hydroxymethyl)cyclohexane-1,2,3,4,5-pentol: Q19 (= Q55), H120 (= H156), E165 (= E201), E350 (= E386), W397 (= W432), E404 (= E439), W405 (= W440), F413 (= F448)
5ossB Beta-glucosidase from thermotoga maritima in complex with gluco-1h- imidazole (see paper)
38% identity, 91% coverage: 39:478/482 of query aligns to 2:442/443 of 5ossB
- active site: R75 (= R112), H119 (= H156), E164 (= E201), V167 (= V204), N291 (= N326), Y293 (= Y328), E349 (= E386)
- binding (4~{S},5~{S},6~{R},7~{R})-7-(hydroxymethyl)-4,5,6,7-tetrahydro-1~{H}-benzimidazole-4,5,6-triol: Q18 (= Q55), H119 (= H156), E164 (= E201), Y293 (= Y328), E349 (= E386), W396 (= W432), E403 (= E439), W404 (= W440), F412 (= F448)
5n6tA Thermotoga maritima family 1 glycoside hydrolase complexed with a cyclophellitol analogue transition state mimic (see paper)
38% identity, 91% coverage: 39:478/482 of query aligns to 2:442/443 of 5n6tA
- active site: R75 (= R112), H119 (= H156), E164 (= E201), V167 (= V204), N291 (= N326), Y293 (= Y328), E349 (= E386)
- 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 (= Q55), H119 (= H156), N163 (= N200), E164 (= E201), Y293 (= Y328), E349 (= E386), W396 (= W432), E403 (= E439), W404 (= W440), F412 (= F448)
5n6sA Thermotoga maritima family 1 glycoside hydrolase complexed with carba- cyclophellitol transition state mimic (see paper)
38% identity, 91% coverage: 39:478/482 of query aligns to 2:442/443 of 5n6sA
- active site: R75 (= R112), H119 (= H156), E164 (= E201), V167 (= V204), N291 (= N326), Y293 (= Y328), E349 (= E386)
- 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 (= Q55), H119 (= H156), W120 (= W157), N163 (= N200), E164 (= E201), W166 (≠ A203), V167 (= V204), E349 (= E386), W396 (= W432), E403 (= E439), W404 (= W440), F412 (= F448)
2wc4A Structure of family 1 beta-glucosidase from thermotoga maritima in complex with 3-imino-2-thia-(+)-castanospermine (see paper)
38% identity, 91% coverage: 39:478/482 of query aligns to 2:442/443 of 2wc4A
- active site: R75 (= R112), H119 (= H156), E164 (= E201), V167 (= V204), N291 (= N326), Y293 (= Y328), E349 (= E386)
- binding (3Z,5S,6R,7S,8R,8aS)-3-(octylimino)hexahydro[1,3]thiazolo[3,4-a]pyridine-5,6,7,8-tetrol: Q18 (= Q55), H119 (= H156), N163 (= N200), E164 (= E201), Y293 (= Y328), W322 (≠ R359), E349 (= E386), W396 (= W432), E403 (= E439), W404 (= W440), F412 (= F448)
2wbgA Structure of family 1 beta-glucosidase from thermotoga maritima in complex with 3-imino-2-oxa-(+)-castanospermine (see paper)
38% identity, 91% coverage: 39:478/482 of query aligns to 2:442/443 of 2wbgA
- active site: R75 (= R112), H119 (= H156), E164 (= E201), V167 (= V204), N291 (= N326), Y293 (= Y328), E349 (= E386)
- binding (3Z,5S,6R,7S,8R,8aR)-3-(octylimino)hexahydro[1,3]oxazolo[3,4-a]pyridine-5,6,7,8-tetrol: Q18 (= Q55), H119 (= H156), N163 (= N200), E164 (= E201), Y293 (= Y328), H296 (≠ A331), W322 (≠ R359), E349 (= E386), W396 (= W432), E403 (= E439), W404 (= W440)
1oifA Family 1 b-glucosidase from thermotoga maritima (see paper)
38% identity, 91% coverage: 39:478/482 of query aligns to 2:442/444 of 1oifA
- active site: R75 (= R112), H119 (= H156), E164 (= E201), V167 (= V204), N291 (= N326), Y293 (= Y328), E349 (= E386)
- binding 5-hydroxymethyl-3,4-dihydroxypiperidine: Q18 (= Q55), E164 (= E201), Y293 (= Y328), E349 (= E386), W396 (= W432), E403 (= E439), W404 (= W440), F412 (= F448)
1w3jA Family 1 b-glucosidase from thermotoga maritima in complex with tetrahydrooxazine (see paper)
38% identity, 91% coverage: 39:478/482 of query aligns to 1:441/443 of 1w3jA
- active site: R74 (= R112), H118 (= H156), E163 (= E201), V166 (= V204), N290 (= N326), Y292 (= Y328), E348 (= E386)
- binding tetrahydrooxazine: Q17 (= Q55), H118 (= H156), E163 (= E201), Y292 (= Y328), E348 (= E386), W395 (= W432), E402 (= E439), W403 (= W440)
2j75A Beta-glucosidase from thermotoga maritima in complex with noeuromycin (see paper)
38% identity, 91% coverage: 39:478/482 of query aligns to 2:437/438 of 2j75A
- active site: R75 (= R112), H119 (= H156), E164 (= E201), V167 (= V204), N288 (= N326), Y290 (= Y328), E344 (= E386)
- binding (2r,3s,4r,5r)-5-(hydroxymethyl)piperidine-2,3,4-triol: Q18 (= Q55), H119 (= H156), N163 (= N200), E164 (= E201), Y290 (= Y328), E344 (= E386), W391 (= W432), E398 (= E439), W399 (= W440), F407 (= F448)
2vrjA Beta-glucosidase from thermotoga maritima in complex with n-octyl-5- deoxy-6-oxa-n-(thio)carbamoylcalystegine (see paper)
38% identity, 91% coverage: 39:478/482 of query aligns to 2:437/438 of 2vrjA
- active site: R75 (= R112), H119 (= H156), E164 (= E201), V167 (= V204), N288 (= N326), Y290 (= Y328), E344 (= E386)
- binding calcium ion: H38 (≠ R75), D50 (≠ A87)
- binding (1S,2R,3S,4R,5R)-2,3,4-trihydroxy-N-octyl-6-oxa-8-azabicyclo[3.2.1]octane-8-carbothioamide: Q18 (= Q55), H119 (= H156), E164 (= E201), H178 (= H215), Y290 (= Y328), E344 (= E386), W391 (= W432), E398 (= E439), W399 (= W440), A400 (≠ D441), E401 (≠ L442)
2j7dA Beta-glucosidase from thermotoga maritima in complex with methoxycarbonyl-substituted glucoimidazole (see paper)
39% identity, 91% coverage: 39:478/482 of query aligns to 2:436/437 of 2j7dA
- active site: R75 (= R112), H119 (= H156), E164 (= E201), V167 (= V204), N287 (= N326), Y289 (= Y328), E343 (= E386)
- binding methoxycarbonyl-substituted glucoimidazole: Q18 (= Q55), H119 (= H156), E164 (= E201), N220 (≠ A257), Y289 (= Y328), W316 (≠ R359), E343 (= E386), W390 (= W432), E397 (= E439), W398 (= W440), F406 (= F448)
2j7cA Beta-glucosidase from thermotoga maritima in complex with phenylaminomethyl-derived glucoimidazole (see paper)
39% identity, 91% coverage: 39:478/482 of query aligns to 2:436/437 of 2j7cA
- active site: R75 (= R112), H119 (= H156), E164 (= E201), V167 (= V204), N287 (= N326), Y289 (= Y328), E343 (= E386)
- binding (5r,6r,7s,8s)-3-(anilinomethyl)-5,6,7,8-tetrahydro-5-(hydroxymethyl)-imidazo[1,2-a]pyridine-6,7,8-triol: Q18 (= Q55), H119 (= H156), E164 (= E201), Y289 (= Y328), W316 (≠ R359), E343 (= E386), W390 (= W432), E397 (= E439), W398 (= W440), F406 (= F448)
2j7bA Beta-glucosidase from thermotoga maritima in complex with gluco- tetrazole (see paper)
39% identity, 91% coverage: 39:478/482 of query aligns to 2:436/437 of 2j7bA
- active site: R75 (= R112), H119 (= H156), E164 (= E201), V167 (= V204), N287 (= N326), Y289 (= Y328), E343 (= E386)
- binding nojirimycine tetrazole: Q18 (= Q55), H119 (= H156), N163 (= N200), E164 (= E201), Y289 (= Y328), E343 (= E386), W390 (= W432), E397 (= E439), W398 (= W440), F406 (= F448)
2j7gA Beta-glucosidase from thermotoga maritima in complex with methyl acetic acid-substituted glucoimidazole (see paper)
38% identity, 91% coverage: 39:478/482 of query aligns to 2:436/437 of 2j7gA
- active site: R75 (= R112), H119 (= H156), E164 (= E201), V167 (= V204), N288 (= N326), Y290 (= Y328), E343 (= E386)
- binding methyl acetic acid-substituted glucoimidazole: Q18 (= Q55), H119 (= H156), E164 (= E201), Y290 (= Y328), E343 (= E386), W390 (= W432), E397 (= E439), W398 (= W440), F406 (= F448)
2j7fA Beta-glucosidase from thermotoga maritima in complex with carboxylate- substituted glucoimidazole (see paper)
39% identity, 91% coverage: 39:478/482 of query aligns to 2:434/435 of 2j7fA
- active site: R75 (= R112), H119 (= H156), E164 (= E201), V167 (= V204), N286 (= N326), Y288 (= Y328), E341 (= E386)
- binding carboxylate-substituted glucoimidazole: Q18 (= Q55), H119 (= H156), E164 (= E201), Y288 (= Y328), W314 (≠ R359), E341 (= E386), W388 (= W432), E395 (= E439), W396 (= W440), F404 (= F448)
Query Sequence
>CCNA_02220 FitnessBrowser__Caulo:CCNA_02220
MDRSGVSRRALGTLALGGAALGLSACEGPGETDLTPKGRQFPKDFVWGVATAAFQTEGSQ
TADGRGPSIWDVFERVPGHVKNGDTAADATDSYRRYQDDVDLIAGASLSAYRFSMSWSRI
LPTGAGAVNAAGLDHYSRLVDALLAKGITPYATLFHWDLPQGLQDKGGWANRDTAQRLAD
YARAVVERLGDRLKNYIILNEAAVHTVFGHVLGDHAPGLKDAALLGPVTHHMNLGQGLAI
QALRAARSDLSVGTTMALQPCRPAGGPLAFWNRLASDGLDEIWNLAWLDPLFKGTYPKAM
EEPLKGVVRDGDLKTTRQPVDFLGVNYYAPAYVRLDLSAPSKIAAAAAPNSAEQDAFGRH
IDPSGLFEVLDRVRREYGAPKMLVTENGCSDPFSSGPAILDDTFRIKYLRRHLEAVLAAR
EAGCDVRGYFEWTLIDNFEWDLGYTSKFGITTMEAASGRRIPKASYGWFKALAQTGTLPS
SP
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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