SitesBLAST
Comparing H281DRAFT_01117 H281DRAFT_01117 aldehyde dehydrogenase (NAD+) 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)
6mvtA Structure of a bacterial aldh16 complexed with nadh (see paper)
59% identity, 98% coverage: 15:794/795 of query aligns to 1:751/751 of 6mvtA
- active site: N151 (= N169), E247 (= E266), C281 (= C300), E450 (= E475)
- binding 1,4-dihydronicotinamide adenine dinucleotide: V147 (≠ I165), I148 (≠ V166), K174 (= K192), E177 (= E195), G207 (= G225), G210 (= G228), E211 (≠ A229), F223 (= F242), S226 (= S245), V229 (= V248), D327 (≠ V346), R331 (= R350)
6mvsA Structure of a bacterial aldh16 complexed with NAD (see paper)
59% identity, 98% coverage: 15:794/795 of query aligns to 1:751/751 of 6mvsA
- active site: N151 (= N169), E247 (= E266), C281 (= C300), E450 (= E475)
- binding nicotinamide-adenine-dinucleotide: V147 (≠ I165), I148 (≠ V166), W150 (= W168), K174 (= K192), E177 (= E195), G207 (= G225), G210 (= G228), E211 (≠ A229), F223 (= F242), S226 (= S245), V229 (= V248)
6mvuA Structure of a bacterial aldh16 active site mutant c295a complexed with p-nitrophenylacetate (see paper)
59% identity, 98% coverage: 15:794/795 of query aligns to 1:751/752 of 6mvuA
- active site: N151 (= N169), E247 (= E266), A281 (≠ C300), E450 (= E475)
- binding 4-nitrophenyl acetate: G207 (= G225), G210 (= G228), E211 (≠ A229), V214 (= V232), V229 (= V248), R232 (≠ L251), I233 (= I252), A236 (≠ V255)
5l13A Structure of aldh2 in complex with 2p3 (see paper)
45% identity, 57% coverage: 36:488/795 of query aligns to 17:483/494 of 5l13A
- active site: N163 (= N169), K186 (= K192), E262 (= E266), C296 (= C300), E393 (= E398), E470 (= E475)
- binding 2,3,5-trimethyl-6-propyl-7H-furo[3,2-g][1]benzopyran-7-one: F164 (= F170), M168 (= M174), W171 (= W177), F290 (= F294), C295 (≠ V299), C296 (= C300), C297 (= C301), D451 (≠ N456), F453 (= F458)
4kwgA Crystal structure analysis of aldh2+aldib13 (see paper)
45% identity, 57% coverage: 36:488/795 of query aligns to 17:483/494 of 4kwgA
- active site: N163 (= N169), K186 (= K192), E262 (= E266), C296 (= C300), E393 (= E398), E470 (= E475)
- binding 7-bromo-5-methyl-1H-indole-2,3-dione: F164 (= F170), M168 (= M174), C295 (≠ V299), C296 (= C300), C297 (= C301), D451 (≠ N456), F453 (= F458)
4kwfA Crystal structure analysis of aldh2+aldib33 (see paper)
45% identity, 57% coverage: 36:488/795 of query aligns to 17:483/494 of 4kwfA
- active site: N163 (= N169), K186 (= K192), E262 (= E266), C296 (= C300), E393 (= E398), E470 (= E475)
- binding 1-benzyl-1H-indole-2,3-dione: F164 (= F170), M168 (= M174), W171 (= W177), E262 (= E266), C295 (≠ V299), C296 (= C300), C297 (= C301), D451 (≠ N456), F453 (= F458), F459 (= F464)
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)
45% identity, 57% coverage: 36:488/795 of query aligns to 17:483/494 of 3sz9A
- active site: N163 (= N169), K186 (= K192), E262 (= E266), C296 (= C300), E393 (= E398), E470 (= E475)
- binding 1-(4-ethylphenyl)propan-1-one: F164 (= F170), C295 (≠ V299), C296 (= C300), D451 (≠ N456), F453 (= F458), F459 (= F464)
3injA Human mitochondrial aldehyde dehydrogenase complexed with agonist alda-1 (see paper)
45% identity, 57% coverage: 36:488/795 of query aligns to 17:483/494 of 3injA
- active site: N163 (= N169), K186 (= K192), E262 (= E266), C296 (= C300), E393 (= E398), E470 (= E475)
- binding N-(1,3-benzodioxol-5-ylmethyl)-2,6-dichlorobenzamide: M118 (≠ L134), F164 (= F170), L167 (= L173), F286 (≠ D290), F290 (= F294), D451 (≠ N456), F453 (= F458)
2vleA The structure of daidzin, a naturally occurring anti alcohol- addiction agent, in complex with human mitochondrial aldehyde dehydrogenase (see paper)
45% identity, 57% coverage: 36:488/795 of query aligns to 17:483/494 of 2vleA
- active site: N163 (= N169), K186 (= K192), E262 (= E266), C296 (= C300), E393 (= E398), E470 (= E475)
- binding daidzin: M118 (≠ L134), F164 (= F170), M168 (= M174), W171 (= W177), F286 (≠ D290), F290 (= F294), C295 (≠ V299), C296 (= C300), D451 (≠ N456), V452 (≠ L457), F453 (= F458)
1o01B Human mitochondrial aldehyde dehydrogenase complexed with crotonaldehyde, NAD(h) and mg2+ (see paper)
45% identity, 57% coverage: 36:488/795 of query aligns to 17:483/494 of 1o01B
- active site: N163 (= N169), K186 (= K192), E262 (= E266), C296 (= C300), E393 (= E398), E470 (= E475)
- binding (2e)-but-2-enal: C296 (= C300), C297 (= C301), F453 (= F458)
- binding nicotinamide-adenine-dinucleotide: I159 (= I165), I160 (≠ V166), P161 (= P167), W162 (= W168), K186 (= K192), E189 (= E195), G219 (= G225), G223 (= G228), A224 (= A229), F237 (= F242), G239 (= G244), S240 (= S245), I243 (≠ V248), L263 (= L267), G264 (= G268), C296 (= C300), Q343 (= Q347), E393 (= E398), F395 (= F400)
1cw3A Human mitochondrial aldehyde dehydrogenase complexed with NAD+ and mn2+ (see paper)
45% identity, 57% coverage: 36:488/795 of query aligns to 17:483/494 of 1cw3A
- active site: N163 (= N169), K186 (= K192), E262 (= E266), C296 (= C300), E393 (= E398), E470 (= E475)
- binding magnesium ion: V34 (≠ H53), D103 (= D119), Q190 (≠ Y196)
- binding nicotinamide-adenine-dinucleotide: I159 (= I165), I160 (≠ V166), P161 (= P167), W162 (= W168), K186 (= K192), G219 (= G225), G223 (= G228), A224 (= A229), F237 (= F242), G239 (= G244), S240 (= S245), I243 (≠ V248), L263 (= L267), G264 (= G268), C296 (= C300), Q343 (= Q347), K346 (≠ R350), E393 (= E398), F395 (= F400)
2onmA Human mitochondrial aldehyde dehydrogenase asian variant, aldh2 2, Complexed with NAD+ (see paper)
46% identity, 56% coverage: 36:484/795 of query aligns to 17:479/494 of 2onmA
- active site: N163 (= N169), K186 (= K192), E262 (= E266), C296 (= C300), E393 (= E398), E470 (= E475)
- binding adenosine-5'-diphosphate: E189 (= E195), G219 (= G225), G223 (= G228), A224 (= A229), F237 (= F242), G239 (= G244), S240 (= S245), I243 (≠ V248)
P20000 Aldehyde dehydrogenase, mitochondrial; ALDH class 2; ALDH-E2; ALDHI; EC 1.2.1.3 from Bos taurus (Bovine) (see 2 papers)
45% identity, 56% coverage: 36:484/795 of query aligns to 43:505/520 of P20000
Sites not aligning to the query:
- 1:21 modified: transit peptide, Mitochondrion
6b5hA Aldh1a2 liganded with NAD and 1-(4-cyanophenyl)-n-(3-fluorophenyl)-3- [4-(methylsulfonyl)phenyl]-1h-pyrazole-4-carboxamide (compound cm121) (see paper)
44% identity, 56% coverage: 36:484/795 of query aligns to 15:477/492 of 6b5hA
- active site: N161 (= N169), E260 (= E266), C294 (= C300), E468 (= E475)
- binding 1-(4-cyanophenyl)-N-(3-fluorophenyl)-3-[4-(methylsulfonyl)phenyl]-1H-pyrazole-4-carboxamide: V112 (≠ L130), G116 (≠ L134), F162 (= F170), W169 (= W177), Q284 (≠ D290), F288 (= F294), T295 (≠ C301), N449 (= N456), L451 (≠ F458), N452 (≠ D459), F457 (= F464)
- binding nicotinamide-adenine-dinucleotide: I157 (= I165), I158 (≠ V166), W160 (= W168), N161 (= N169), K184 (= K192), G217 (= G225), G221 (= G228), F235 (= F242), T236 (= T243), G237 (= G244), S238 (= S245), V241 (= V248), E260 (= E266), L261 (= L267), C294 (= C300), F393 (= F400)
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)
44% identity, 56% coverage: 36:484/795 of query aligns to 15:477/492 of 6b5gA
- active site: N161 (= N169), E260 (= E266), C294 (= C300), E468 (= E475)
- binding (3-ethoxythiophen-2-yl){4-[4-nitro-3-(pyrrolidin-1-yl)phenyl]piperazin-1-yl}methanone: F162 (= F170), L165 (= L173), W169 (= W177), F288 (= F294), C293 (≠ V299), C294 (= C300), T295 (≠ C301), N449 (= N456), L451 (≠ F458)
- binding nicotinamide-adenine-dinucleotide: I157 (= I165), I158 (≠ V166), P159 (= P167), W160 (= W168), N161 (= N169), M166 (= M174), K184 (= K192), E187 (= E195), G217 (= G225), G221 (= G228), F235 (= F242), T236 (= T243), G237 (= G244), S238 (= S245), V241 (= V248), E260 (= E266), L261 (= L267), C294 (= C300), E391 (= E398), F393 (= F400)
6aljA Aldh1a2 liganded with NAD and compound win18,446 (see paper)
44% identity, 56% coverage: 36:484/795 of query aligns to 15:477/492 of 6aljA
- active site: N161 (= N169), E260 (= E266), C294 (= C300), E468 (= E475)
- binding N,N'-(octane-1,8-diyl)bis(2,2-dichloroacetamide): G116 (≠ L134), F162 (= F170), L165 (= L173), M166 (= M174), W169 (= W177), E260 (= E266), C293 (≠ V299), C294 (= C300), L451 (≠ F458), N452 (≠ D459), A453 (= A460)
- binding nicotinamide-adenine-dinucleotide: I157 (= I165), I158 (≠ V166), P159 (= P167), W160 (= W168), N161 (= N169), K184 (= K192), E187 (= E195), G217 (= G225), G221 (= G228), F235 (= F242), G237 (= G244), S238 (= S245), V241 (= V248), Q341 (= Q347), K344 (≠ R350), E391 (= E398), F393 (= F400)
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)
44% identity, 56% coverage: 36:484/795 of query aligns to 41:503/518 of O94788
- E50 (≠ A45) to G: in dbSNP:rs34266719
- A110 (= A102) to V: in dbSNP:rs35365164
- Q182 (= Q164) to K: in DIH4; decreased retinoic acid biosynthetic process
- IPW 184:186 (≠ VPW 166:168) binding
- KPAE 210:213 (= KPAE 192:195) binding
- STE 264:266 (= STE 245:247) binding
- C320 (= C300) active site, Nucleophile
- R347 (≠ L327) to H: in DIH4; decreased expression; dbSNP:rs141245344
- V348 (≠ R328) to I: in dbSNP:rs4646626
- KQYNK 366:370 (≠ VQLER 346:350) binding
- A383 (≠ C363) to T: in DIH4; uncertain significance; dbSNP:rs749124508
- E417 (= E398) binding
- E436 (≠ A417) to K: in dbSNP:rs34744827
- S461 (≠ A442) to Y: in DIH4; decreased retinoic acid biosynthetic process
1nzwA Cys302ser mutant of human mitochondrial aldehyde dehydrogenase complexed with nadh and mg2+ (see paper)
45% identity, 57% coverage: 36:488/795 of query aligns to 17:483/494 of 1nzwA
- active site: N163 (= N169), K186 (= K192), E262 (= E266), S296 (≠ C300), E393 (= E398), E470 (= E475)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I159 (= I165), I160 (≠ V166), P161 (= P167), K186 (= K192), E189 (= E195), G219 (= G225), P220 (≠ S226), G223 (= G228), A224 (= A229), F237 (= F242), G239 (= G244), S240 (= S245), I243 (≠ V248), E262 (= E266), G264 (= G268), S296 (≠ C300), Q343 (= Q347), E393 (= E398), F395 (= F400)
4fr8C Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
45% identity, 57% coverage: 36:488/795 of query aligns to 19:485/496 of 4fr8C
- active site: N165 (= N169), K188 (= K192), Q264 (≠ E266), C298 (= C300), E395 (= E398), E472 (= E475)
- binding nicotinamide-adenine-dinucleotide: I161 (= I165), I162 (≠ V166), W164 (= W168), K188 (= K192), G221 (= G225), G225 (= G228), A226 (= A229), F239 (= F242), G241 (= G244), S242 (= S245), I245 (≠ V248), Q345 (= Q347), E395 (= E398), F397 (= F400)
4fr8A Crystal structure of human aldehyde dehydrogenase-2 in complex with nitroglycerin (see paper)
45% identity, 57% coverage: 36:488/795 of query aligns to 16:482/493 of 4fr8A
- active site: N162 (= N169), K185 (= K192), Q261 (≠ E266), C295 (= C300), E392 (= E398), E469 (= E475)
- binding nicotinamide-adenine-dinucleotide: I158 (= I165), I159 (≠ V166), W161 (= W168), K185 (= K192), G218 (= G225), G222 (= G228), A223 (= A229), F236 (= F242), G238 (= G244), S239 (= S245), I242 (≠ V248), Q342 (= Q347), K345 (≠ R350), E392 (= E398), F394 (= F400)
- binding propane-1,2,3-triyl trinitrate: F163 (= F170), L166 (= L173), W170 (= W177), F289 (= F294), S294 (≠ V299), C295 (= C300), D450 (≠ N456), F452 (= F458)
Query Sequence
>H281DRAFT_01117 H281DRAFT_01117 aldehyde dehydrogenase (NAD+)
MSVAEYFSSMDYGPAPEDDQPARQWLAQHEARFGHFIGGAWHAPASGAQFVSHAPASGER
LADIAQGDAADIDAALAAARAAQPGWLALGGKGRARHLYALARMVQRHSRLFAVLEALDN
GKPIRETRDLDVPLVARHFLHHAGWAQLQDSEFADHAPLGVIGQIVPWNFPLLMLAWKIA
PAIATGNCVVLKPAEYTPLTALLFAELAHQAGLPAGVLNVVTGDGSTGAALVEHPQVDKI
AFTGSTEVGKLIRSVTAGSGKSLTLELGGKSPFIVFDDADLDGAVEGVVDAIWFNQGQVC
CAGSRLLVQEGIEARFIAKLKRRMETLRVGPSLDKSIDMGAIVDPVQLERIHSLVETGRR
EGCAIWQAADTPLPANGCFYPPTLVTNVAPASTLAQEEIFGPVLVTMSFRTPDEAIALAN
NSRYGLAASVWSETIGRALDVAPRLAAGVVWVNATNLFDAAVGFGGYRESGYGREGGREG
IHEYLKPRAWLNLPKRQPVSAATNASDDRQVSNLALVDRTAKLFIGGKQVRPDSGYSLPV
HAPDGTRVGEVGEGNRKDIRNAVQAARAAQKWSQASTHNRAQVLFYLAENLAVRADEFAH
QLTVRNGATDAAAHAEVEASVTRLFTYAAWADKFDGAVHTPPLRGVALAMHEPLGVIGIA
CPDEAPLLAFVSLAAPALAMGNRVVVLPGEACPLAVTDFYQVVETSDVPGGVVNIVTGKR
EALLPALARHDDVDAVWCFGSAADATLIERESVGNLKRTFTDYGRQFDWFDRASEGLPFL
RQAVQVKNIWIPYGD
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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