SitesBLAST
Comparing 8499450 FitnessBrowser__Miya:8499450 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)
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
38% identity, 97% coverage: 7:465/473 of query aligns to 2:444/452 of 2eq7A
- active site: P11 (= P16), L36 (= L40), C40 (= C44), C45 (= C49), S48 (≠ T52), G72 (vs. gap), V73 (≠ I78), V177 (≠ A195), E181 (= E199), S314 (≠ D331), H432 (≠ F453), H434 (= H455), E439 (= E460)
- binding flavin-adenine dinucleotide: G10 (= G15), P11 (= P16), G12 (= G17), E31 (≠ D36), K32 (≠ R37), G38 (= G42), T39 (= T43), C40 (= C44), R42 (≠ N46), G44 (= G48), C45 (= C49), K49 (= K53), T110 (≠ E115), A111 (≠ G116), T137 (= T155), G138 (= G156), S157 (= S175), I178 (= I196), R262 (= R280), Y265 (≠ A283), D302 (= D319), M308 (≠ L325), L309 (= L326), A310 (= A327), H311 (= H328), Y341 (= Y359)
- binding nicotinamide-adenine-dinucleotide: W146 (≠ G164), G174 (= G192), G176 (= G194), V177 (≠ A195), I178 (= I196), E197 (= E215), Y198 (≠ G216), V231 (= V249), V260 (= V278), G261 (= G279), R262 (= R280), M308 (≠ L325), L309 (= L326), V339 (≠ C357)
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
38% identity, 97% coverage: 7:465/473 of query aligns to 2:444/455 of 2yquB
- active site: P11 (= P16), L36 (= L40), C40 (= C44), C45 (= C49), S48 (≠ T52), G72 (vs. gap), V73 (≠ I78), V177 (≠ A195), E181 (= E199), S314 (≠ D331), H432 (≠ F453), H434 (= H455), E439 (= E460)
- binding carbonate ion: A310 (= A327), S314 (≠ D331), S423 (≠ T444), D426 (= D447)
- binding flavin-adenine dinucleotide: G8 (= G13), G10 (= G15), P11 (= P16), G12 (= G17), E31 (≠ D36), K32 (≠ R37), G38 (= G42), T39 (= T43), C40 (= C44), R42 (≠ N46), G44 (= G48), C45 (= C49), K49 (= K53), T110 (≠ E115), A111 (≠ G116), T137 (= T155), G138 (= G156), I178 (= I196), Y265 (≠ A283), G301 (= G318), D302 (= D319), M308 (≠ L325), L309 (= L326), A310 (= A327), H311 (= H328)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
38% identity, 97% coverage: 7:465/473 of query aligns to 2:444/455 of 2yquA
- active site: P11 (= P16), L36 (= L40), C40 (= C44), C45 (= C49), S48 (≠ T52), G72 (vs. gap), V73 (≠ I78), V177 (≠ A195), E181 (= E199), S314 (≠ D331), H432 (≠ F453), H434 (= H455), E439 (= E460)
- binding flavin-adenine dinucleotide: G8 (= G13), G10 (= G15), P11 (= P16), G12 (= G17), E31 (≠ D36), K32 (≠ R37), G38 (= G42), T39 (= T43), C40 (= C44), R42 (≠ N46), G44 (= G48), C45 (= C49), K49 (= K53), T110 (≠ E115), A111 (≠ G116), T137 (= T155), G138 (= G156), S157 (= S175), I178 (= I196), Y265 (≠ A283), G301 (= G318), D302 (= D319), M308 (≠ L325), L309 (= L326), A310 (= A327)
3ladA Refined crystal structure of lipoamide dehydrogenase from azotobacter vinelandii at 2.2 angstroms resolution. A comparison with the structure of glutathione reductase (see paper)
33% identity, 98% coverage: 4:465/473 of query aligns to 1:460/472 of 3ladA
- active site: L44 (= L40), C48 (= C44), C53 (= C49), S56 (≠ T52), V190 (≠ A195), E194 (= E199), F448 (= F453), H450 (= H455), E455 (= E460)
- binding flavin-adenine dinucleotide: I9 (≠ L12), G10 (= G13), G12 (= G15), P13 (= P16), E33 (≠ D36), K34 (≠ R37), G46 (= G42), T47 (= T43), C48 (= C44), G52 (= G48), C53 (= C49), H120 (≠ E115), G121 (= G116), A149 (= A154), S150 (≠ T155), G151 (= G156), I191 (= I196), R278 (= R280), D318 (= D319), L325 (= L326), A326 (= A327)
P18925 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Azotobacter vinelandii (see 2 papers)
33% identity, 98% coverage: 4:465/473 of query aligns to 2:461/477 of P18925
- 34:49 (vs. 36:44, 31% identical) binding
- C49 (= C44) modified: Disulfide link with 54, Redox-active
- C54 (= C49) modified: Disulfide link with 49, Redox-active
- K58 (= K53) binding
- D319 (= D319) binding
- A327 (= A327) binding
P09624 Dihydrolipoyl dehydrogenase, mitochondrial; DLD; 2-oxoglutarate dehydrogenase complex component E3; OGDC-E3; OGDHC subunit E3; Alpha-ketoglutarate dehydrogenase complex subunit E3; alpha-KGDHC subunit E3; Dihydrolipoamide dehydrogenase; Dihydrolipoamide:NAD(+) oxidoreductase; Glycine decarboxylase complex subunit L; GDC subunit L; Lipoamide dehydrogenase component of pyruvate dehydrogenase complex; Pyruvate dehydrogenase complex E3 component; PDC subunit E3; PDH complex subunit E3; EC 1.8.1.4 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
34% identity, 98% coverage: 1:465/473 of query aligns to 21:488/499 of P09624
- 56:65 (vs. 36:44, 60% identical) binding
- C65 (= C44) modified: Disulfide link with 70, Redox-active
- C70 (= C49) modified: Disulfide link with 65, Redox-active
- K74 (= K53) binding
- G139 (= G116) binding
- D346 (= D319) binding
- MLAH 352:355 (≠ LLAH 325:328) binding
- H478 (= H455) active site, Proton acceptor
Sites not aligning to the query:
- 1:21 modified: transit peptide, Mitochondrion
1v59A Crystal structure of yeast lipoamide dehydrogenase complexed with NAD+
34% identity, 98% coverage: 2:465/473 of query aligns to 1:467/478 of 1v59A
- active site: L40 (= L40), C44 (= C44), C49 (= C49), S52 (≠ T52), I193 (≠ A195), E197 (= E199), T349 (≠ C342), H455 (≠ F453), H457 (= H455), E462 (= E460)
- binding flavin-adenine dinucleotide: G14 (= G15), P15 (= P16), A16 (≠ G17), E35 (≠ D36), K36 (≠ R37), R37 (≠ D38), G42 (= G42), T43 (= T43), C44 (= C44), G48 (= G48), C49 (= C49), K53 (= K53), N117 (≠ E115), G118 (= G116), T153 (= T155), G154 (= G156), R285 (= R280), Y288 (≠ A283), G324 (= G318), D325 (= D319), M331 (≠ L325), L332 (= L326), A333 (= A327), H334 (= H328), Y364 (= Y359)
- binding nicotinamide-adenine-dinucleotide: I189 (≠ V191), G190 (= G192), E213 (= E215), F214 (≠ G216), K246 (= K248), V283 (= V278)
1jehA Crystal structure of yeast e3, lipoamide dehydrogenase (see paper)
34% identity, 98% coverage: 2:465/473 of query aligns to 1:467/478 of 1jehA
- active site: L40 (= L40), C44 (= C44), C49 (= C49), S52 (≠ T52), I193 (≠ A195), E197 (= E199), T349 (≠ C342), H455 (≠ F453), H457 (= H455), E462 (= E460)
- binding flavin-adenine dinucleotide: I11 (≠ L12), G14 (= G15), P15 (= P16), A16 (≠ G17), V34 (= V35), E35 (≠ D36), K36 (≠ R37), R37 (≠ D38), G42 (= G42), T43 (= T43), C44 (= C44), G48 (= G48), C49 (= C49), K53 (= K53), G118 (= G116), T153 (= T155), G154 (= G156), I194 (= I196), R285 (= R280), Y288 (≠ A283), L292 (≠ I287), G324 (= G318), D325 (= D319), M331 (≠ L325), L332 (= L326), A333 (= A327), H334 (= H328)
P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 from Pseudomonas fluorescens (see 2 papers)
31% identity, 98% coverage: 4:465/473 of query aligns to 2:461/478 of P14218
- 34:49 (vs. 36:44, 31% identical) binding
- C49 (= C44) modified: Disulfide link with 54, Redox-active
- C54 (= C49) modified: Disulfide link with 49, Redox-active
- K58 (= K53) binding
- G122 (= G116) binding
- D319 (= D319) binding
- A327 (= A327) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
31% identity, 98% coverage: 4:465/473 of query aligns to 1:460/473 of 5u8wA
- active site: P13 (= P16), L44 (= L40), C48 (= C44), C53 (= C49), S56 (≠ T52), G82 (vs. gap), V83 (≠ I78), V190 (≠ A195), E194 (= E199), S330 (≠ D331), F448 (= F453), H450 (= H455), E455 (= E460)
- binding flavin-adenine dinucleotide: I9 (≠ L12), G12 (= G15), P13 (= P16), G14 (= G17), E33 (≠ D36), K34 (≠ R37), G46 (= G42), T47 (= T43), C48 (= C44), G52 (= G48), C53 (= C49), K57 (= K53), H120 (≠ E115), G121 (= G116), A149 (= A154), S150 (≠ T155), G151 (= G156), S170 (= S175), G317 (= G318), D318 (= D319), M324 (≠ L325), L325 (= L326), A326 (= A327), H327 (= H328), Y357 (= Y359), H450 (= H455), P451 (= P456)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (≠ V191), G189 (= G194), V190 (≠ A195), I191 (= I196), E194 (= E199), E210 (= E215), A211 (≠ G216), L212 (≠ M217), A275 (= A277), V276 (= V278), G277 (= G279), R278 (= R280), M324 (≠ L325), L325 (= L326), V355 (≠ C357), Y357 (= Y359)
Sites not aligning to the query:
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
31% identity, 98% coverage: 4:465/473 of query aligns to 4:463/477 of 5u8uD
- active site: P16 (= P16), L47 (= L40), C51 (= C44), C56 (= C49), S59 (≠ T52), G85 (vs. gap), V86 (≠ I78), V193 (≠ A195), E197 (= E199), S333 (≠ D331), F451 (= F453), H453 (= H455), E458 (= E460)
- binding flavin-adenine dinucleotide: I12 (≠ L12), G15 (= G15), P16 (= P16), G17 (= G17), E36 (≠ D36), K37 (≠ R37), G49 (= G42), T50 (= T43), C51 (= C44), G55 (= G48), C56 (= C49), K60 (= K53), H123 (≠ E115), G124 (= G116), A152 (= A154), S153 (≠ T155), G154 (= G156), I194 (= I196), R281 (= R280), G320 (= G318), D321 (= D319), M327 (≠ L325), L328 (= L326), A329 (= A327), H330 (= H328), H453 (= H455), P454 (= P456)
Sites not aligning to the query:
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
31% identity, 97% coverage: 6:465/473 of query aligns to 2:459/472 of 5u8vA
- active site: P12 (= P16), L43 (= L40), C47 (= C44), C52 (= C49), S55 (≠ T52), G81 (vs. gap), V82 (≠ I78), V189 (≠ A195), E193 (= E199), S329 (≠ D331), F447 (= F453), H449 (= H455), E454 (= E460)
- binding flavin-adenine dinucleotide: I8 (≠ L12), G11 (= G15), P12 (= P16), G13 (= G17), E32 (≠ D36), G45 (= G42), T46 (= T43), C47 (= C44), G51 (= G48), C52 (= C49), K56 (= K53), H119 (≠ E115), G120 (= G116), A148 (= A154), S149 (≠ T155), G150 (= G156), S169 (= S175), I190 (= I196), R277 (= R280), G316 (= G318), D317 (= D319), M323 (≠ L325), L324 (= L326), A325 (= A327), H326 (= H328), H449 (= H455), P450 (= P456)
- binding nicotinamide-adenine-dinucleotide: I185 (≠ V191), G186 (= G192), G188 (= G194), V189 (≠ A195), I190 (= I196), L208 (≠ V214), E209 (= E215), A210 (≠ G216), V243 (= V249), V275 (= V278), G276 (= G279)
Sites not aligning to the query:
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
33% identity, 97% coverage: 7:465/473 of query aligns to 1:455/465 of 3urhB
- active site: Y35 (≠ L40), C39 (= C44), C44 (= C49), S47 (≠ T52), V183 (≠ A195), E187 (= E199), H443 (= H446), H445 (= H455), E450 (= E460)
- binding flavin-adenine dinucleotide: I6 (≠ L12), G7 (= G13), G9 (= G15), P10 (= P16), G11 (= G17), E30 (≠ D36), K31 (vs. gap), G37 (= G42), T38 (= T43), C39 (= C44), G43 (= G48), C44 (= C49), K48 (= K53), T111 (≠ E115), G112 (= G116), A140 (= A154), T141 (= T155), G142 (= G156), I184 (= I196), R273 (= R280), G312 (= G318), D313 (= D319), M319 (≠ L325), L320 (= L326), A321 (= A327), H322 (= H328)
6awaA 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from pseudomonas putida in complex with fad and adenosine-5'-monophosphate.
31% identity, 98% coverage: 4:465/473 of query aligns to 2:461/475 of 6awaA
- active site: L45 (= L40), C49 (= C44), C54 (= C49), S57 (≠ T52), V191 (≠ A195), E195 (= E199), F449 (= F453), H451 (= H455), E456 (= E460)
- binding adenosine monophosphate: I187 (≠ V191), E211 (= E215), A212 (≠ G216), L213 (≠ M217), V245 (= V249), V277 (= V278)
- binding flavin-adenine dinucleotide: I10 (≠ L12), G13 (= G15), P14 (= P16), G15 (= G17), E34 (≠ D36), K35 (≠ R37), T48 (= T43), C49 (= C44), G53 (= G48), C54 (= C49), K58 (= K53), H121 (≠ E115), G122 (= G116), S151 (≠ T155), G152 (= G156), I192 (= I196), R279 (= R280), G318 (= G318), D319 (= D319), M325 (≠ L325), L326 (= L326), A327 (= A327), Y358 (= Y359)
Sites not aligning to the query:
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
30% identity, 97% coverage: 8:465/473 of query aligns to 6:460/472 of 1zmdA
- active site: L39 (= L40), C43 (= C44), C48 (= C49), S51 (≠ T52), V186 (≠ A195), E190 (= E199), H448 (≠ F453), H450 (= H455), E455 (= E460)
- binding flavin-adenine dinucleotide: I10 (≠ L12), G11 (= G13), G13 (= G15), P14 (= P16), G15 (= G17), E34 (≠ D36), K35 (≠ R37), N36 (≠ D38), G41 (= G42), T42 (= T43), C43 (= C44), G47 (= G48), C48 (= C49), K52 (= K53), Y116 (≠ E115), G117 (= G116), T146 (= T155), G147 (= G156), S166 (= S175), R278 (= R280), F281 (≠ A283), G317 (= G318), D318 (= D319), M324 (≠ L325), L325 (= L326), A326 (= A327), H327 (= H328)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (≠ V191), G183 (= G192), G185 (= G194), V186 (≠ A195), I187 (= I196), E190 (= E199), E206 (= E215), F207 (≠ G216), L208 (≠ M217), I276 (≠ V278), G277 (= G279), R278 (= R280), M324 (≠ L325), L325 (= L326), V355 (≠ C357), Y357 (= Y359)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
30% identity, 97% coverage: 8:465/473 of query aligns to 6:460/472 of 1zmcA
- active site: L39 (= L40), C43 (= C44), C48 (= C49), S51 (≠ T52), V186 (≠ A195), E190 (= E199), H448 (≠ F453), H450 (= H455), E455 (= E460)
- binding flavin-adenine dinucleotide: I10 (≠ L12), G11 (= G13), G13 (= G15), P14 (= P16), G15 (= G17), E34 (≠ D36), K35 (≠ R37), N36 (≠ D38), G41 (= G42), T42 (= T43), C43 (= C44), G47 (= G48), C48 (= C49), K52 (= K53), Y116 (≠ E115), G117 (= G116), T146 (= T155), G147 (= G156), S166 (= S175), I187 (= I196), F281 (≠ A283), G317 (= G318), D318 (= D319), M324 (≠ L325), L325 (= L326), A326 (= A327), H327 (= H328)
- binding nicotinamide-adenine-dinucleotide: G183 (= G192), G185 (= G194), V205 (= V214), E206 (= E215), F207 (≠ G216), L208 (≠ M217), K240 (= K248), V241 (= V249), I276 (≠ V278), G277 (= G279), R278 (= R280), R297 (≠ P299), M324 (≠ L325)
P09622 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; EC 1.8.1.4 from Homo sapiens (Human) (see 14 papers)
30% identity, 97% coverage: 8:465/473 of query aligns to 43:497/509 of P09622
- 71:80 (vs. 36:44, 50% identical) binding
- K72 (≠ R37) to E: in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX; dbSNP:rs121964987
- K89 (= K53) binding ; mutation to E: Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- K104 (≠ Q68) to T: in dbSNP:rs1130477
- G154 (= G116) binding
- TGS 183:185 (= TGS 155:157) binding
- 220:227 (vs. 192:199, 63% identical) binding
- E243 (= E215) binding
- V278 (= V249) binding
- G314 (= G279) binding
- D355 (= D319) binding
- MLAH 361:364 (≠ LLAH 325:328) binding
- E375 (≠ R339) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (≠ P348) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (vs. gap) Important for interaction with PDHX and activity of multienzyme pyruvate dehydrogenase complex; mutation to A: Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity.; mutation to N: Does not affect dihydrolipoyl dehydrogenase activity.
- E466 (≠ L429) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ T441) Important for interaction with PDHX and activity of multienzyme pyruvate dehydrogenase complex; mutation to A: Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity.; mutation to F: Does not affect dihydrolipoyl dehydrogenase activity.; mutation to H: Reduces interaction with PDHX. Inhibits multienzyme pyruvate dehydrogenase complex activity. Does not affect dihydrolipoyl dehydrogenase activity.
- D479 (= D447) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (≠ N450) to G: in DLDD; reduced enzyme activity; dbSNP:rs397514650; mutation to A: Does not affect dihydrolipoyl dehydrogenase activity.; mutation to M: Does not affect interaction with PDHX.
- H485 (≠ F453) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
- P488 (= P456) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
- S491 (≠ D459) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
- E492 (= E460) mutation to Q: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- R495 (≠ E463) to G: in DLDD; loss of enzyme activity; reduced interaction with PDHX; dbSNP:rs121964989
Sites not aligning to the query:
- 505 K→M: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
6hg8B Crystal structure of the r460g disease-causing mutant of the human dihydrolipoamide dehydrogenase.
30% identity, 96% coverage: 8:462/473 of query aligns to 16:467/482 of 6hg8B
- active site: C53 (= C44), C58 (= C49), S61 (≠ T52), V196 (≠ A195), E200 (= E199), H460 (= H455), E465 (= E460)
- binding flavin-adenine dinucleotide: I20 (≠ L12), G23 (= G15), P24 (= P16), G25 (= G17), E44 (≠ D36), K45 (≠ R37), N46 (≠ D38), G51 (= G42), T52 (= T43), C53 (= C44), G57 (= G48), C58 (= C49), K62 (= K53), Y126 (≠ E115), G127 (= G116), T156 (= T155), G157 (= G156), I197 (= I196), R288 (= R280), F291 (≠ A283), G327 (= G318), D328 (= D319), M334 (≠ L325), L335 (= L326), A336 (= A327), H337 (= H328)
2qaeA Crystal structure analysis of trypanosoma cruzi lipoamide dehydrogenase
35% identity, 95% coverage: 21:468/473 of query aligns to 17:457/465 of 2qaeA
- active site: L37 (= L40), C41 (= C44), C46 (= C49), S49 (≠ T52), V184 (≠ A195), E188 (= E199), H442 (≠ F453), H444 (= H455), E449 (= E460)
- binding flavin-adenine dinucleotide: E32 (≠ D36), K33 (≠ R37), R34 (≠ D38), G39 (= G42), T40 (= T43), C41 (= C44), G45 (= G48), C46 (= C49), K50 (= K53), E114 (= E115), G115 (= G116), T144 (= T155), G145 (= G156), S164 (= S175), I185 (= I196), F274 (≠ A283), G310 (= G318), D311 (= D319), M318 (≠ L325), L319 (= L326), A320 (= A327), H321 (= H328)
Sites not aligning to the query:
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
31% identity, 97% coverage: 8:465/473 of query aligns to 5:451/455 of 1ebdA
- active site: P13 (= P16), L37 (= L40), C41 (= C44), C46 (= C49), S49 (≠ T52), N74 (≠ H77), V75 (≠ I78), Y180 (≠ A195), E184 (= E199), S320 (≠ D331), H438 (≠ F453), H440 (= H455), E445 (= E460)
- binding flavin-adenine dinucleotide: G10 (= G13), G12 (= G15), P13 (= P16), V32 (= V35), E33 (≠ D36), K34 (≠ R37), G39 (= G42), V40 (≠ T43), C41 (= C44), G45 (= G48), C46 (= C49), K50 (= K53), E112 (= E115), A113 (≠ G116), T141 (= T155), G142 (= G156), Y180 (≠ A195), I181 (= I196), R268 (= R280), D308 (= D319), A314 (≠ L325), L315 (= L326), A316 (= A327)
Query Sequence
>8499450 FitnessBrowser__Miya:8499450
MTPSTRYDMIILGGGPGGSRAAFDAAARGLSVALVDRDGLGGTCLNRGCIPTKLLLGATA
ALPLLETQKKLKGADGHIAFDLPALQQRKDRYVKGTRQALEKRLKAAGIAVYAGEGRVTG
ERQGDADGELAVVAAQADGTTQETRLGWGTLIVATGSTPASFPGLAADGAAVLDSTALLD
VTEAPESLIVVGGGAIGLEMADFFSRFGTRITIVEGMGRLAPTEDAEVGDTLRKVYAREG
WTIHNGRKVASLATVDGHAVLRFEDGEELTASKALLAVGRRPASVGIGLEALGTTLRGPG
WMQTDEWLRAAPHVYAIGDVNGRTLLAHAADHQARYAVRHACGDTAAPYDAGVMPACIYG
HLEAMRVGPTAEELKNAGFSPRVSRSMLIANPIAQAYGTTQGFIKIVWVDGRIRGVTAVG
HGVSHLVTLAAVLAGGSGTATGWTAHDAGNVIFAHPTLDEALEAAIEAPQELA
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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