SitesBLAST
Comparing Echvi_3562 FitnessBrowser__Cola:Echvi_3562 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)
3krbA Structure of aldose reductase from giardia lamblia at 1.75a resolution (see paper)
47% identity, 90% coverage: 13:298/319 of query aligns to 6:296/307 of 3krbA
- active site: D36 (= D43), Y41 (= Y48), K72 (= K77), H105 (= H110)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G11 (= G18), T12 (= T19), W13 (= W20), D36 (= D43), Y41 (= Y48), H105 (= H110), Q178 (= Q180), Y204 (= Y206), S205 (≠ A207), P206 (= P208), M207 (≠ L209), G209 (≠ A211), N216 (≠ Q218), H236 (≠ A244), I255 (= I259), P256 (= P260), K257 (= K261), S258 (= S262), Q259 (≠ V263), T260 (= T264), R263 (= R267), N267 (= N271)
P14550 Aldo-keto reductase family 1 member A1; Alcohol dehydrogenase [NADP(+)]; Aldehyde reductase; Glucuronate reductase; Glucuronolactone reductase; EC 1.1.1.2; EC 1.1.1.372; EC 1.1.1.54; EC 1.1.1.19; EC 1.1.1.20 from Homo sapiens (Human) (see 3 papers)
45% identity, 93% coverage: 3:300/319 of query aligns to 5:308/325 of P14550
- Y50 (= Y48) active site, Proton donor; mutation to F: Complete loss of enzymatic activity.; mutation to H: Complete loss of enzymatic activity.
- N52 (= N50) to S: reduced activity towards daunorubicin; dbSNP:rs2229540
- E55 (= E53) to D: reduced activity towards daunorubicin; dbSNP:rs6690497
- K80 (= K77) Lowers pKa of active site Tyr; mutation to M: Complete loss of enzymatic activity.
- H113 (= H110) binding ; mutation to Q: Strong decrease in enzymatic activity.
- I299 (vs. gap) mutation to A: No change in enzymatic activity.; mutation to C: No change in enzymatic activity.
- V300 (vs. gap) mutation to C: No change in enzymatic activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
3fx4A Porcine aldehyde reductase in ternary complex with inhibitor (see paper)
45% identity, 93% coverage: 3:300/319 of query aligns to 5:308/325 of 3fx4A
- active site: D45 (= D43), Y50 (= Y48), K80 (= K77), H113 (= H110)
- binding [(5Z)-5-{[3-(carboxymethoxy)-4-methoxyphenyl]methylidene}-2,4-dioxo-1,3-thiazolidin-3-yl]acetic acid: W22 (= W20), Y50 (= Y48), H113 (= H110), R218 (= R214), A219 (≠ T215), F298 (= F296), I299 (vs. gap), V300 (vs. gap)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G18), T21 (= T19), W22 (= W20), D45 (= D43), Y50 (= Y48), H113 (= H110), Q184 (= Q180), Y210 (= Y206), S211 (≠ A207), P212 (= P208), L213 (= L209), S215 (≠ A211), A246 (= A244), I261 (= I259), P262 (= P260), K263 (= K261), S264 (= S262), V265 (= V263), T266 (= T264), R269 (= R267), Q272 (≠ E270), N273 (= N271)
P50578 Aldo-keto reductase family 1 member A1; Alcohol dehydrogenase [NADP(+)]; Aldehyde reductase; Glucuronate reductase; Glucuronolactone reductase; EC 1.1.1.2; EC 1.1.1.372; EC 1.1.1.54; EC 1.1.1.19; EC 1.1.1.20 from Sus scrofa (Pig) (see paper)
45% identity, 93% coverage: 3:300/319 of query aligns to 5:308/325 of P50578
- Y50 (= Y48) active site, Proton donor
- H113 (= H110) binding
- 211:273 (vs. 207:271, 45% identical) binding
3h4gA Structure of aldehyde reductase holoenzyme in complex with potent aldose reductase inhibitor fidarestat: implications for inhibitor binding and selectivity (see paper)
45% identity, 92% coverage: 3:296/319 of query aligns to 5:298/320 of 3h4gA
- active site: D45 (= D43), Y50 (= Y48), K80 (= K77), H113 (= H110)
- binding (2s,4s)-2-aminoformyl-6-fluoro-spiro[chroman-4,4'-imidazolidine]-2',5'-dione: W22 (= W20), Y50 (= Y48), H113 (= H110), W114 (= W111), W220 (≠ Q216)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G18), T21 (= T19), W22 (= W20), D45 (= D43), Y50 (= Y48), H113 (= H110), S162 (= S158), N163 (= N159), Q184 (= Q180), Y210 (= Y206), S211 (≠ A207), P212 (= P208), L213 (= L209), S215 (≠ A211), D217 (≠ Y213), A246 (= A244), I261 (= I259), P262 (= P260), K263 (= K261), S264 (= S262), V265 (= V263), T266 (= T264), R269 (= R267), Q272 (≠ E270), N273 (= N271)
Sites not aligning to the query:
3cv7A Crystal structure of porcine aldehyde reductase ternary complex (see paper)
45% identity, 92% coverage: 3:296/319 of query aligns to 5:298/322 of 3cv7A
- active site: D45 (= D43), Y50 (= Y48), K80 (= K77), H113 (= H110)
- binding 3,5-dichloro-2-hydroxybenzoic acid: W22 (= W20), Y50 (= Y48), W82 (= W79), H113 (= H110)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G18), T21 (= T19), W22 (= W20), Y50 (= Y48), H113 (= H110), Q184 (= Q180), Y210 (= Y206), S211 (≠ A207), P212 (= P208), L213 (= L209), S215 (≠ A211), A246 (= A244), I261 (= I259), P262 (= P260), K263 (= K261), S264 (= S262), V265 (= V263), T266 (= T264), R269 (= R267), Q272 (≠ E270), N273 (= N271)
Sites not aligning to the query:
P51635 Aldo-keto reductase family 1 member A1; 3-DG-reducing enzyme; Alcohol dehydrogenase [NADP(+)]; Aldehyde reductase; Glucuronate reductase; Glucuronolactone reductase; EC 1.1.1.2; EC 1.1.1.372; EC 1.1.1.54; EC 1.1.1.19; EC 1.1.1.20 from Rattus norvegicus (Rat) (see paper)
44% identity, 93% coverage: 3:300/319 of query aligns to 5:308/325 of P51635
- K13 (≠ T11) Not glycated
- K23 (≠ Q21) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K30 (≠ Y28) Not glycated
- K34 (≠ L32) Not glycated
- K61 (≠ A59) Not glycated
- K68 (vs. gap) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K80 (= K77) Not glycated
- K85 (≠ S82) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K97 (≠ S94) Not glycated
- K127 (≠ E123) Not glycated
- K134 (≠ H130) Not glycated
- K141 (≠ S137) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K145 (≠ A141) Not glycated
- K153 (≠ T149) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K157 (= K153) Not glycated
- K240 (= K238) Not glycated
- K257 (≠ D255) Not glycated
- K263 (= K261) Not glycated
- K287 (≠ D285) Not glycated
- K294 (≠ G292) Not glycated
- K308 (= K300) Not glycated
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylthreonine
2ipwA Crystal structure of c298a w219y aldose reductase complexed with dichlorophenylacetic acid (see paper)
46% identity, 95% coverage: 4:305/319 of query aligns to 3:300/309 of 2ipwA
- active site: D42 (= D43), Y47 (= Y48), K76 (= K77), H109 (= H110)
- binding (2,6-dichlorophenyl)acetic acid: W19 (= W20), Y47 (= Y48), H109 (= H110)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G17 (= G18), T18 (= T19), W19 (= W20), K20 (≠ Q21), D42 (= D43), Y47 (= Y48), H109 (= H110), Q179 (= Q180), Y205 (= Y206), S206 (≠ A207), P207 (= P208), L208 (= L209), S210 (≠ A211), P211 (≠ A212), D212 (≠ Y213), A239 (= A244), I254 (= I259), P255 (= P260), K256 (= K261), S257 (= S262), V258 (= V263), T259 (= T264), R262 (= R267), E265 (= E270), N266 (= N271)
1az1A Alrestatin bound to c298a/w219y mutant human aldose reductase (see paper)
46% identity, 95% coverage: 4:305/319 of query aligns to 3:305/314 of 1az1A
- active site: D42 (= D43), Y47 (= Y48), K76 (= K77), H109 (= H110)
- binding alrestatin: W19 (= W20), Y47 (= Y48), H109 (= H110), W110 (= W111), F121 (vs. gap), A297 (≠ T297), A297 (≠ T297), A298 (≠ D298), L299 (≠ G299), L300 (≠ K300)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G17 (= G18), T18 (= T19), W19 (= W20), K20 (≠ Q21), D42 (= D43), Y47 (= Y48), W110 (= W111), Q182 (= Q180), Y208 (= Y206), S209 (≠ A207), P210 (= P208), L211 (= L209), S213 (≠ A211), P214 (≠ A212), D215 (≠ Y213), A244 (= A244), I259 (= I259), P260 (= P260), K261 (= K261), S262 (= S262), V263 (= V263), T264 (= T264), R267 (= R267), E270 (= E270), N271 (= N271)
8fh9A Crystal structure of aldose reductase (akr1b1) complexed with NADP+ and at-007
46% identity, 95% coverage: 4:305/319 of query aligns to 4:306/315 of 8fh9A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G18), T19 (= T19), W20 (= W20), K21 (≠ Q21), D43 (= D43), Y48 (= Y48), H110 (= H110), W111 (= W111), N160 (= N159), Q183 (= Q180), Y209 (= Y206), S210 (≠ A207), P211 (= P208), L212 (= L209), S214 (≠ A211), P215 (≠ A212), D216 (≠ Y213), L228 (= L227), A245 (= A244), I260 (= I259), P261 (= P260), K262 (= K261), S263 (= S262), T265 (= T264), R268 (= R267), E271 (= E270), N272 (= N271), C298 (≠ T297)
- binding (4-oxo-3-{[5-(trifluoromethyl)-1,3-benzothiazol-2-yl]methyl}-3,4-dihydrothieno[3,4-d]pyridazin-1-yl)acetic acid: W20 (= W20), Y48 (= Y48), H110 (= H110), W111 (= W111), T113 (≠ L113), F115 (≠ L115), F122 (vs. gap), W219 (≠ Q216), A299 (≠ D298), L300 (≠ G299), C303 (≠ W302)
Sites not aligning to the query:
8fh7A Crystal structure of aldose reductase (akr1b1) complexed with NADP+ and at-003
46% identity, 95% coverage: 4:305/319 of query aligns to 4:306/315 of 8fh7A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G18), T19 (= T19), W20 (= W20), K21 (≠ Q21), D43 (= D43), Y48 (= Y48), H110 (= H110), N160 (= N159), Q183 (= Q180), Y209 (= Y206), S210 (≠ A207), P211 (= P208), L212 (= L209), S214 (≠ A211), P215 (≠ A212), D216 (≠ Y213), A245 (= A244), I260 (= I259), K262 (= K261), S263 (= S262), T265 (= T264), R268 (= R267), E271 (= E270), N272 (= N271), C298 (≠ T297)
- binding {7-[(5-chloro-1,3-benzothiazol-2-yl)methyl]-8-oxo-7,8-dihydropyrazino[2,3-d]pyridazin-5-yl}acetic acid: W20 (= W20), Y48 (= Y48), H110 (= H110), W111 (= W111), T113 (≠ L113), F115 (≠ L115), F122 (vs. gap), W219 (≠ Q216), A299 (≠ D298), L300 (≠ G299), C303 (≠ W302)
8fh5A Crystal structure of aldose reductase (akr1b1) complexed with NADP+ and at-001
46% identity, 95% coverage: 4:305/319 of query aligns to 4:306/315 of 8fh5A
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G18), T19 (= T19), W20 (= W20), K21 (≠ Q21), D43 (= D43), Y48 (= Y48), H110 (= H110), W111 (= W111), N160 (= N159), Q183 (= Q180), Y209 (= Y206), S210 (≠ A207), P211 (= P208), L212 (= L209), S214 (≠ A211), P215 (≠ A212), D216 (≠ Y213), A245 (= A244), I260 (= I259), K262 (= K261), S263 (= S262), T265 (= T264), R268 (= R267), E271 (= E270), N272 (= N271)
- binding (8-oxo-7-{[5-(trifluoromethyl)-1,3-benzothiazol-2-yl]methyl}-7,8-dihydropyrazino[2,3-d]pyridazin-5-yl)acetic acid: W20 (= W20), Y48 (= Y48), H110 (= H110), W111 (= W111), T113 (≠ L113), F115 (≠ L115), F122 (vs. gap), W219 (≠ Q216), A299 (≠ D298), L300 (≠ G299)
Sites not aligning to the query:
2iqdA Crystal structure of aldose reductase complexed with lipoic acid (see paper)
46% identity, 95% coverage: 4:305/319 of query aligns to 4:306/315 of 2iqdA
- active site: D43 (= D43), Y48 (= Y48), K77 (= K77), H110 (= H110)
- binding lipoic acid: W20 (= W20), Y48 (= Y48), H110 (= H110)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G18), T19 (= T19), W20 (= W20), D43 (= D43), Y48 (= Y48), H110 (= H110), Q183 (= Q180), Y209 (= Y206), S210 (≠ A207), P211 (= P208), L212 (= L209), S214 (≠ A211), P215 (≠ A212), D216 (≠ Y213), A245 (= A244), I260 (= I259), P261 (= P260), K262 (= K261), S263 (= S262), T265 (= T264), R268 (= R267), E271 (= E270), N272 (= N271), C298 (≠ T297)
2inzA Crystal structure of aldose reductase complexed with 2- hydroxyphenylacetic acid (see paper)
46% identity, 95% coverage: 4:305/319 of query aligns to 4:306/315 of 2inzA
- active site: D43 (= D43), Y48 (= Y48), K77 (= K77), H110 (= H110)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G18), T19 (= T19), W20 (= W20), D43 (= D43), Y48 (= Y48), H110 (= H110), S159 (= S158), Q183 (= Q180), Y209 (= Y206), S210 (≠ A207), P211 (= P208), L212 (= L209), S214 (≠ A211), P215 (≠ A212), D216 (≠ Y213), A245 (= A244), I260 (= I259), P261 (= P260), K262 (= K261), S263 (= S262), V264 (= V263), T265 (= T264), R268 (= R267), E271 (= E270), N272 (= N271), C298 (≠ T297)
- binding (2-hydroxyphenyl)acetic acid: W20 (= W20), Y48 (= Y48), H110 (= H110)
2f2kA Aldose reductase tertiary complex with NADPH and deg (see paper)
46% identity, 95% coverage: 4:305/319 of query aligns to 4:306/315 of 2f2kA
- active site: D43 (= D43), Y48 (= Y48), K77 (= K77), H110 (= H110)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G18 (= G18), T19 (= T19), W20 (= W20), D43 (= D43), Y48 (= Y48), H110 (= H110), N160 (= N159), Q183 (= Q180), Y209 (= Y206), S210 (≠ A207), P211 (= P208), L212 (= L209), S214 (≠ A211), P215 (≠ A212), D216 (≠ Y213), A245 (= A244), I260 (= I259), P261 (= P260), K262 (= K261), S263 (= S262), T265 (= T264), R268 (= R267), E271 (= E270), N272 (= N271), C298 (≠ T297)
- binding gamma-glutamyl-s-(1,2-dicarboxyethyl)cysteinylglycine: W20 (= W20), Y48 (= Y48), H110 (= H110), F122 (vs. gap), W219 (≠ Q216), C298 (≠ T297), L300 (≠ G299), L301 (≠ K300)
2acrA An anion binding site in human aldose reductase: mechanistic implications for the binding of citrate, cacodylate, and glucose-6- phosphate (see paper)
46% identity, 95% coverage: 4:305/319 of query aligns to 4:306/315 of 2acrA
- active site: D43 (= D43), Y48 (= Y48), K77 (= K77), H110 (= H110)
- binding cacodylate ion: W20 (= W20), Y48 (= Y48), H110 (= H110)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G18), T19 (= T19), W20 (= W20), K21 (≠ Q21), D43 (= D43), Y48 (= Y48), H110 (= H110), Q183 (= Q180), Y209 (= Y206), S210 (≠ A207), P211 (= P208), L212 (= L209), S214 (≠ A211), P215 (≠ A212), D216 (≠ Y213), A245 (= A244), I260 (= I259), P261 (= P260), K262 (= K261), S263 (= S262), V264 (= V263), T265 (= T264), R268 (= R267), E271 (= E270), N272 (= N271)
2acqA An anion binding site in human aldose reductase: mechanistic implications for the binding of citrate, cacodylate, and glucose-6- phosphate (see paper)
46% identity, 95% coverage: 4:305/319 of query aligns to 4:306/315 of 2acqA
- active site: D43 (= D43), Y48 (= Y48), K77 (= K77), H110 (= H110)
- binding 6-O-phosphono-alpha-D-glucopyranose: W20 (= W20), Y48 (= Y48), W79 (= W79), H110 (= H110), W111 (= W111), F122 (vs. gap), W219 (≠ Q216)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G18), T19 (= T19), W20 (= W20), K21 (≠ Q21), D43 (= D43), Y48 (= Y48), H110 (= H110), Q183 (= Q180), Y209 (= Y206), S210 (≠ A207), P211 (= P208), L212 (= L209), S214 (≠ A211), P215 (≠ A212), D216 (≠ Y213), A245 (= A244), I260 (= I259), P261 (= P260), K262 (= K261), S263 (= S262), T265 (= T264), R268 (= R267), E271 (= E270), N272 (= N271)
1ieiA Crystal structure of human aldose reductase complexed with the inhibitor zenarestat. (see paper)
46% identity, 95% coverage: 4:305/319 of query aligns to 4:306/315 of 1ieiA
- active site: D43 (= D43), Y48 (= Y48), K77 (= K77), H110 (= H110)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G18), W20 (= W20), D43 (= D43), Y48 (= Y48), H110 (= H110), S159 (= S158), Q183 (= Q180), Y209 (= Y206), S210 (≠ A207), P211 (= P208), L212 (= L209), S214 (≠ A211), D216 (≠ Y213), A245 (= A244), I260 (= I259), K262 (= K261), S263 (= S262), T265 (= T264), R268 (= R267), E271 (= E270), N272 (= N271)
- binding [3-(4-bromo-2-fluoro-benzyl)-7-chloro-2,4-dioxo-3,4-dihydro-2h-quinazolin-1-yl]-acetic acid: W20 (= W20), V47 (≠ I47), Y48 (= Y48), H110 (= H110), W111 (= W111), T113 (≠ L113), F122 (vs. gap), C298 (≠ T297), A299 (≠ D298), L300 (≠ G299)
Sites not aligning to the query:
1ef3A Fidarestat bound to human aldose reductase (see paper)
46% identity, 95% coverage: 4:305/319 of query aligns to 4:306/315 of 1ef3A
- active site: D43 (= D43), Y48 (= Y48), K77 (= K77), H110 (= H110)
- binding (2s,4s)-2-aminoformyl-6-fluoro-spiro[chroman-4,4'-imidazolidine]-2',5'-dione: W20 (= W20), Y48 (= Y48), H110 (= H110), W111 (= W111), W219 (≠ Q216), C298 (≠ T297), L300 (≠ G299)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G18), T19 (= T19), W20 (= W20), K21 (≠ Q21), D43 (= D43), Y48 (= Y48), K77 (= K77), H110 (= H110), Q183 (= Q180), Y209 (= Y206), S210 (≠ A207), L212 (= L209), S214 (≠ A211), P215 (≠ A212), D216 (≠ Y213), A245 (= A244), I260 (= I259), K262 (= K261), S263 (= S262), V264 (= V263), T265 (= T264), R268 (= R267), N272 (= N271)
4jirA Crystal structure of aldose reductase (akr1b1) complexed with NADP+ and epalrestat (see paper)
46% identity, 95% coverage: 4:305/319 of query aligns to 5:307/316 of 4jirA
- active site: D44 (= D43), Y49 (= Y48), K78 (= K77), H111 (= H110)
- binding {5-[(2E)-2-methyl-3-phenylprop-2-en-1-ylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl}acetic acid: W21 (= W20), Y49 (= Y48), H111 (= H110), F123 (vs. gap), C299 (≠ T297)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G19 (= G18), T20 (= T19), W21 (= W20), K22 (≠ Q21), D44 (= D43), Y49 (= Y48), H111 (= H110), N161 (= N159), Q184 (= Q180), Y210 (= Y206), S211 (≠ A207), P212 (= P208), L213 (= L209), S215 (≠ A211), P216 (≠ A212), D217 (≠ Y213), A246 (= A244), I261 (= I259), P262 (= P260), K263 (= K261), S264 (= S262), V265 (= V263), T266 (= T264), R269 (= R267), E272 (= E270), N273 (= N271), C299 (≠ T297)
Query Sequence
>Echvi_3562 FitnessBrowser__Cola:Echvi_3562
MKSLTFSNGDTMPIIGLGTWQSKPGEVYNAVLKAIEIGYRHFDCAYIYKNEKEIGDAFAK
AFADGTIKREDIWVTSKLWNDSHKPEHVLPALESTLKDLQLDYLDLYLVHWPLALKHGVD
FPEENGDFEHLDNIPLSTTWAAMEGLLETGKVKHIGVSNFKIEKLKEILASAKSKPEVNQ
VEMHPFLPQQGLVDYCKKEGIHLTAYAPLGAAYRTQGQDGVDLPILLENDQVKNIANKLN
ATTAQVVLAWNIQRDIAVIPKSVTPSRIEENFKSNLLTLSQEEMDQLNQLEGPYRFTDGK
LWTTHNSPYELSDFWEEYS
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