SitesBLAST
Comparing WP_024770448.1 NCBI__GCF_000520995.1:WP_024770448.1 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)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
74% identity, 100% coverage: 1:468/468 of query aligns to 4:470/470 of 6uziC
- active site: C45 (= C42), C50 (= C47), S53 (= S50), V187 (= V185), E191 (= E189), H448 (= H446), E453 (= E451)
- binding flavin-adenine dinucleotide: I12 (= I9), G13 (= G10), G15 (= G12), P16 (= P13), G17 (= G14), E36 (= E33), K37 (= K34), G43 (= G40), T44 (= T41), C45 (= C42), G49 (= G46), C50 (= C47), S53 (= S50), K54 (= K51), V117 (= V115), G118 (= G116), T147 (= T145), G148 (= G146), I188 (= I186), R276 (= R274), D316 (= D314), M322 (= M320), L323 (= L321), A324 (= A322)
- binding zinc ion: H448 (= H446), E453 (= E451)
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
54% identity, 97% coverage: 4:459/468 of query aligns to 1:458/465 of 3urhB
- active site: Y35 (≠ L38), C39 (= C42), C44 (= C47), S47 (= S50), V183 (= V185), E187 (= E189), H443 (= H444), H445 (= H446), E450 (= E451)
- binding flavin-adenine dinucleotide: I6 (= I9), G7 (= G10), G9 (= G12), P10 (= P13), G11 (= G14), E30 (= E33), K31 (= K34), G37 (= G40), T38 (= T41), C39 (= C42), G43 (= G46), C44 (= C47), K48 (= K51), T111 (≠ V115), G112 (= G116), A140 (= A144), T141 (= T145), G142 (= G146), I184 (= I186), R273 (= R274), G312 (= G313), D313 (= D314), M319 (= M320), L320 (= L321), A321 (= A322), H322 (= H323)
6aonA 1.72 angstrom resolution crystal structure of 2-oxoglutarate dehydrogenase complex subunit dihydrolipoamide dehydrogenase from bordetella pertussis in complex with fad
51% identity, 99% coverage: 4:468/468 of query aligns to 3:473/473 of 6aonA
- active site: P43 (≠ L38), C47 (= C42), C52 (= C47), S55 (= S50), V191 (= V185), E195 (= E189), H450 (= H444), H452 (= H446), E457 (= E451)
- binding calcium ion: A218 (≠ P212), A220 (≠ M214), Q222 (≠ K216)
- binding flavin-adenine dinucleotide: I8 (= I9), G11 (= G12), P12 (= P13), G13 (= G14), D32 (≠ E33), A33 (≠ K34), W34 (≠ Y35), G45 (= G40), T46 (= T41), C47 (= C42), G51 (= G46), C52 (= C47), K56 (= K51), K119 (≠ V115), G120 (= G116), T151 (= T145), G152 (= G146), N171 (≠ S165), I192 (= I186), R280 (= R274), Y283 (= Y277), G319 (= G313), D320 (= D314), M326 (= M320), L327 (= L321), A328 (= A322), H329 (= H323)
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
51% identity, 99% coverage: 4:468/468 of query aligns to 2:455/455 of 2yquB
- active site: P11 (= P13), L36 (= L38), C40 (= C42), C45 (= C47), S48 (= S50), G72 (= G76), V73 (= V78), V177 (= V185), E181 (= E189), S314 (≠ E326), H432 (= H444), H434 (= H446), E439 (= E451)
- binding carbonate ion: A310 (= A322), S314 (≠ E326), S423 (= S435), D426 (= D438)
- binding flavin-adenine dinucleotide: G8 (= G10), G10 (= G12), P11 (= P13), G12 (= G14), E31 (= E33), K32 (= K34), G38 (= G40), T39 (= T41), C40 (= C42), R42 (≠ N44), G44 (= G46), C45 (= C47), K49 (= K51), T110 (≠ V115), A111 (≠ G116), T137 (= T145), G138 (= G146), I178 (= I186), Y265 (= Y277), G301 (= G313), D302 (= D314), M308 (= M320), L309 (= L321), A310 (= A322), H311 (= H323)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
51% identity, 99% coverage: 4:468/468 of query aligns to 2:455/455 of 2yquA
- active site: P11 (= P13), L36 (= L38), C40 (= C42), C45 (= C47), S48 (= S50), G72 (= G76), V73 (= V78), V177 (= V185), E181 (= E189), S314 (≠ E326), H432 (= H444), H434 (= H446), E439 (= E451)
- binding flavin-adenine dinucleotide: G8 (= G10), G10 (= G12), P11 (= P13), G12 (= G14), E31 (= E33), K32 (= K34), G38 (= G40), T39 (= T41), C40 (= C42), R42 (≠ N44), G44 (= G46), C45 (= C47), K49 (= K51), T110 (≠ V115), A111 (≠ G116), T137 (= T145), G138 (= G146), S157 (= S165), I178 (= I186), Y265 (= Y277), G301 (= G313), D302 (= D314), M308 (= M320), L309 (= L321), A310 (= A322)
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
52% identity, 98% coverage: 4:463/468 of query aligns to 2:451/452 of 2eq7A
- active site: P11 (= P13), L36 (= L38), C40 (= C42), C45 (= C47), S48 (= S50), G72 (= G76), V73 (= V78), V177 (= V185), E181 (= E189), S314 (≠ E326), H432 (= H444), H434 (= H446), E439 (= E451)
- binding flavin-adenine dinucleotide: G10 (= G12), P11 (= P13), G12 (= G14), E31 (= E33), K32 (= K34), G38 (= G40), T39 (= T41), C40 (= C42), R42 (≠ N44), G44 (= G46), C45 (= C47), K49 (= K51), T110 (≠ V115), A111 (≠ G116), T137 (= T145), G138 (= G146), S157 (= S165), I178 (= I186), R262 (= R274), Y265 (= Y277), D302 (= D314), M308 (= M320), L309 (= L321), A310 (= A322), H311 (= H323), Y341 (= Y353)
- binding nicotinamide-adenine-dinucleotide: W146 (≠ F154), G174 (= G182), G176 (= G184), V177 (= V185), I178 (= I186), E197 (= E205), Y198 (= Y206), V231 (= V239), V260 (= V272), G261 (= G273), R262 (= R274), M308 (= M320), L309 (= L321), V339 (= V351)
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)
50% identity, 99% coverage: 4:468/468 of query aligns to 4:471/472 of 3ladA
- active site: L44 (= L38), C48 (= C42), C53 (= C47), S56 (= S50), V190 (= V185), E194 (= E189), F448 (≠ H444), H450 (= H446), E455 (= E451)
- binding flavin-adenine dinucleotide: I9 (= I9), G10 (= G10), G12 (= G12), P13 (= P13), E33 (= E33), K34 (= K34), G46 (= G40), T47 (= T41), C48 (= C42), G52 (= G46), C53 (= C47), H120 (≠ V115), G121 (= G116), A149 (= A144), S150 (≠ T145), G151 (= G146), I191 (= I186), R278 (= R274), D318 (= D314), L325 (= L321), A326 (= A322)
P18925 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Azotobacter vinelandii (see 2 papers)
50% identity, 99% coverage: 4:468/468 of query aligns to 5:472/477 of P18925
- 34:49 (vs. 33:42, 50% identical) binding FAD
- C49 (= C42) modified: Disulfide link with 54, Redox-active
- C54 (= C47) modified: Disulfide link with 49, Redox-active
- K58 (= K51) binding FAD
- D319 (= D314) binding FAD
- A327 (= A322) 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)
49% identity, 99% coverage: 5:468/468 of query aligns to 43:509/509 of P09622
- 71:80 (vs. 33:42, 80% identical) binding FAD
- K72 (= K34) to E: in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX; dbSNP:rs121964987
- K89 (= K51) binding FAD; mutation to E: Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- K104 (= K65) to T: in dbSNP:rs1130477
- G154 (= G116) binding FAD
- TGS 183:185 (= TGS 145:147) binding FAD
- 220:227 (vs. 182:189, 75% identical) binding NAD(+)
- E243 (= E205) binding NAD(+)
- V278 (= V239) binding NAD(+)
- G314 (= G273) binding NAD(+)
- D355 (= D314) binding FAD
- MLAH 361:364 (= MLAH 320:323) binding FAD
- E375 (= E334) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (= H342) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (= D407) 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 (= E425) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ F432) 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 (= D438) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (= R441) 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 (= H444) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
- P488 (= P447) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
- S491 (≠ T450) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
- E492 (= E451) mutation to Q: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- R495 (≠ K454) to G: in DLDD; loss of enzyme activity; reduced interaction with PDHX; dbSNP:rs121964989
- K505 (≠ R464) mutation to 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.
49% identity, 99% coverage: 5:468/468 of query aligns to 16:482/482 of 6hg8B
- active site: C53 (= C42), C58 (= C47), S61 (= S50), V196 (= V185), E200 (= E189), H460 (= H446), E465 (= E451)
- binding flavin-adenine dinucleotide: I20 (= I9), G23 (= G12), P24 (= P13), G25 (= G14), E44 (= E33), K45 (= K34), N46 (≠ Y35), G51 (= G40), T52 (= T41), C53 (= C42), G57 (= G46), C58 (= C47), K62 (= K51), Y126 (≠ V115), G127 (= G116), T156 (= T145), G157 (= G146), I197 (= I186), R288 (= R274), F291 (≠ Y277), G327 (= G313), D328 (= D314), M334 (= M320), L335 (= L321), A336 (= A322), H337 (= H323)
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
49% identity, 99% coverage: 5:468/468 of query aligns to 6:472/472 of 1zmdA
- active site: L39 (= L38), C43 (= C42), C48 (= C47), S51 (= S50), V186 (= V185), E190 (= E189), H448 (= H444), H450 (= H446), E455 (= E451)
- binding flavin-adenine dinucleotide: I10 (= I9), G11 (= G10), G13 (= G12), P14 (= P13), G15 (= G14), E34 (= E33), K35 (= K34), N36 (≠ Y35), G41 (= G40), T42 (= T41), C43 (= C42), G47 (= G46), C48 (= C47), K52 (= K51), Y116 (≠ V115), G117 (= G116), T146 (= T145), G147 (= G146), S166 (= S165), R278 (= R274), F281 (≠ Y277), G317 (= G313), D318 (= D314), M324 (= M320), L325 (= L321), A326 (= A322), H327 (= H323)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (= I181), G183 (= G182), G185 (= G184), V186 (= V185), I187 (= I186), E190 (= E189), E206 (= E205), F207 (≠ Y206), L208 (≠ M207), I276 (≠ V272), G277 (= G273), R278 (= R274), M324 (= M320), L325 (= L321), V355 (= V351), Y357 (= Y353)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
49% identity, 99% coverage: 5:468/468 of query aligns to 6:472/472 of 1zmcA
- active site: L39 (= L38), C43 (= C42), C48 (= C47), S51 (= S50), V186 (= V185), E190 (= E189), H448 (= H444), H450 (= H446), E455 (= E451)
- binding flavin-adenine dinucleotide: I10 (= I9), G11 (= G10), G13 (= G12), P14 (= P13), G15 (= G14), E34 (= E33), K35 (= K34), N36 (≠ Y35), G41 (= G40), T42 (= T41), C43 (= C42), G47 (= G46), C48 (= C47), K52 (= K51), Y116 (≠ V115), G117 (= G116), T146 (= T145), G147 (= G146), S166 (= S165), I187 (= I186), F281 (≠ Y277), G317 (= G313), D318 (= D314), M324 (= M320), L325 (= L321), A326 (= A322), H327 (= H323)
- binding nicotinamide-adenine-dinucleotide: G183 (= G182), G185 (= G184), V205 (= V204), E206 (= E205), F207 (≠ Y206), L208 (≠ M207), K240 (= K238), V241 (= V239), I276 (≠ V272), G277 (= G273), R278 (= R274), R297 (= R293), M324 (= M320)
6awaA 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from pseudomonas putida in complex with fad and adenosine-5'-monophosphate.
50% identity, 99% coverage: 4:468/468 of query aligns to 5:472/475 of 6awaA
- active site: L45 (= L38), C49 (= C42), C54 (= C47), S57 (= S50), V191 (= V185), E195 (= E189), F449 (≠ H444), H451 (= H446), E456 (= E451)
- binding adenosine monophosphate: I187 (= I181), E211 (= E205), A212 (≠ Y206), L213 (≠ M207), V245 (= V239), V277 (= V272)
- binding flavin-adenine dinucleotide: I10 (= I9), G13 (= G12), P14 (= P13), G15 (= G14), E34 (= E33), K35 (= K34), T48 (= T41), C49 (= C42), G53 (= G46), C54 (= C47), K58 (= K51), H121 (≠ V115), G122 (= G116), S151 (≠ T145), G152 (= G146), I192 (= I186), R279 (= R274), G318 (= G313), D319 (= D314), M325 (= M320), L326 (= L321), A327 (= A322), Y358 (= Y353)
Sites not aligning to the query:
P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 from Pseudomonas fluorescens (see 2 papers)
50% identity, 99% coverage: 4:468/468 of query aligns to 5:472/478 of P14218
- 34:49 (vs. 33:42, 50% identical) binding FAD
- C49 (= C42) modified: Disulfide link with 54, Redox-active
- C54 (= C47) modified: Disulfide link with 49, Redox-active
- K58 (= K51) binding FAD
- G122 (= G116) binding FAD
- D319 (= D314) binding FAD
- A327 (= A322) binding FAD
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
50% identity, 99% coverage: 4:468/468 of query aligns to 4:471/473 of 5u8wA
- active site: P13 (= P13), L44 (= L38), C48 (= C42), C53 (= C47), S56 (= S50), G82 (= G76), V83 (= V78), V190 (= V185), E194 (= E189), S330 (≠ E326), F448 (≠ H444), H450 (= H446), E455 (= E451)
- binding flavin-adenine dinucleotide: I9 (= I9), G12 (= G12), P13 (= P13), G14 (= G14), E33 (= E33), K34 (= K34), G46 (= G40), T47 (= T41), C48 (= C42), G52 (= G46), C53 (= C47), K57 (= K51), H120 (≠ V115), G121 (= G116), A149 (= A144), S150 (≠ T145), G151 (= G146), S170 (= S165), G317 (= G313), D318 (= D314), M324 (= M320), L325 (= L321), A326 (= A322), H327 (= H323), Y357 (= Y353), H450 (= H446), P451 (= P447)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (= I181), G189 (= G184), V190 (= V185), I191 (= I186), E194 (= E189), E210 (= E205), A211 (≠ Y206), L212 (≠ M207), A275 (≠ S271), V276 (= V272), G277 (= G273), R278 (= R274), M324 (= M320), L325 (= L321), V355 (= V351), Y357 (= Y353)
Sites not aligning to the query:
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
50% identity, 99% coverage: 4:468/468 of query aligns to 3:470/472 of 5u8vA
- active site: P12 (= P13), L43 (= L38), C47 (= C42), C52 (= C47), S55 (= S50), G81 (= G76), V82 (= V78), V189 (= V185), E193 (= E189), S329 (≠ E326), F447 (≠ H444), H449 (= H446), E454 (= E451)
- binding flavin-adenine dinucleotide: I8 (= I9), G11 (= G12), P12 (= P13), G13 (= G14), E32 (= E33), G45 (= G40), T46 (= T41), C47 (= C42), G51 (= G46), C52 (= C47), K56 (= K51), H119 (≠ V115), G120 (= G116), A148 (= A144), S149 (≠ T145), G150 (= G146), S169 (= S165), I190 (= I186), R277 (= R274), G316 (= G313), D317 (= D314), M323 (= M320), L324 (= L321), A325 (= A322), H326 (= H323), H449 (= H446), P450 (= P447)
- binding nicotinamide-adenine-dinucleotide: I185 (= I181), G186 (= G182), G188 (= G184), V189 (= V185), I190 (= I186), L208 (≠ V204), E209 (= E205), A210 (≠ Y206), V243 (= V239), V275 (= V272), G276 (= G273)
Sites not aligning to the query:
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
50% identity, 99% coverage: 4:468/468 of query aligns to 7:474/477 of 5u8uD
- active site: P16 (= P13), L47 (= L38), C51 (= C42), C56 (= C47), S59 (= S50), G85 (= G76), V86 (= V78), V193 (= V185), E197 (= E189), S333 (≠ E326), F451 (≠ H444), H453 (= H446), E458 (= E451)
- binding flavin-adenine dinucleotide: I12 (= I9), G15 (= G12), P16 (= P13), G17 (= G14), E36 (= E33), K37 (= K34), G49 (= G40), T50 (= T41), C51 (= C42), G55 (= G46), C56 (= C47), K60 (= K51), H123 (≠ V115), G124 (= G116), A152 (= A144), S153 (≠ T145), G154 (= G146), I194 (= I186), R281 (= R274), G320 (= G313), D321 (= D314), M327 (= M320), L328 (= L321), A329 (= A322), H330 (= H323), H453 (= H446), P454 (= P447)
Sites not aligning to the query:
6bz0A 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from acinetobacter baumannii in complex with fad.
50% identity, 99% coverage: 4:467/468 of query aligns to 2:467/469 of 6bz0A
- active site: C45 (= C42), C50 (= C47), S53 (= S50), V187 (= V185), E191 (= E189), H447 (= H446), E452 (= E451)
- binding flavin-adenine dinucleotide: I7 (= I9), G10 (= G12), P11 (= P13), G12 (= G14), E31 (= E33), K32 (= K34), R33 (≠ Y35), G43 (= G40), T44 (= T41), C45 (= C42), G49 (= G46), C50 (= C47), K54 (= K51), T117 (≠ V115), G118 (= G116), S147 (≠ T145), G148 (= G146), S167 (= S165), I188 (= I186), R275 (= R274), Y278 (= Y277), D315 (= D314), M321 (= M320), L322 (= L321), A323 (= A322), A326 (= A325), Y354 (= Y353)
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)
48% identity, 99% coverage: 5:468/468 of query aligns to 39:501/501 of P31023
- 67:76 (vs. 33:42, 70% identical) binding FAD
- C76 (= C42) modified: Disulfide link with 81, Redox-active
- C81 (= C47) modified: Disulfide link with 76, Redox-active
- G149 (= G116) binding FAD
- D348 (= D314) binding FAD
- MLAH 354:357 (= MLAH 320:323) 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)
48% identity, 99% coverage: 5:468/468 of query aligns to 5:467/467 of 1dxlA
- active site: L38 (= L38), C42 (= C42), C47 (= C47), S50 (= S50), Y184 (≠ V185), E188 (= E189), H444 (= H444), H446 (= H446), E451 (= E451)
- binding flavin-adenine dinucleotide: I9 (= I9), P13 (= P13), G14 (= G14), E33 (= E33), K34 (= K34), R35 (≠ Y35), G40 (= G40), T41 (= T41), C42 (= C42), G46 (= G46), C47 (= C47), K51 (= K51), Y114 (≠ V115), G115 (= G116), T144 (= T145), G145 (= G146), Y184 (≠ V185), I185 (= I186), R274 (= R274), D314 (= D314), M320 (= M320), L321 (= L321), A322 (= A322), H323 (= H323)
Query Sequence
>WP_024770448.1 NCBI__GCF_000520995.1:WP_024770448.1
MSTYDVAVIGSGPGGYVAAIRCAQLGMKTAIIEKYSTLGGTCLNVGCIPSKALLDSSHHY
EHAVKHFADHGIEIPGDVKINLEKMIARKQSVVDQTCDGVSFLMKKNKIDVFEGVGSFKD
ATHVNITKADGTVETIEAKNTIIATGSKPSTLPFIKIDKKRVITSTEALKLKEVPKHLII
IGGGVIGLELGQVYRRLGAEVSVVEYMDRIIPGMDKALSKELQKVMKKQKSKIYTSHKVT
GVSVSGDEVTVTADDKKGNPVELKGDYCLVSVGRRPYTDGLNAEAAGVKLNDRGQVEVND
HLQTSASNIYAIGDVIKGAMLAHKAEEEGTFVAETLAGQKPHIDYNLIPGVVYTWPEVAA
VGKTEEELTEAGIKYKSGQFPFRALGRSRASGDLDGFVKILADETTDEVLGVHMIGARCA
DLIAEAVTAMEFRASAEDISRMSHAHPTFTEAVKEAALAATDNRALHM
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