SitesBLAST
Comparing H281DRAFT_00358 FitnessBrowser__Burk376:H281DRAFT_00358 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)
3fx4A Porcine aldehyde reductase in ternary complex with inhibitor (see paper)
40% identity, 95% coverage: 14:310/312 of query aligns to 7:312/325 of 3fx4A
- active site: D45 (= D52), Y50 (= Y57), K80 (= K86), H113 (= H119)
- binding [(5Z)-5-{[3-(carboxymethoxy)-4-methoxyphenyl]methylidene}-2,4-dioxo-1,3-thiazolidin-3-yl]acetic acid: W22 (≠ L29), Y50 (= Y57), H113 (= H119), R218 (= R225), A219 (vs. gap), F298 (= F296), I299 (≠ N297), V300 (≠ Q298)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G27), T21 (= T28), W22 (≠ L29), D45 (= D52), Y50 (= Y57), H113 (= H119), Q184 (= Q191), Y210 (≠ F217), S211 (≠ A218), P212 (= P219), L213 (= L220), S215 (≠ H222), A246 (= A246), I261 (≠ L261), P262 (≠ T262), K263 (≠ T263), S264 (≠ P264), V265 (≠ K265), T266 (= T266), R269 (= R269), Q272 (≠ E272), N273 (= N273)
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)
40% identity, 95% coverage: 14:310/312 of query aligns to 7:312/325 of P50578
- Y50 (= Y57) active site, Proton donor
- H113 (= H119) binding
- 211:273 (vs. 218:273, 37% identical) binding
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)
40% identity, 95% coverage: 14:310/312 of query aligns to 7:312/325 of P51635
- K13 (≠ S20) Not glycated
- K23 (≠ I30) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K30 (≠ I37) Not glycated
- K34 (= K41) Not glycated
- K61 (≠ Q68) Not glycated
- K68 (vs. gap) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K80 (= K86) Not glycated
- K85 (≠ N91) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K97 (≠ A103) Not glycated
- K127 (≠ R133) Not glycated
- K134 (≠ L140) Not glycated
- K141 (≠ L148) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K145 (≠ R152) Not glycated
- K153 (≠ G160) modified: carbohydrate, N-linked (Glc) (glycation) lysine
- K157 (≠ R164) Not glycated
- K240 (≠ R240) Not glycated
- K257 (≠ G257) Not glycated
- K263 (≠ T263) Not glycated
- K287 (≠ D285) Not glycated
- K294 (≠ T292) Not glycated
- K308 (≠ G306) Not glycated
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylthreonine
3h4gA Structure of aldehyde reductase holoenzyme in complex with potent aldose reductase inhibitor fidarestat: implications for inhibitor binding and selectivity (see paper)
41% identity, 91% coverage: 14:296/312 of query aligns to 7:298/320 of 3h4gA
- active site: D45 (= D52), Y50 (= Y57), K80 (= K86), H113 (= H119)
- binding (2s,4s)-2-aminoformyl-6-fluoro-spiro[chroman-4,4'-imidazolidine]-2',5'-dione: W22 (≠ L29), Y50 (= Y57), H113 (= H119), W114 (≠ T120), W220 (vs. gap)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G27), T21 (= T28), W22 (≠ L29), D45 (= D52), Y50 (= Y57), H113 (= H119), S162 (= S169), N163 (≠ D170), Q184 (= Q191), Y210 (≠ F217), S211 (≠ A218), P212 (= P219), L213 (= L220), S215 (≠ H222), D217 (≠ I224), A246 (= A246), I261 (≠ L261), P262 (≠ T262), K263 (≠ T263), S264 (≠ P264), V265 (≠ K265), T266 (= T266), R269 (= R269), Q272 (≠ E272), N273 (= N273)
Sites not aligning to the query:
3cv7A Crystal structure of porcine aldehyde reductase ternary complex (see paper)
41% identity, 91% coverage: 14:296/312 of query aligns to 7:298/322 of 3cv7A
- active site: D45 (= D52), Y50 (= Y57), K80 (= K86), H113 (= H119)
- binding 3,5-dichloro-2-hydroxybenzoic acid: W22 (≠ L29), Y50 (= Y57), W82 (= W88), H113 (= H119)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G20 (= G27), T21 (= T28), W22 (≠ L29), Y50 (= Y57), H113 (= H119), Q184 (= Q191), Y210 (≠ F217), S211 (≠ A218), P212 (= P219), L213 (= L220), S215 (≠ H222), A246 (= A246), I261 (≠ L261), P262 (≠ T262), K263 (≠ T263), S264 (≠ P264), V265 (≠ K265), T266 (= T266), R269 (= R269), Q272 (≠ E272), N273 (= N273)
Sites not aligning to the query:
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)
39% identity, 95% coverage: 14:310/312 of query aligns to 7:312/325 of P14550
- Y50 (= Y57) active site, Proton donor; mutation to F: Complete loss of enzymatic activity.; mutation to H: Complete loss of enzymatic activity.
- N52 (= N59) to S: reduced activity towards daunorubicin; dbSNP:rs2229540
- E55 (= E62) to D: reduced activity towards daunorubicin; dbSNP:rs6690497
- K80 (= K86) Lowers pKa of active site Tyr; mutation to M: Complete loss of enzymatic activity.
- H113 (= H119) binding ; mutation to Q: Strong decrease in enzymatic activity.
- I299 (≠ N297) mutation to A: No change in enzymatic activity.; mutation to C: No change in enzymatic activity.
- V300 (≠ Q298) mutation to C: No change in enzymatic activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
Q9JII6 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 Mus musculus (Mouse)
41% identity, 88% coverage: 14:289/312 of query aligns to 7:294/325 of Q9JII6
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylthreonine
1xf0A Crystal structure of human 17beta-hydroxysteroid dehydrogenase type 5 (akr1c3) complexed with delta4-androstene-3,17-dione and NADP (see paper)
40% identity, 93% coverage: 18:307/312 of query aligns to 9:310/316 of 1xf0A
- active site: D43 (= D52), Y48 (= Y57), K77 (= K86), H110 (= H119)
- binding 4-androstene-3-17-dione: M113 (≠ F122), N160 (≠ D170), W220 (vs. gap), F299 (= F296), F304 (≠ K301)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G27), Y20 (≠ L29), D43 (= D52), Y48 (= Y57), H110 (= H119), N160 (≠ D170), Q183 (= Q191), Y209 (≠ F217), S210 (≠ A218), L212 (= L220), S214 (≠ H222), Q215 (≠ G223), L229 (= L229), A246 (= A246), L261 (= L261), K263 (≠ T263), S264 (≠ P264), R269 (= R269), Q272 (≠ E272), N273 (= N273), F299 (= F296)
Q04828 Aldo-keto reductase family 1 member C1; 20-alpha-hydroxysteroid dehydrogenase; 20-alpha-HSD; Chlordecone reductase homolog HAKRC; Dihydrodiol dehydrogenase 1; DD1; High-affinity hepatic bile acid-binding protein; HBAB; EC 1.1.1.-; EC 1.1.1.112; EC 1.1.1.209; EC 1.1.1.210; EC 1.1.1.357; EC 1.1.1.51; EC 1.1.1.53; EC 1.1.1.62; EC 1.3.1.20; EC 1.1.1.149 from Homo sapiens (Human) (see 2 papers)
40% identity, 91% coverage: 6:289/312 of query aligns to 2:301/323 of Q04828
- GFGTY 20:24 (≠ GFGTL 25:29) binding
- D50 (= D52) binding
- E127 (= E129) mutation to D: 30-fold decrease in k(cat)/K(m) value for progesterone reduction; no effect on the K(m) value.
- SN 166:167 (≠ SD 169:170) binding
- Q190 (= Q191) binding
- 216:222 (vs. 217:223, 29% identical) binding
- H222 (≠ G223) mutation to I: Marked decrease in k(cat)/K(m) value for progesterone; 24-fold decrease for progesterone reduction; 18-fold decrease for 20alpha-OHProg oxidation. 95-fold decrease in K(m) value for NADPH.; mutation to S: Marked decrease in k(cat)/K(m) value for progesterone; 10-fold decrease for progesterone reduction; 3-fold decrease for 20alpha-OHProg oxidation. 10-fold decrease in K(m) value for NADPH.
- 270:280 (vs. 263:273, 27% identical) binding
Sites not aligning to the query:
- 304 R→L: 70-fold decrease in progesterone reduction. No effect on DHT reduction.
- 305 Y→F: No effect on progesterone reduction.
- 307 T→V: No effect on progesterone reduction.
- 309 D→V: No effect on progesterone reduction.
P52895 Aldo-keto reductase family 1 member C2; 3-alpha-HSD3; Chlordecone reductase homolog HAKRD; Dihydrodiol dehydrogenase 2; DD-2; DD2; Dihydrodiol dehydrogenase/bile acid-binding protein; DD/BABP; Type III 3-alpha-hydroxysteroid dehydrogenase; EC 1.-.-.-; EC 1.1.1.112; EC 1.1.1.209; EC 1.1.1.53; EC 1.1.1.62; EC 1.3.1.20; EC 1.1.1.357 from Homo sapiens (Human) (see 7 papers)
40% identity, 91% coverage: 6:289/312 of query aligns to 2:301/323 of P52895
- GFGTY 20:24 (≠ GFGTL 25:29) binding
- Y24 (≠ L29) mutation to A: Strongly decreases affinity for androstenedione. Decreases androstenedione reductase activity about 60-fold.
- K31 (vs. gap) mutation K->A,M: Increases the low androstenedione reductase activity.
- F46 (≠ Y48) to Y: in dbSNP:rs2854482
- D50 (= D52) binding
- I79 (= I81) to V: in SRXY8; partially impaired activity; dbSNP:rs387906750
- H90 (= H92) to Q: in SRXY8; partially impaired activity; dbSNP:rs797044460
- SN 166:167 (≠ SD 169:170) binding
- Q190 (= Q191) binding
- 216:222 (vs. 217:223, 29% identical) binding
- H222 (≠ G223) to Q: in SRXY8; partially impaired activity; dbSNP:rs13222
- 270:280 (vs. 263:273, 27% identical) binding
- N300 (= N288) to T: in SRXY8; partially impaired activity; dbSNP:rs387906751
- R301 (= R289) mutation to A: Decreases 3-alpha-hydroxysteroid reductase activity about 50-fold.
Sites not aligning to the query:
- 304 R→A: Decreases 3-alpha-hydroxysteroid reductase activity about 500-fold.
4zfcB Crystal structure of akr1c3 complexed with glicazide (see paper)
39% identity, 97% coverage: 6:307/312 of query aligns to 2:317/320 of 4zfcB
- active site: D50 (= D52), Y55 (= Y57), K84 (= K86), H117 (= H119)
- binding N-[(3aR,6aS)-hexahydrocyclopenta[c]pyrrol-2(1H)-ylcarbamoyl]-4-methylbenzenesulfonamide: Y24 (≠ L29), L54 (≠ R56), Y55 (= Y57), W86 (= W88), H117 (= H119), W227 (vs. gap), F306 (= F296)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G22 (= G27), Y24 (≠ L29), D50 (= D52), Y55 (= Y57), H117 (= H119), N167 (≠ D170), Q190 (= Q191), Y216 (≠ F217), S217 (≠ A218), L219 (= L220), S221 (≠ H222), Q222 (≠ G223), A253 (= A246), L268 (= L261), K270 (≠ T263), S271 (≠ P264), R276 (= R269), Q279 (≠ E272), N280 (= N273)
4xo7A Crystal structure of human 3-alpha hydroxysteroid dehydrogenase type 3 in complex with NADP+, 5alpha-androstan-3,17-dione and (3beta, 5alpha)-3-hydroxyandrostan-17-one (see paper)
40% identity, 91% coverage: 6:289/312 of query aligns to 1:300/322 of 4xo7A
- active site: D49 (= D52), Y54 (= Y57), K83 (= K86), H116 (= H119)
- binding 4-androstene-3-17-dione: Y23 (≠ L29), V127 (≠ Q130), I128 (≠ D131), H221 (≠ G223), W226 (vs. gap)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G21 (= G27), T22 (= T28), Y23 (≠ L29), D49 (= D52), Y54 (= Y57), H116 (= H119), S165 (= S169), N166 (≠ D170), Q189 (= Q191), Y215 (≠ F217), S216 (≠ A218), L218 (= L220), S220 (≠ H222), H221 (≠ G223), A252 (= A246), L267 (= L261), K269 (≠ T263), S270 (≠ P264), R275 (= R269), Q278 (≠ E272), N279 (= N273)
2hdjA Crystal structure of human type 3 3alpha-hydroxysteroid dehydrogenase in complex with NADP(h) (see paper)
40% identity, 91% coverage: 6:289/312 of query aligns to 1:300/322 of 2hdjA
- active site: D49 (= D52), Y54 (= Y57), K83 (= K86), H116 (= H119)
- binding nadph dihydro-nicotinamide-adenine-dinucleotide phosphate: G21 (= G27), T22 (= T28), Y23 (≠ L29), D49 (= D52), Y54 (= Y57), H116 (= H119), Q189 (= Q191), Y215 (≠ F217), S216 (≠ A218), L218 (= L220), S220 (≠ H222), H221 (≠ G223), L235 (= L229), A252 (= A246), K269 (≠ T263), S270 (≠ P264), R275 (= R269), Q278 (≠ E272), N279 (= N273)
7x3lA Crystal structure of aldo-keto reductase 1c3 complexed with compound s07044 (see paper)
39% identity, 97% coverage: 6:307/312 of query aligns to 1:316/319 of 7x3lA
- binding (2~{R})-2-[4-(3-fluoranyl-4-methyl-phenyl)-3-(trifluoromethyl)phenyl]butanoic acid: Y23 (≠ L29), Y54 (= Y57), W85 (= W88), H116 (= H119), M119 (≠ F122), N166 (≠ D170), W226 (vs. gap), F305 (= F296), F310 (≠ K301)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G21 (= G27), T22 (= T28), Y23 (≠ L29), D49 (= D52), Y54 (= Y57), H116 (= H119), N166 (≠ D170), Q189 (= Q191), Y215 (≠ F217), S216 (≠ A218), L218 (= L220), S220 (≠ H222), Q221 (≠ G223), A252 (= A246), K269 (≠ T263), S270 (≠ P264), R275 (= R269), Q278 (≠ E272), N279 (= N273)
1j96A Human 3alpha-hsd type 3 in ternary complex with NADP and testosterone (see paper)
40% identity, 91% coverage: 6:289/312 of query aligns to 2:301/323 of 1j96A
- active site: D50 (= D52), Y55 (= Y57), K84 (= K86), H117 (= H119)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G22 (= G27), T23 (= T28), Y24 (≠ L29), D50 (= D52), Y55 (= Y57), Q190 (= Q191), Y216 (≠ F217), S217 (≠ A218), L219 (= L220), S221 (≠ H222), H222 (≠ G223), A253 (= A246), K270 (≠ T263), S271 (≠ P264), R276 (= R269), Q279 (≠ E272), N280 (= N273)
- binding testosterone: Y24 (≠ L29), V128 (≠ Q130), I129 (≠ D131), W227 (vs. gap)
Sites not aligning to the query:
4xo6B Crystal structure of human 3-alpha hydroxysteroid dehydrogenase type 3 in complex with NADP+, 5alpha-androstan-3,17-dione and (3beta, 5alpha)-3-hydroxyandrostan-17-one (see paper)
40% identity, 91% coverage: 6:289/312 of query aligns to 4:303/325 of 4xo6B
- active site: D52 (= D52), Y57 (= Y57), K86 (= K86), H119 (= H119)
- binding (3Beta,5alpha)-3-Hydroxyandrostan-17-one: Y26 (≠ L29), V56 (≠ R56), I131 (≠ D131), H224 (≠ G223)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G24 (= G27), T25 (= T28), Y26 (≠ L29), D52 (= D52), Y57 (= Y57), H119 (= H119), Q192 (= Q191), Y218 (≠ F217), S219 (≠ A218), L221 (= L220), S223 (≠ H222), H224 (≠ G223), A255 (= A246), L270 (= L261), K272 (≠ T263), S273 (≠ P264), R278 (= R269), Q281 (≠ E272), N282 (= N273)
4xo6A Crystal structure of human 3-alpha hydroxysteroid dehydrogenase type 3 in complex with NADP+, 5alpha-androstan-3,17-dione and (3beta, 5alpha)-3-hydroxyandrostan-17-one (see paper)
40% identity, 91% coverage: 6:289/312 of query aligns to 4:303/325 of 4xo6A
- active site: D52 (= D52), Y57 (= Y57), K86 (= K86), H119 (= H119)
- binding 5alpha-androstan-3,17-dione: Y26 (≠ L29), W88 (= W88), I131 (≠ D131)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G24 (= G27), T25 (= T28), Y26 (≠ L29), D52 (= D52), Y57 (= Y57), H119 (= H119), Q192 (= Q191), Y218 (≠ F217), S219 (≠ A218), L221 (= L220), S223 (≠ H222), H224 (≠ G223), A255 (= A246), L270 (= L261), K272 (≠ T263), S273 (≠ P264), R278 (= R269), Q281 (≠ E272), N282 (= N273)
4l1wA Crystal structuer of human 3-alpha hydroxysteroid dehydrogenase type 3 in complex with NADP+ and progesterone (see paper)
40% identity, 91% coverage: 6:289/312 of query aligns to 4:303/325 of 4l1wA
- active site: D52 (= D52), Y57 (= Y57), K86 (= K86), H119 (= H119)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G24 (= G27), T25 (= T28), Y26 (≠ L29), D52 (= D52), Y57 (= Y57), H119 (= H119), Q192 (= Q191), Y218 (≠ F217), S219 (≠ A218), L221 (= L220), S223 (≠ H222), H224 (≠ G223), A255 (= A246), L270 (= L261), K272 (≠ T263), S273 (≠ P264), R278 (= R269), Q281 (≠ E272), N282 (= N273)
- binding progesterone: Y26 (≠ L29), V130 (≠ Q130), I131 (≠ D131), W229 (vs. gap)
Sites not aligning to the query:
1xjbA Crystal structure of human type 3 3alpha-hydroxysteroid dehydrogenase in complex with NADP(h), citrate and acetate molecules (see paper)
40% identity, 91% coverage: 6:289/312 of query aligns to 4:303/325 of 1xjbA
- active site: D52 (= D52), Y57 (= Y57), K86 (= K86), H119 (= H119)
- binding acetate ion: P19 (= P22), L21 (≠ I24), Y57 (= Y57), H119 (= H119), F286 (vs. gap)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G24 (= G27), T25 (= T28), Y26 (≠ L29), D52 (= D52), Y57 (= Y57), H119 (= H119), N169 (≠ D170), Q192 (= Q191), Y218 (≠ F217), S219 (≠ A218), L221 (= L220), S223 (≠ H222), H224 (≠ G223), L238 (= L229), A255 (= A246), L270 (= L261), A271 (≠ T262), K272 (≠ T263), S273 (≠ P264), R278 (= R269), Q281 (≠ E272), N282 (= N273)
8i0cA Crystal structure of aldo-keto reductase 1c3 complexed with compound s0703 (see paper)
39% identity, 93% coverage: 18:307/312 of query aligns to 9:313/316 of 8i0cA
- binding 1-[4-[3,5-bis(chloranyl)phenyl]-3-fluoranyl-phenyl]cyclopropane-1-carboxylic acid: Y20 (≠ L29), Y51 (= Y57), M116 (≠ F122), N163 (≠ D170), F302 (= F296)
- binding nadp nicotinamide-adenine-dinucleotide phosphate: G18 (= G27), D46 (= D52), Y51 (= Y57), H113 (= H119), Q186 (= Q191), Y212 (≠ F217), S213 (≠ A218), L215 (= L220), S217 (≠ H222), Q218 (≠ G223), A249 (= A246), K266 (≠ T263), S267 (≠ P264), R272 (= R269), Q275 (≠ E272), N276 (= N273)
Sites not aligning to the query:
Query Sequence
>H281DRAFT_00358 FitnessBrowser__Burk376:H281DRAFT_00358
MIEPCDFRLKRIALNHGGGSMPAIGFGTLIADAAITISATKDALEAGYRHFDCAERYRNE
REVGDALQAGLAAGGIAREDIFVTTKLWNSNHRPERVKPAFDASLERLRLDYLDLYLIHT
PFAFQAGDEQDPRDANGNVLYDEGVTLLDTWRAMEDLVDGGRCRAIGLSDIGLDDLVPLY
ESARIKPAVVQVEAHPYLPESELLEFCKKKEIVFLAFAPLGHGIRPGPLEDPVVSRIAAR
IGKTPAQVLLAWAVQRGTAVLTTPKTAARARENFDISALPADAFDEINRIETRQRFNQVV
KTGNPGFIPRIE
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