SitesBLAST
Comparing WP_011779673.1 NCBI__GCF_000015305.1:WP_011779673.1 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)
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
38% identity, 97% coverage: 7:462/471 of query aligns to 1:462/465 of 3urhB
- active site: Y35 (≠ L41), C39 (= C45), C44 (≠ T50), S47 (= S53), V183 (= V188), E187 (= E192), H443 (≠ F443), H445 (≠ Y445), E450 (= E450)
- binding flavin-adenine dinucleotide: I6 (= I12), G7 (= G13), G9 (= G15), P10 (= P16), G11 (= G17), E30 (= E36), K31 (≠ R37), G37 (= G43), T38 (≠ V44), C39 (= C45), G43 (= G49), C44 (≠ T50), K48 (= K54), T111 (≠ H117), G112 (= G118), A140 (= A147), T141 (= T148), G142 (= G149), I184 (= I189), R273 (= R273), G312 (= G312), D313 (= D313), M319 (≠ A319), L320 (= L320), A321 (= A321), H322 (≠ A322)
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
36% identity, 97% coverage: 7:462/471 of query aligns to 2:451/452 of 2eq7A
- active site: P11 (= P16), L36 (= L41), C40 (= C45), C45 (≠ T50), S48 (= S53), G72 (≠ V78), V73 (≠ K79), V177 (= V188), E181 (= E192), S314 (≠ M325), H432 (≠ F443), H434 (≠ Y445), E439 (= E450)
- binding flavin-adenine dinucleotide: G10 (= G15), P11 (= P16), G12 (= G17), E31 (= E36), K32 (≠ R37), G38 (= G43), T39 (≠ V44), C40 (= C45), R42 (≠ N47), G44 (= G49), C45 (≠ T50), K49 (= K54), T110 (≠ H117), A111 (≠ G118), T137 (= T148), G138 (= G149), S157 (= S168), I178 (= I189), R262 (= R273), Y265 (≠ Q276), D302 (= D313), M308 (≠ A319), L309 (= L320), A310 (= A321), H311 (≠ A322), Y341 (= Y352)
- binding nicotinamide-adenine-dinucleotide: W146 (≠ G157), G174 (= G185), G176 (= G187), V177 (= V188), I178 (= I189), E197 (= E208), Y198 (≠ K209), V231 (= V242), V260 (≠ A271), G261 (= G272), R262 (= R273), M308 (≠ A319), L309 (= L320), V339 (≠ G350)
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
36% identity, 97% coverage: 7:462/471 of query aligns to 2:451/455 of 2yquB
- active site: P11 (= P16), L36 (= L41), C40 (= C45), C45 (≠ T50), S48 (= S53), G72 (≠ V78), V73 (≠ K79), V177 (= V188), E181 (= E192), S314 (≠ M325), H432 (≠ F443), H434 (≠ Y445), E439 (= E450)
- binding carbonate ion: A310 (= A321), S314 (≠ M325), S423 (≠ T434), D426 (≠ Y437)
- binding flavin-adenine dinucleotide: G8 (= G13), G10 (= G15), P11 (= P16), G12 (= G17), E31 (= E36), K32 (≠ R37), G38 (= G43), T39 (≠ V44), C40 (= C45), R42 (≠ N47), G44 (= G49), C45 (≠ T50), K49 (= K54), T110 (≠ H117), A111 (≠ G118), T137 (= T148), G138 (= G149), I178 (= I189), Y265 (≠ Q276), G301 (= G312), D302 (= D313), M308 (≠ A319), L309 (= L320), A310 (= A321), H311 (≠ A322)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
36% identity, 97% coverage: 7:462/471 of query aligns to 2:451/455 of 2yquA
- active site: P11 (= P16), L36 (= L41), C40 (= C45), C45 (≠ T50), S48 (= S53), G72 (≠ V78), V73 (≠ K79), V177 (= V188), E181 (= E192), S314 (≠ M325), H432 (≠ F443), H434 (≠ Y445), E439 (= E450)
- binding flavin-adenine dinucleotide: G8 (= G13), G10 (= G15), P11 (= P16), G12 (= G17), E31 (= E36), K32 (≠ R37), G38 (= G43), T39 (≠ V44), C40 (= C45), R42 (≠ N47), G44 (= G49), C45 (≠ T50), K49 (= K54), T110 (≠ H117), A111 (≠ G118), T137 (= T148), G138 (= G149), S157 (= S168), I178 (= I189), Y265 (≠ Q276), G301 (= G312), D302 (= D313), M308 (≠ A319), L309 (= L320), A310 (= A321)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
32% identity, 98% coverage: 6:466/471 of query aligns to 6:468/470 of 6uziC
- active site: C45 (= C45), C50 (≠ T50), S53 (= S53), V187 (= V188), E191 (= E192), H448 (≠ Y445), E453 (= E450)
- binding flavin-adenine dinucleotide: I12 (= I12), G13 (= G13), G15 (= G15), P16 (= P16), G17 (= G17), E36 (= E36), K37 (≠ R37), G43 (= G43), T44 (≠ V44), C45 (= C45), G49 (= G49), C50 (≠ T50), S53 (= S53), K54 (= K54), V117 (≠ H117), G118 (= G118), T147 (= T148), G148 (= G149), I188 (= I189), R276 (= R273), D316 (= D313), M322 (≠ A319), L323 (= L320), A324 (= A321)
- binding zinc ion: H448 (≠ Y445), E453 (= E450)
P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 from Pseudomonas fluorescens (see 2 papers)
34% identity, 96% coverage: 6:459/471 of query aligns to 4:465/478 of P14218
- 34:49 (vs. 36:45, 38% identical) binding FAD
- C49 (= C45) modified: Disulfide link with 54, Redox-active
- C54 (≠ T50) modified: Disulfide link with 49, Redox-active
- K58 (= K54) binding FAD
- G122 (= G118) binding FAD
- D319 (= D313) binding FAD
- A327 (= A321) binding FAD
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
6awaA 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from pseudomonas putida in complex with fad and adenosine-5'-monophosphate.
34% identity, 96% coverage: 6:459/471 of query aligns to 4:465/475 of 6awaA
- active site: L45 (= L41), C49 (= C45), C54 (≠ T50), S57 (= S53), V191 (= V188), E195 (= E192), F449 (= F443), H451 (≠ Y445), E456 (= E450)
- binding adenosine monophosphate: I187 (≠ V184), E211 (= E208), A212 (≠ K209), L213 (≠ R210), V245 (= V242), V277 (≠ A271)
- binding flavin-adenine dinucleotide: I10 (= I12), G13 (= G15), P14 (= P16), G15 (= G17), E34 (= E36), K35 (≠ R37), T48 (≠ V44), C49 (= C45), G53 (= G49), C54 (≠ T50), K58 (= K54), H121 (= H117), G122 (= G118), S151 (≠ T148), G152 (= G149), I192 (= I189), R279 (= R273), G318 (= G312), D319 (= D313), M325 (≠ A319), L326 (= L320), A327 (= A321), Y358 (= Y352)
Sites not aligning to the query:
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
34% identity, 96% coverage: 6:459/471 of query aligns to 2:463/472 of 5u8vA
- active site: P12 (= P16), L43 (= L41), C47 (= C45), C52 (≠ T50), S55 (= S53), G81 (≠ V78), V82 (≠ K79), V189 (= V188), E193 (= E192), S329 (≠ M325), F447 (= F443), H449 (≠ Y445), E454 (= E450)
- binding flavin-adenine dinucleotide: I8 (= I12), G11 (= G15), P12 (= P16), G13 (= G17), E32 (= E36), G45 (= G43), T46 (≠ V44), C47 (= C45), G51 (= G49), C52 (≠ T50), K56 (= K54), H119 (= H117), G120 (= G118), A148 (= A147), S149 (≠ T148), G150 (= G149), S169 (= S168), I190 (= I189), R277 (= R273), G316 (= G312), D317 (= D313), M323 (≠ A319), L324 (= L320), A325 (= A321), H326 (≠ A322), H449 (≠ Y445), P450 (= P446)
- binding nicotinamide-adenine-dinucleotide: I185 (≠ V184), G186 (= G185), G188 (= G187), V189 (= V188), I190 (= I189), L208 (≠ V207), E209 (= E208), A210 (≠ K209), V243 (= V242), V275 (≠ A271), G276 (= G272)
Sites not aligning to the query:
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
34% identity, 96% coverage: 6:459/471 of query aligns to 6:467/477 of 5u8uD
- active site: P16 (= P16), L47 (= L41), C51 (= C45), C56 (≠ T50), S59 (= S53), G85 (≠ V78), V86 (≠ K79), V193 (= V188), E197 (= E192), S333 (≠ M325), F451 (= F443), H453 (≠ Y445), E458 (= E450)
- binding flavin-adenine dinucleotide: I12 (= I12), G15 (= G15), P16 (= P16), G17 (= G17), E36 (= E36), K37 (≠ R37), G49 (= G43), T50 (≠ V44), C51 (= C45), G55 (= G49), C56 (≠ T50), K60 (= K54), H123 (= H117), G124 (= G118), A152 (= A147), S153 (≠ T148), G154 (= G149), I194 (= I189), R281 (= R273), G320 (= G312), D321 (= D313), M327 (≠ A319), L328 (= L320), A329 (= A321), H330 (≠ A322), H453 (≠ Y445), P454 (= P446)
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)
33% identity, 96% coverage: 6:459/471 of query aligns to 3:464/472 of 3ladA
- active site: L44 (= L41), C48 (= C45), C53 (≠ T50), S56 (= S53), V190 (= V188), E194 (= E192), F448 (= F443), H450 (≠ Y445), E455 (= E450)
- binding flavin-adenine dinucleotide: I9 (= I12), G10 (= G13), G12 (= G15), P13 (= P16), E33 (= E36), K34 (≠ R37), G46 (= G43), T47 (≠ V44), C48 (= C45), G52 (= G49), C53 (≠ T50), H120 (= H117), G121 (= G118), A149 (= A147), S150 (≠ T148), G151 (= G149), I191 (= I189), R278 (= R273), D318 (= D313), L325 (= L320), A326 (= A321)
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
34% identity, 96% coverage: 6:459/471 of query aligns to 3:464/473 of 5u8wA
- active site: P13 (= P16), L44 (= L41), C48 (= C45), C53 (≠ T50), S56 (= S53), G82 (≠ V78), V83 (≠ K79), V190 (= V188), E194 (= E192), S330 (≠ M325), F448 (= F443), H450 (≠ Y445), E455 (= E450)
- binding flavin-adenine dinucleotide: I9 (= I12), G12 (= G15), P13 (= P16), G14 (= G17), E33 (= E36), K34 (≠ R37), G46 (= G43), T47 (≠ V44), C48 (= C45), G52 (= G49), C53 (≠ T50), K57 (= K54), H120 (= H117), G121 (= G118), A149 (= A147), S150 (≠ T148), G151 (= G149), S170 (= S168), G317 (= G312), D318 (= D313), M324 (≠ A319), L325 (= L320), A326 (= A321), H327 (≠ A322), Y357 (= Y352), H450 (≠ Y445), P451 (= P446)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (≠ V184), G189 (= G187), V190 (= V188), I191 (= I189), E194 (= E192), E210 (= E208), A211 (≠ K209), L212 (≠ R210), A275 (≠ S270), V276 (≠ A271), G277 (= G272), R278 (= R273), M324 (≠ A319), L325 (= L320), V355 (≠ G350), Y357 (= Y352)
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)
33% identity, 96% coverage: 6:459/471 of query aligns to 4:465/477 of P18925
- 34:49 (vs. 36:45, 31% identical) binding FAD
- C49 (= C45) modified: Disulfide link with 54, Redox-active
- C54 (≠ T50) modified: Disulfide link with 49, Redox-active
- K58 (= K54) binding FAD
- D319 (= D313) binding FAD
- A327 (= A321) binding FAD
P09622 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; EC 1.8.1.4 from Homo sapiens (Human) (see 14 papers)
33% identity, 96% coverage: 5:457/471 of query aligns to 40:499/509 of P09622
- 71:80 (vs. 36:45, 50% identical) binding FAD
- K72 (≠ R37) to E: in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX; dbSNP:rs121964987
- K89 (= K54) binding FAD; mutation to E: Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- K104 (≠ R69) to T: in dbSNP:rs1130477
- G154 (= G118) binding FAD
- TGS 183:185 (≠ TGT 148:150) binding FAD
- 220:227 (vs. 185:192, 88% identical) binding NAD(+)
- E243 (= E208) binding NAD(+)
- V278 (= V242) binding NAD(+)
- G314 (= G272) binding NAD(+)
- D355 (= D313) binding FAD
- MLAH 361:364 (≠ ALAA 319:322) binding FAD
- E375 (≠ Y333) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (≠ Q341) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (≠ L406) 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 (≠ I424) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ C431) 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 (≠ Y437) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (≠ D440) 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 (≠ F443) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
- P488 (= P446) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
- S491 (= S449) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
- E492 (= E450) mutation to Q: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- R495 (≠ K453) 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.
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)
33% identity, 97% coverage: 6:462/471 of query aligns to 37:497/501 of P31023
- 67:76 (vs. 36:45, 50% identical) binding FAD
- C76 (= C45) modified: Disulfide link with 81, Redox-active
- C81 (≠ T50) modified: Disulfide link with 76, Redox-active
- G149 (= G118) binding FAD
- D348 (= D313) binding FAD
- MLAH 354:357 (≠ ALAA 319:322) binding FAD
Sites not aligning to the query:
- 1:31 modified: transit peptide, Mitochondrion
1dxlA Dihydrolipoamide dehydrogenase of glycine decarboxylase from pisum sativum (see paper)
33% identity, 97% coverage: 6:462/471 of query aligns to 3:463/467 of 1dxlA
- active site: L38 (= L41), C42 (= C45), C47 (≠ T50), S50 (= S53), Y184 (≠ V188), E188 (= E192), H444 (≠ F443), H446 (≠ Y445), E451 (= E450)
- binding flavin-adenine dinucleotide: I9 (= I12), P13 (= P16), G14 (= G17), E33 (= E36), K34 (≠ R37), R35 (≠ G38), G40 (= G43), T41 (≠ V44), C42 (= C45), G46 (= G49), C47 (≠ T50), K51 (= K54), Y114 (≠ H117), G115 (= G118), T144 (= T148), G145 (= G149), Y184 (≠ V188), I185 (= I189), R274 (= R273), D314 (= D313), M320 (≠ A319), L321 (= L320), A322 (= A321), H323 (≠ A322)
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
33% identity, 96% coverage: 5:457/471 of query aligns to 3:462/472 of 1zmdA
- active site: L39 (= L41), C43 (= C45), C48 (≠ T50), S51 (= S53), V186 (= V188), E190 (= E192), H448 (≠ F443), H450 (≠ Y445), E455 (= E450)
- binding flavin-adenine dinucleotide: I10 (= I12), G11 (= G13), G13 (= G15), P14 (= P16), G15 (= G17), E34 (= E36), K35 (≠ R37), N36 (≠ G38), G41 (= G43), T42 (≠ V44), C43 (= C45), G47 (= G49), C48 (≠ T50), K52 (= K54), Y116 (≠ H117), G117 (= G118), T146 (= T148), G147 (= G149), S166 (= S168), R278 (= R273), F281 (≠ Q276), G317 (= G312), D318 (= D313), M324 (≠ A319), L325 (= L320), A326 (= A321), H327 (≠ A322)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (≠ V184), G183 (= G185), G185 (= G187), V186 (= V188), I187 (= I189), E190 (= E192), E206 (= E208), F207 (≠ K209), L208 (≠ R210), I276 (≠ A271), G277 (= G272), R278 (= R273), M324 (≠ A319), L325 (= L320), V355 (≠ G350), Y357 (= Y352)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
33% identity, 96% coverage: 5:457/471 of query aligns to 3:462/472 of 1zmcA
- active site: L39 (= L41), C43 (= C45), C48 (≠ T50), S51 (= S53), V186 (= V188), E190 (= E192), H448 (≠ F443), H450 (≠ Y445), E455 (= E450)
- binding flavin-adenine dinucleotide: I10 (= I12), G11 (= G13), G13 (= G15), P14 (= P16), G15 (= G17), E34 (= E36), K35 (≠ R37), N36 (≠ G38), G41 (= G43), T42 (≠ V44), C43 (= C45), G47 (= G49), C48 (≠ T50), K52 (= K54), Y116 (≠ H117), G117 (= G118), T146 (= T148), G147 (= G149), S166 (= S168), I187 (= I189), F281 (≠ Q276), G317 (= G312), D318 (= D313), M324 (≠ A319), L325 (= L320), A326 (= A321), H327 (≠ A322)
- binding nicotinamide-adenine-dinucleotide: G183 (= G185), G185 (= G187), V205 (= V207), E206 (= E208), F207 (≠ K209), L208 (≠ R210), K240 (≠ E241), V241 (= V242), I276 (≠ A271), G277 (= G272), R278 (= R273), R297 (= R292), M324 (≠ A319)
6hg8B Crystal structure of the r460g disease-causing mutant of the human dihydrolipoamide dehydrogenase.
33% identity, 96% coverage: 5:457/471 of query aligns to 13:472/482 of 6hg8B
- active site: C53 (= C45), C58 (≠ T50), S61 (= S53), V196 (= V188), E200 (= E192), H460 (≠ Y445), E465 (= E450)
- binding flavin-adenine dinucleotide: I20 (= I12), G23 (= G15), P24 (= P16), G25 (= G17), E44 (= E36), K45 (≠ R37), N46 (≠ G38), G51 (= G43), T52 (≠ V44), C53 (= C45), G57 (= G49), C58 (≠ T50), K62 (= K54), Y126 (≠ H117), G127 (= G118), T156 (= T148), G157 (= G149), I197 (= I189), R288 (= R273), F291 (≠ Q276), G327 (= G312), D328 (= D313), M334 (≠ A319), L335 (= L320), A336 (= A321), H337 (≠ A322)
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
34% identity, 95% coverage: 5:450/471 of query aligns to 2:445/455 of 1ebdA
- active site: P13 (= P16), L37 (= L41), C41 (= C45), C46 (≠ T50), S49 (= S53), N74 (≠ K79), V75 (≠ E80), Y180 (≠ V188), E184 (= E192), S320 (≠ M325), H438 (≠ F443), H440 (≠ Y445), E445 (= E450)
- binding flavin-adenine dinucleotide: G10 (= G13), G12 (= G15), P13 (= P16), V32 (= V35), E33 (= E36), K34 (≠ R37), G39 (= G43), V40 (= V44), C41 (= C45), G45 (= G49), C46 (≠ T50), K50 (= K54), E112 (≠ H117), A113 (≠ G118), T141 (= T148), G142 (= G149), Y180 (≠ V188), I181 (= I189), R268 (= R273), D308 (= D313), A314 (= A319), L315 (= L320), A316 (= A321)
P11959 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
34% identity, 95% coverage: 5:450/471 of query aligns to 8:451/470 of P11959
- 39:47 (vs. 36:45, 70% identical) binding FAD
- K56 (= K54) binding FAD
- D314 (= D313) binding FAD
- A322 (= A321) binding FAD
Query Sequence
>WP_011779673.1 NCBI__GCF_000015305.1:WP_011779673.1
MASKLEYDLVVIGSGPGGQKAAIAAAKLGKTVAVVERGRMLGGVCVNTGTIPSKTLREAV
VYLTGMSQRELYGTSYRVKEKITPADLLARTTHVISREQDVVRSQLMRNRVDLVQGHGRF
LDAHTVLVEEPHRGERTTLTGEHIVIATGTKPARPAGVEFDEERVLDSDGILDLKTLPTS
MVVVGAGVIGIEYASMFAALGTKVTVVEKRGSMLEFCDPEIVESLKFHLRDLAVTFRFGE
EVTGVDVGAAGTVTTLASGKQIPAETVMYSAGRQGQTDHLDLASAGLEADDRGRIFVDDN
YQTKVDHIYAVGDVIGFPALAATSMDQGRLAAYHAFGEPTQGMTELQPIGIYSIPEVSYV
GATEVELTKNAIPYEVGVSRYRELARGQIAGDSYGMLKLLVSTEDLRLLGVHIFGTSATE
MVHIGQAVMGCGGTVEYLVDAVFNYPTFSEAYKVAALDVMNKLRALSQFRS
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