SitesBLAST
Comparing WP_011318723.1 NCBI__GCF_000204075.1:WP_011318723.1 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)
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
37% identity, 98% coverage: 6:469/475 of query aligns to 4:460/472 of 1zmdA
- active site: L39 (≠ M40), C43 (= C44), C48 (= C49), S51 (= S52), V186 (≠ Y187), E190 (= E191), H448 (= H457), H450 (= H459), E455 (= E464)
- binding flavin-adenine dinucleotide: I10 (= I12), G11 (= G13), G13 (= G15), P14 (≠ V16), G15 (= G17), E34 (= E36), K35 (≠ A37), N36 (≠ G38), G41 (= G42), T42 (= T43), C43 (= C44), G47 (= G48), C48 (= C49), K52 (= K53), Y116 (≠ W118), G117 (= G119), T146 (≠ P147), G147 (= G148), S166 (= S167), R278 (= R278), F281 (≠ A281), G317 (= G322), D318 (= D323), M324 (= M329), L325 (= L330), A326 (= A331), H327 (= H332)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (= I183), G183 (= G184), G185 (= G186), V186 (≠ Y187), I187 (= I188), E190 (= E191), E206 (= E207), F207 (≠ A208), L208 (= L209), I276 (≠ T276), G277 (= G277), R278 (= R278), M324 (= M329), L325 (= L330), V355 (≠ A360), Y357 (≠ F362)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
37% identity, 98% coverage: 6:469/475 of query aligns to 4:460/472 of 1zmcA
- active site: L39 (≠ M40), C43 (= C44), C48 (= C49), S51 (= S52), V186 (≠ Y187), E190 (= E191), H448 (= H457), H450 (= H459), E455 (= E464)
- binding flavin-adenine dinucleotide: I10 (= I12), G11 (= G13), G13 (= G15), P14 (≠ V16), G15 (= G17), E34 (= E36), K35 (≠ A37), N36 (≠ G38), G41 (= G42), T42 (= T43), C43 (= C44), G47 (= G48), C48 (= C49), K52 (= K53), Y116 (≠ W118), G117 (= G119), T146 (≠ P147), G147 (= G148), S166 (= S167), I187 (= I188), F281 (≠ A281), G317 (= G322), D318 (= D323), M324 (= M329), L325 (= L330), A326 (= A331), H327 (= H332)
- binding nicotinamide-adenine-dinucleotide: G183 (= G184), G185 (= G186), V205 (≠ I206), E206 (= E207), F207 (≠ A208), L208 (= L209), K240 (= K237), V241 (= V238), I276 (≠ T276), G277 (= G277), R278 (= R278), R297 (= R297), M324 (= M329)
P09622 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; EC 1.8.1.4 from Homo sapiens (Human) (see 14 papers)
37% identity, 98% coverage: 6:469/475 of query aligns to 41:497/509 of P09622
- 71:80 (vs. 36:44, 50% identical) binding FAD
- K72 (≠ A37) to E: in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX; dbSNP:rs121964987
- K89 (= K53) binding FAD; mutation to E: Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- K104 (≠ H69) to T: in dbSNP:rs1130477
- G154 (= G119) binding FAD
- TGS 183:185 (≠ PGS 147:149) binding FAD
- 220:227 (vs. 184:191, 63% identical) binding NAD(+)
- E243 (= E207) binding NAD(+)
- V278 (= V238) binding NAD(+)
- G314 (= G277) binding NAD(+)
- D355 (= D323) binding FAD
- MLAH 361:364 (= MLAH 329:332) binding FAD
- E375 (= E343) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (≠ T351) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (≠ G420) 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 (= E438) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ N445) 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 (≠ T451) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (≠ H454) 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 (= H457) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
- P488 (= P460) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
- S491 (= S463) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
- E492 (= E464) mutation to Q: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- R495 (≠ D467) 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.
37% identity, 98% coverage: 6:469/475 of query aligns to 14:470/482 of 6hg8B
- active site: C53 (= C44), C58 (= C49), S61 (= S52), V196 (≠ Y187), E200 (= E191), H460 (= H459), E465 (= E464)
- binding flavin-adenine dinucleotide: I20 (= I12), G23 (= G15), P24 (≠ V16), G25 (= G17), E44 (= E36), K45 (≠ A37), N46 (≠ G38), G51 (= G42), T52 (= T43), C53 (= C44), G57 (= G48), C58 (= C49), K62 (= K53), Y126 (≠ W118), G127 (= G119), T156 (≠ P147), G157 (= G148), I197 (= I188), R288 (= R278), F291 (≠ A281), G327 (= G322), D328 (= D323), M334 (= M329), L335 (= L330), A336 (= A331), H337 (= H332)
6awaA 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from pseudomonas putida in complex with fad and adenosine-5'-monophosphate.
37% identity, 99% coverage: 1:469/475 of query aligns to 1:461/475 of 6awaA
- active site: L45 (≠ M40), C49 (= C44), C54 (= C49), S57 (= S52), V191 (≠ Y187), E195 (= E191), F449 (≠ H457), H451 (= H459), E456 (= E464)
- binding adenosine monophosphate: I187 (= I183), E211 (= E207), A212 (= A208), L213 (= L209), V245 (= V240), V277 (≠ T276)
- binding flavin-adenine dinucleotide: I10 (= I12), G13 (= G15), P14 (≠ V16), G15 (= G17), E34 (= E36), K35 (≠ A37), T48 (= T43), C49 (= C44), G53 (= G48), C54 (= C49), K58 (= K53), H121 (≠ W118), G122 (= G119), S151 (≠ P147), G152 (= G148), I192 (= I188), R279 (= R278), G318 (= G322), D319 (= D323), M325 (= M329), L326 (= L330), A327 (= A331), Y358 (≠ F362)
Sites not aligning to the query:
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
36% identity, 97% coverage: 7:469/475 of query aligns to 2:444/452 of 2eq7A
- active site: P11 (≠ V16), L36 (≠ M40), C40 (= C44), C45 (= C49), S48 (= S52), G72 (≠ N80), V73 (= V81), V177 (≠ Y187), E181 (= E191), S314 (= S335), H432 (= H457), H434 (= H459), E439 (= E464)
- binding flavin-adenine dinucleotide: G10 (= G15), P11 (≠ V16), G12 (= G17), E31 (= E36), K32 (≠ A37), G38 (= G42), T39 (= T43), C40 (= C44), R42 (≠ N46), G44 (= G48), C45 (= C49), K49 (= K53), T110 (≠ W118), A111 (≠ G119), T137 (≠ P147), G138 (= G148), S157 (= S167), I178 (= I188), R262 (= R278), Y265 (≠ A281), D302 (= D323), M308 (= M329), L309 (= L330), A310 (= A331), H311 (= H332), Y341 (≠ F362)
- binding nicotinamide-adenine-dinucleotide: W146 (≠ G156), G174 (= G184), G176 (= G186), V177 (≠ Y187), I178 (= I188), E197 (= E207), Y198 (≠ A208), V231 (≠ A242), V260 (≠ T276), G261 (= G277), R262 (= R278), M308 (= M329), L309 (= L330), V339 (≠ A360)
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
36% identity, 97% coverage: 7:469/475 of query aligns to 2:444/455 of 2yquB
- active site: P11 (≠ V16), L36 (≠ M40), C40 (= C44), C45 (= C49), S48 (= S52), G72 (≠ N80), V73 (= V81), V177 (≠ Y187), E181 (= E191), S314 (= S335), H432 (= H457), H434 (= H459), E439 (= E464)
- binding carbonate ion: A310 (= A331), S314 (= S335), S423 (≠ T448), D426 (≠ T451)
- binding flavin-adenine dinucleotide: G8 (= G13), G10 (= G15), P11 (≠ V16), G12 (= G17), E31 (= E36), K32 (≠ A37), G38 (= G42), T39 (= T43), C40 (= C44), R42 (≠ N46), G44 (= G48), C45 (= C49), K49 (= K53), T110 (≠ W118), A111 (≠ G119), T137 (≠ P147), G138 (= G148), I178 (= I188), Y265 (≠ A281), G301 (= G322), D302 (= D323), M308 (= M329), L309 (= L330), A310 (= A331), H311 (= H332)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
36% identity, 97% coverage: 7:469/475 of query aligns to 2:444/455 of 2yquA
- active site: P11 (≠ V16), L36 (≠ M40), C40 (= C44), C45 (= C49), S48 (= S52), G72 (≠ N80), V73 (= V81), V177 (≠ Y187), E181 (= E191), S314 (= S335), H432 (= H457), H434 (= H459), E439 (= E464)
- binding flavin-adenine dinucleotide: G8 (= G13), G10 (= G15), P11 (≠ V16), G12 (= G17), E31 (= E36), K32 (≠ A37), G38 (= G42), T39 (= T43), C40 (= C44), R42 (≠ N46), G44 (= G48), C45 (= C49), K49 (= K53), T110 (≠ W118), A111 (≠ G119), T137 (≠ P147), G138 (= G148), S157 (= S167), I178 (= I188), Y265 (≠ A281), G301 (= G322), D302 (= D323), M308 (= M329), L309 (= L330), A310 (= A331)
P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 from Pseudomonas fluorescens (see 2 papers)
37% identity, 99% coverage: 1:469/475 of query aligns to 1:461/478 of P14218
- M1 (= M1) modified: Initiator methionine, Removed
- 34:49 (vs. 36:44, 31% identical) binding FAD
- C49 (= C44) modified: Disulfide link with 54, Redox-active
- C54 (= C49) modified: Disulfide link with 49, Redox-active
- K58 (= K53) binding FAD
- G122 (= G119) binding FAD
- D319 (= D323) binding FAD
- A327 (= A331) binding FAD
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
37% identity, 99% coverage: 1:469/475 of query aligns to 3:463/477 of 5u8uD
- active site: P16 (≠ V16), L47 (≠ M40), C51 (= C44), C56 (= C49), S59 (= S52), G85 (≠ N80), V86 (= V81), V193 (≠ Y187), E197 (= E191), S333 (= S335), F451 (≠ H457), H453 (= H459), E458 (= E464)
- binding flavin-adenine dinucleotide: I12 (= I12), G15 (= G15), P16 (≠ V16), G17 (= G17), E36 (= E36), K37 (≠ A37), G49 (= G42), T50 (= T43), C51 (= C44), G55 (= G48), C56 (= C49), K60 (= K53), H123 (≠ W118), G124 (= G119), A152 (≠ S146), S153 (≠ P147), G154 (= G148), I194 (= I188), R281 (= R278), G320 (= G322), D321 (= D323), M327 (= M329), L328 (= L330), A329 (= A331), H330 (= H332), H453 (= H459), P454 (= P460)
Sites not aligning to the query:
P18925 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Azotobacter vinelandii (see 2 papers)
36% identity, 99% coverage: 1:469/475 of query aligns to 1:461/477 of P18925
- 34:49 (vs. 36:44, 31% identical) binding FAD
- C49 (= C44) modified: Disulfide link with 54, Redox-active
- C54 (= C49) modified: Disulfide link with 49, Redox-active
- K58 (= K53) binding FAD
- D319 (= D323) binding FAD
- A327 (= A331) binding FAD
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
37% identity, 97% coverage: 7:469/475 of query aligns to 3:459/472 of 5u8vA
- active site: P12 (≠ V16), L43 (≠ M40), C47 (= C44), C52 (= C49), S55 (= S52), G81 (≠ N80), V82 (= V81), V189 (≠ Y187), E193 (= E191), S329 (= S335), F447 (≠ H457), H449 (= H459), E454 (= E464)
- binding flavin-adenine dinucleotide: I8 (= I12), G11 (= G15), P12 (≠ V16), G13 (= G17), E32 (= E36), G45 (= G42), T46 (= T43), C47 (= C44), G51 (= G48), C52 (= C49), K56 (= K53), H119 (≠ W118), G120 (= G119), A148 (≠ S146), S149 (≠ P147), G150 (= G148), S169 (= S167), I190 (= I188), R277 (= R278), G316 (= G322), D317 (= D323), M323 (= M329), L324 (= L330), A325 (= A331), H326 (= H332), H449 (= H459), P450 (= P460)
- binding nicotinamide-adenine-dinucleotide: I185 (= I183), G186 (= G184), G188 (= G186), V189 (≠ Y187), I190 (= I188), L208 (≠ I206), E209 (= E207), A210 (= A208), V243 (= V240), V275 (≠ T276), G276 (= G277)
Sites not aligning to the query:
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
37% identity, 97% coverage: 7:469/475 of query aligns to 4:460/473 of 5u8wA
- active site: P13 (≠ V16), L44 (≠ M40), C48 (= C44), C53 (= C49), S56 (= S52), G82 (≠ N80), V83 (= V81), V190 (≠ Y187), E194 (= E191), S330 (= S335), F448 (≠ H457), H450 (= H459), E455 (= E464)
- binding flavin-adenine dinucleotide: I9 (= I12), G12 (= G15), P13 (≠ V16), G14 (= G17), E33 (= E36), K34 (≠ A37), G46 (= G42), T47 (= T43), C48 (= C44), G52 (= G48), C53 (= C49), K57 (= K53), H120 (≠ W118), G121 (= G119), A149 (≠ S146), S150 (≠ P147), G151 (= G148), S170 (= S167), G317 (= G322), D318 (= D323), M324 (= M329), L325 (= L330), A326 (= A331), H327 (= H332), Y357 (≠ F362), H450 (= H459), P451 (= P460)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (= I183), G189 (= G186), V190 (≠ Y187), I191 (= I188), E194 (= E191), E210 (= E207), A211 (= A208), L212 (= L209), A275 (= A275), V276 (≠ T276), G277 (= G277), R278 (= R278), M324 (= M329), L325 (= L330), V355 (≠ A360), Y357 (≠ F362)
Sites not aligning to the query:
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)
36% identity, 97% coverage: 7:469/475 of query aligns to 4:460/472 of 3ladA
- active site: L44 (≠ M40), C48 (= C44), C53 (= C49), S56 (= S52), V190 (≠ Y187), E194 (= E191), F448 (≠ H457), H450 (= H459), E455 (= E464)
- binding flavin-adenine dinucleotide: I9 (= I12), G10 (= G13), G12 (= G15), P13 (≠ V16), E33 (= E36), K34 (≠ A37), G46 (= G42), T47 (= T43), C48 (= C44), G52 (= G48), C53 (= C49), H120 (≠ W118), G121 (= G119), A149 (≠ S146), S150 (≠ P147), G151 (= G148), I191 (= I188), R278 (= R278), D318 (= D323), L325 (= L330), A326 (= A331)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
34% identity, 99% coverage: 3:474/475 of query aligns to 3:468/470 of 6uziC
- active site: C45 (= C44), C50 (= C49), S53 (= S52), V187 (≠ Y187), E191 (= E191), H448 (= H459), E453 (= E464)
- binding flavin-adenine dinucleotide: I12 (= I12), G13 (= G13), G15 (= G15), P16 (≠ V16), G17 (= G17), E36 (= E36), K37 (≠ A37), G43 (= G42), T44 (= T43), C45 (= C44), G49 (= G48), C50 (= C49), S53 (= S52), K54 (= K53), V117 (≠ W118), G118 (= G119), T147 (≠ P147), G148 (= G148), I188 (= I188), R276 (= R278), D316 (= D323), M322 (= M329), L323 (= L330), A324 (= A331)
- binding zinc ion: H448 (= H459), E453 (= E464)
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
35% identity, 97% coverage: 7:469/475 of query aligns to 1:455/465 of 3urhB
- active site: Y35 (≠ M40), C39 (= C44), C44 (= C49), S47 (= S52), V183 (≠ Y187), E187 (= E191), H443 (= H457), H445 (= H459), E450 (= E464)
- binding flavin-adenine dinucleotide: I6 (= I12), G7 (= G13), G9 (= G15), P10 (≠ V16), G11 (= G17), E30 (= E36), K31 (≠ A37), G37 (= G42), T38 (= T43), C39 (= C44), G43 (= G48), C44 (= C49), K48 (= K53), T111 (≠ W118), G112 (= G119), A140 (≠ S146), T141 (≠ P147), G142 (= G148), I184 (= I188), R273 (= R278), G312 (= G322), D313 (= D323), M319 (= M329), L320 (= L330), A321 (= A331), H322 (= H332)
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
34% identity, 99% coverage: 5:474/475 of query aligns to 2:455/455 of 1ebdA
- active site: P13 (≠ V16), L37 (≠ M40), C41 (= C44), C46 (= C49), S49 (= S52), N74 (= N80), V75 (= V81), Y180 (= Y187), E184 (= E191), S320 (= S335), H438 (= H457), H440 (= H459), E445 (= E464)
- binding flavin-adenine dinucleotide: G10 (= G13), G12 (= G15), P13 (≠ V16), V32 (≠ I35), E33 (= E36), K34 (≠ A37), G39 (= G42), V40 (≠ T43), C41 (= C44), G45 (= G48), C46 (= C49), K50 (= K53), E112 (≠ W118), A113 (≠ G119), T141 (≠ P147), G142 (= G148), Y180 (= Y187), I181 (= I188), R268 (= R278), D308 (= D323), A314 (≠ M329), L315 (= L330), A316 (= A331)
1dxlA Dihydrolipoamide dehydrogenase of glycine decarboxylase from pisum sativum (see paper)
36% identity, 97% coverage: 8:469/475 of query aligns to 5:456/467 of 1dxlA
- active site: L38 (≠ M40), C42 (= C44), C47 (= C49), S50 (= S52), Y184 (= Y187), E188 (= E191), H444 (= H457), H446 (= H459), E451 (= E464)
- binding flavin-adenine dinucleotide: I9 (= I12), P13 (≠ V16), G14 (= G17), E33 (= E36), K34 (≠ A37), R35 (vs. gap), G40 (= G42), T41 (= T43), C42 (= C44), G46 (= G48), C47 (= C49), K51 (= K53), Y114 (≠ W118), G115 (= G119), T144 (≠ P147), G145 (= G148), Y184 (= Y187), I185 (= I188), R274 (= R278), D314 (= D323), M320 (= M329), L321 (= L330), A322 (= A331), H323 (= H332)
P31023 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; Pyruvate dehydrogenase complex E3 subunit; E3; PDC-E3; EC 1.8.1.4 from Pisum sativum (Garden pea) (Lathyrus oleraceus) (see 2 papers)
36% identity, 97% coverage: 8:469/475 of query aligns to 39:490/501 of P31023
- 67:76 (vs. 36:44, 60% identical) binding FAD
- C76 (= C44) modified: Disulfide link with 81, Redox-active
- C81 (= C49) modified: Disulfide link with 76, Redox-active
- G149 (= G119) binding FAD
- D348 (= D323) binding FAD
- MLAH 354:357 (= MLAH 329:332) binding FAD
Sites not aligning to the query:
- 1:31 modified: transit peptide, Mitochondrion
P11959 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
34% identity, 99% coverage: 5:474/475 of query aligns to 8:461/470 of P11959
- 39:47 (vs. 36:44, 56% identical) binding FAD
- K56 (= K53) binding FAD
- D314 (= D323) binding FAD
- A322 (= A331) binding FAD
Query Sequence
>WP_011318723.1 NCBI__GCF_000204075.1:WP_011318723.1
MSHEFDYDLVIIGAGVGGHGAALHAVSCGLKTAIIEAGDMGGTCVNRGCIPSKALLAASG
RVRELRDAHHLKSLGIQIGNVEFDRQAIANHANNLVSKIQGDLTNSLKRLGVDIIRGWGK
IAGTQKVTVTGDGGEKTITARDIILSPGSVPFVPPGIEVDGKTVFTSDQGVKLETLPEWV
AIIGSGYIGLEFSDIYSALGCEITLIEALDQLMPGFDRDIAKLAERVLITPRDIETKVGV
YAKKVIPGSPVVIELADFKTKEVVDVIEVDACLVATGRIPATKNLGLESIGVELDRRNFI
PVDDRMAVLSAGEVVPHLWAIGDANGKMMLAHAASAQGIVAVENIIGKERTVDYRSIPAA
AFTHPEVSYVGLTETGAKELGQAEGFEIATSRSYFKGNSKALAENEADGIAKVIYRKDTG
EVLGVHIFGLHASDLIHEASAAVANRQTVQTLAHLVHAHPTLSEVLDEAYKRAIV
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