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Comparing HSERO_RS05115 FitnessBrowser__HerbieS:HSERO_RS05115 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)
6mvtA Structure of a bacterial aldh16 complexed with nadh (see paper)
58% identity, 98% coverage: 15:792/793 of query aligns to 1:751/751 of 6mvtA
- active site: N151 (= N167), E247 (= E264), C281 (= C298), E450 (= E472)
- binding 1,4-dihydronicotinamide adenine dinucleotide: V147 (≠ I163), I148 (≠ V164), K174 (= K190), E177 (= E193), G207 (= G223), G210 (= G226), E211 (≠ A227), F223 (= F240), S226 (= S243), V229 (= V246), D327 (≠ V344), R331 (= R348)
6mvsA Structure of a bacterial aldh16 complexed with NAD (see paper)
58% identity, 98% coverage: 15:792/793 of query aligns to 1:751/751 of 6mvsA
- active site: N151 (= N167), E247 (= E264), C281 (= C298), E450 (= E472)
- binding nicotinamide-adenine-dinucleotide: V147 (≠ I163), I148 (≠ V164), W150 (= W166), K174 (= K190), E177 (= E193), G207 (= G223), G210 (= G226), E211 (≠ A227), F223 (= F240), S226 (= S243), V229 (= V246)
6mvuA Structure of a bacterial aldh16 active site mutant c295a complexed with p-nitrophenylacetate (see paper)
57% identity, 98% coverage: 15:792/793 of query aligns to 1:751/752 of 6mvuA
- active site: N151 (= N167), E247 (= E264), A281 (≠ C298), E450 (= E472)
- binding 4-nitrophenyl acetate: G207 (= G223), G210 (= G226), E211 (≠ A227), V214 (= V230), V229 (= V246), R232 (≠ L249), I233 (= I250), A236 (≠ Q253)
6b5hA Aldh1a2 liganded with NAD and 1-(4-cyanophenyl)-n-(3-fluorophenyl)-3- [4-(methylsulfonyl)phenyl]-1h-pyrazole-4-carboxamide (compound cm121) (see paper)
45% identity, 54% coverage: 52:481/793 of query aligns to 33:477/492 of 6b5hA
- active site: N161 (= N167), E260 (= E264), C294 (= C298), E468 (= E472)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (= V128), G116 (≠ L132), F162 (= F168), W169 (= W175), Q284 (≠ D288), F288 (= F292), T295 (≠ C299), N449 (= N453), L451 (≠ F455), N452 (≠ D456), F457 (= F461)
- binding nicotinamide-adenine-dinucleotide: I157 (= I163), I158 (≠ V164), W160 (= W166), N161 (= N167), K184 (= K190), G217 (= G223), G221 (= G226), F235 (= F240), T236 (= T241), G237 (= G242), S238 (= S243), V241 (= V246), E260 (= E264), L261 (= L265), C294 (= C298), F393 (= F397)
6b5gA Aldh1a2 liganded with NAD and (3-ethoxythiophen-2-yl){4-[4-nitro-3- (pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone (compound 6-118) (see paper)
45% identity, 54% coverage: 52:481/793 of query aligns to 33:477/492 of 6b5gA
- active site: N161 (= N167), E260 (= E264), C294 (= C298), E468 (= E472)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (= F168), L165 (= L171), W169 (= W175), F288 (= F292), C293 (≠ V297), C294 (= C298), T295 (≠ C299), N449 (= N453), L451 (≠ F455)
- binding nicotinamide-adenine-dinucleotide: I157 (= I163), I158 (≠ V164), P159 (= P165), W160 (= W166), N161 (= N167), M166 (= M172), K184 (= K190), E187 (= E193), G217 (= G223), G221 (= G226), F235 (= F240), T236 (= T241), G237 (= G242), S238 (= S243), V241 (= V246), E260 (= E264), L261 (= L265), C294 (= C298), E391 (= E395), F393 (= F397)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
45% identity, 54% coverage: 52:481/793 of query aligns to 33:477/492 of 6aljA
- active site: N161 (= N167), E260 (= E264), C294 (= C298), E468 (= E472)
- binding N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide): G116 (≠ L132), F162 (= F168), L165 (= L171), M166 (= M172), W169 (= W175), E260 (= E264), C293 (≠ V297), C294 (= C298), L451 (≠ F455), N452 (≠ D456), A453 (= A457)
- binding nicotinamide-adenine-dinucleotide: I157 (= I163), I158 (≠ V164), P159 (= P165), W160 (= W166), N161 (= N167), K184 (= K190), E187 (= E193), G217 (= G223), G221 (= G226), F235 (= F240), G237 (= G242), S238 (= S243), V241 (= V246), Q341 (= Q345), K344 (≠ R348), E391 (= E395), F393 (= F397)
O94788 Retinal dehydrogenase 2; RALDH 2; RalDH2; Aldehyde dehydrogenase family 1 member A2; ALDH1A2; Retinaldehyde-specific dehydrogenase type 2; RALDH(II); EC 1.2.1.36 from Homo sapiens (Human) (see 6 papers)
45% identity, 54% coverage: 52:481/793 of query aligns to 59:503/518 of O94788
- A110 (= A100) to V: in dbSNP:rs35365164
- Q182 (= Q162) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (≠ VPW 164:166) binding
- KPAE 210:213 (= KPAE 190:193) binding
- STE 264:266 (= STE 243:245) binding
- C320 (= C298) active site, Nucleophile
- R347 (≠ L325) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ K326) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ VQLER 344:348) binding
- A383 (= A361) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E395) binding
- E436 (≠ Q414) to K: in dbSNP:rs34744827
- S461 (≠ A439) to Y: in DIH4; decreased retinoic acid biosynthetic process
Sites not aligning to the query:
- 50 E → G: in dbSNP:rs34266719
7radA Crystal structure analysis of aldh1b1
44% identity, 55% coverage: 45:481/793 of query aligns to 27:478/493 of 7radA
- binding nicotinamide-adenine-dinucleotide: I158 (= I163), I159 (≠ V164), P160 (= P165), W161 (= W166), N162 (= N167), M167 (= M172), K185 (= K190), E188 (= E193), G218 (= G223), G222 (= G226), A223 (= A227), T237 (= T241), G238 (= G242), S239 (= S243), V242 (= V246), E261 (= E264), L262 (= L265), C295 (= C298), E392 (= E395), F394 (= F397)
- binding 3-(2-methoxyphenyl)-1-(4-phenylphenyl)-6,7,8,9-tetrahydro-5~{H}-imidazo[1,2-a][1,3]diazepine: L113 (≠ V128), E117 (≠ L132), F163 (= F168), E285 (≠ D288), F289 (= F292), N450 (= N453), V452 (≠ F455)
7mjdA Crystal structure analysis of aldh1b1
44% identity, 55% coverage: 45:481/793 of query aligns to 27:478/493 of 7mjdA
- binding nicotinamide-adenine-dinucleotide: I158 (= I163), I159 (≠ V164), P160 (= P165), W161 (= W166), N162 (= N167), M167 (= M172), K185 (= K190), E188 (= E193), G218 (= G223), G222 (= G226), F236 (= F240), T237 (= T241), G238 (= G242), S239 (= S243), V242 (= V246), E261 (= E264), L262 (= L265), C295 (= C298), E392 (= E395), F394 (= F397)
- binding 8-(2-methoxyphenyl)-10-(4-phenylphenyl)-1$l^{4},8-diazabicyclo[5.3.0]deca-1(7),9-diene: E117 (≠ L132), E285 (≠ D288), F289 (= F292), N450 (= N453), V452 (≠ F455)
7mjcA Crystal structure analysis of aldh1b1
44% identity, 55% coverage: 45:481/793 of query aligns to 27:478/493 of 7mjcA
- binding nicotinamide-adenine-dinucleotide: I158 (= I163), I159 (≠ V164), P160 (= P165), W161 (= W166), N162 (= N167), K185 (= K190), E188 (= E193), G218 (= G223), G222 (= G226), T237 (= T241), G238 (= G242), S239 (= S243), V242 (= V246), E261 (= E264), L262 (= L265), C295 (= C298), E392 (= E395), F394 (= F397)
Q63639 Retinal dehydrogenase 2; RALDH 2; RalDH2; Aldehyde dehydrogenase family 1 member A2; ALDH1A2; Retinaldehyde-specific dehydrogenase type 2; RALDH(II); EC 1.2.1.36 from Rattus norvegicus (Rat) (see paper)
44% identity, 54% coverage: 52:481/793 of query aligns to 59:503/518 of Q63639
5l13A Structure of aldh2 in complex with 2p3 (see paper)
44% identity, 54% coverage: 51:481/793 of query aligns to 34:479/494 of 5l13A
- active site: N163 (= N167), K186 (= K190), E262 (= E264), C296 (= C298), E393 (= E395), E470 (= E472)
- binding 2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one: F164 (= F168), M168 (= M172), W171 (= W175), F290 (= F292), C295 (≠ V297), C296 (= C298), C297 (= C299), D451 (≠ N453), F453 (= F455)
4kwgA Crystal structure analysis of aldh2+aldib13 (see paper)
44% identity, 54% coverage: 51:481/793 of query aligns to 34:479/494 of 4kwgA
- active site: N163 (= N167), K186 (= K190), E262 (= E264), C296 (= C298), E393 (= E395), E470 (= E472)
- binding 7-bromo-5-methyl-1H-indole-2,3-dione: F164 (= F168), M168 (= M172), C295 (≠ V297), C296 (= C298), C297 (= C299), D451 (≠ N453), F453 (= F455)
4kwfA Crystal structure analysis of aldh2+aldib33 (see paper)
44% identity, 54% coverage: 51:481/793 of query aligns to 34:479/494 of 4kwfA
- active site: N163 (= N167), K186 (= K190), E262 (= E264), C296 (= C298), E393 (= E395), E470 (= E472)
- binding 1-benzyl-1H-indole-2,3-dione: F164 (= F168), M168 (= M172), W171 (= W175), E262 (= E264), C295 (≠ V297), C296 (= C298), C297 (= C299), D451 (≠ N453), F453 (= F455), F459 (= F461)
3sz9A Crystal structure of human aldh2 modified with the beta-elimination product of aldi-3; 1-(4-ethylbenzene)prop-2-en-1-one (see paper)
44% identity, 54% coverage: 51:481/793 of query aligns to 34:479/494 of 3sz9A
- active site: N163 (= N167), K186 (= K190), E262 (= E264), C296 (= C298), E393 (= E395), E470 (= E472)
- binding 1-(4-ethylphenyl)propan-1-one: F164 (= F168), C295 (≠ V297), C296 (= C298), D451 (≠ N453), F453 (= F455), F459 (= F461)
3injA Human mitochondrial aldehyde dehydrogenase complexed with agonist alda-1 (see paper)
44% identity, 54% coverage: 51:481/793 of query aligns to 34:479/494 of 3injA
- active site: N163 (= N167), K186 (= K190), E262 (= E264), C296 (= C298), E393 (= E395), E470 (= E472)
- binding N-(1,3-benzodioxol-5-ylmethyl)-2,6-dichlorobenzamide: M118 (≠ L132), F164 (= F168), L167 (= L171), F286 (≠ D288), F290 (= F292), D451 (≠ N453), F453 (= F455)
2vleA The structure of daidzin, a naturally occurring anti alcohol- addiction agent, in complex with human mitochondrial aldehyde dehydrogenase (see paper)
44% identity, 54% coverage: 51:481/793 of query aligns to 34:479/494 of 2vleA
- active site: N163 (= N167), K186 (= K190), E262 (= E264), C296 (= C298), E393 (= E395), E470 (= E472)
- binding daidzin: M118 (≠ L132), F164 (= F168), M168 (= M172), W171 (= W175), F286 (≠ D288), F290 (= F292), C295 (≠ V297), C296 (= C298), D451 (≠ N453), V452 (≠ Q454), F453 (= F455)
1o01B Human mitochondrial aldehyde dehydrogenase complexed with crotonaldehyde, NAD(h) and mg2+ (see paper)
44% identity, 54% coverage: 51:481/793 of query aligns to 34:479/494 of 1o01B
- active site: N163 (= N167), K186 (= K190), E262 (= E264), C296 (= C298), E393 (= E395), E470 (= E472)
- binding (2e)-but-2-enal: C296 (= C298), C297 (= C299), F453 (= F455)
- binding nicotinamide-adenine-dinucleotide: I159 (= I163), I160 (≠ V164), P161 (= P165), W162 (= W166), K186 (= K190), E189 (= E193), G219 (= G223), G223 (= G226), A224 (= A227), F237 (= F240), G239 (= G242), S240 (= S243), I243 (≠ V246), L263 (= L265), G264 (= G266), C296 (= C298), Q343 (= Q345), E393 (= E395), F395 (= F397)
1cw3A Human mitochondrial aldehyde dehydrogenase complexed with NAD+ and mn2+ (see paper)
44% identity, 54% coverage: 51:481/793 of query aligns to 34:479/494 of 1cw3A
- active site: N163 (= N167), K186 (= K190), E262 (= E264), C296 (= C298), E393 (= E395), E470 (= E472)
- binding magnesium ion: V34 (≠ I51), D103 (= D117), Q190 (≠ N194)
- binding nicotinamide-adenine-dinucleotide: I159 (= I163), I160 (≠ V164), P161 (= P165), W162 (= W166), K186 (= K190), G219 (= G223), G223 (= G226), A224 (= A227), F237 (= F240), G239 (= G242), S240 (= S243), I243 (≠ V246), L263 (= L265), G264 (= G266), C296 (= C298), Q343 (= Q345), K346 (≠ R348), E393 (= E395), F395 (= F397)
2onmA Human mitochondrial aldehyde dehydrogenase asian variant, aldh2 2, Complexed with NAD+ (see paper)
44% identity, 54% coverage: 51:481/793 of query aligns to 34:479/494 of 2onmA
- active site: N163 (= N167), K186 (= K190), E262 (= E264), C296 (= C298), E393 (= E395), E470 (= E472)
- binding adenosine-5'-diphosphate: E189 (= E193), G219 (= G223), G223 (= G226), A224 (= A227), F237 (= F240), G239 (= G242), S240 (= S243), I243 (≠ V246)
Query Sequence
>HSERO_RS05115 FitnessBrowser__HerbieS:HSERO_RS05115
MSVSTYFDTMDYGPAPESDKDARAWLASHEASFGHFIAGRFTQPKADLDDIDPASGKLLA
HLSQGSAADVDAAVQAAQAALPGWQALGGHGRARHLYALARTVQRHARLLAVLETLDNGK
PLRESRDVDVPLVARHFYHYAGWAQLQESEFPDHVPVGVVGQIVPWNFPLLMLAWKIAPA
LALGNTVVLKPAENTSLTALLFAELAQQAGLPAGVLNIVTGDGATGAAVVAHPGIQKIAF
TGSTEVGRLIREQTAGSGKSLTLELGGKSPFIVFEDADIDAAIEGVVDAIWFNQGQVCCA
GSRLLVQEGIHDLFIARLKTRMQKLKVGAPLDKCSDMGALISPVQLERVRSLVEQGVREG
AQCHQVVLDTPPGGCFYPPTLLTGVHPAATVASEEIFGPVLVAMSFRTPDEAVQLANNSR
YGLAASIWSETIGLALGVAPQLKAGVVWINSTNQFDAAVGFGGVRESGYGREGGREGCYE
YLKPRRQQAGSLRQPSARRAIRADADSPLQGGAIDRTAKLYIGGKQVRPDGEVSMACHST
QGERLEDVGLGNRKDIRNAVAAAVKAGGWTSASPHRRAQGLYYIAENLSARTEEFARRIA
STTGVTADEARAEVDASIKRLFTYGAWADKFEGAVHQPPMRGVALAMPEAIGVVGVVCPE
EKPLLALISLVAPLIAMGNRVVVVPSEQAPLVATDLYQVLDTSDLPAGVINIVTGKSAEL
LPVLAEHDEVEALWVRGPAEFSATAERLSTGNLKRCFVDHGYVTDWHDAAQGEGAQYLRQ
ATHIKNVWIPYGE
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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