SitesBLAST
Comparing WP_011386317.1 NCBI__GCF_000009985.1:WP_011386317.1 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)
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
62% identity, 99% coverage: 6:468/469 of query aligns to 1:465/465 of 3urhB
- active site: Y35 (≠ L40), C39 (= C44), C44 (= C49), S47 (= S52), V183 (= V186), E187 (= E190), H443 (= H446), H445 (= H448), E450 (= E453)
- binding flavin-adenine dinucleotide: I6 (= I11), G7 (= G12), G9 (= G14), P10 (= P15), G11 (= G16), E30 (= E35), K31 (= K36), G37 (= G42), T38 (= T43), C39 (= C44), G43 (= G48), C44 (= C49), K48 (= K53), T111 (≠ A116), G112 (= G117), A140 (= A145), T141 (= T146), G142 (= G147), I184 (= I187), R273 (= R276), G312 (= G315), D313 (= D316), M319 (= M322), L320 (= L323), A321 (= A324), H322 (= H325)
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)
62% identity, 99% coverage: 7:468/469 of query aligns to 39:500/501 of P31023
- 67:76 (vs. 35:44, 90% identical) binding
- C76 (= C44) modified: Disulfide link with 81, Redox-active
- C81 (= C49) modified: Disulfide link with 76, Redox-active
- G149 (= G117) binding
- D348 (= D316) binding
- MLAH 354:357 (= MLAH 322:325) binding
Sites not aligning to the query:
- 1:31 modified: transit peptide, Mitochondrion
1dxlA Dihydrolipoamide dehydrogenase of glycine decarboxylase from pisum sativum (see paper)
62% identity, 99% coverage: 7:468/469 of query aligns to 5:466/467 of 1dxlA
- active site: L38 (= L40), C42 (= C44), C47 (= C49), S50 (= S52), Y184 (≠ V186), E188 (= E190), H444 (= H446), H446 (= H448), E451 (= E453)
- binding flavin-adenine dinucleotide: I9 (= I11), P13 (= P15), G14 (= G16), E33 (= E35), K34 (= K36), R35 (= R37), G40 (= G42), T41 (= T43), C42 (= C44), G46 (= G48), C47 (= C49), K51 (= K53), Y114 (≠ A116), G115 (= G117), T144 (= T146), G145 (= G147), Y184 (≠ V186), I185 (= I187), R274 (= R276), D314 (= D316), M320 (= M322), L321 (= L323), A322 (= A324), H323 (= H325)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
56% identity, 99% coverage: 4:468/469 of query aligns to 5:469/470 of 6uziC
- active site: C45 (= C44), C50 (= C49), S53 (= S52), V187 (= V186), E191 (= E190), H448 (= H448), E453 (= E453)
- binding flavin-adenine dinucleotide: I12 (= I11), G13 (= G12), G15 (= G14), P16 (= P15), G17 (= G16), E36 (= E35), K37 (= K36), G43 (= G42), T44 (= T43), C45 (= C44), G49 (= G48), C50 (= C49), S53 (= S52), K54 (= K53), V117 (≠ A116), G118 (= G117), T147 (= T146), G148 (= G147), I188 (= I187), R276 (= R276), D316 (= D316), M322 (= M322), L323 (= L323), A324 (= A324)
- binding zinc ion: H448 (= H448), E453 (= E453)
P09622 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; EC 1.8.1.4 from Homo sapiens (Human) (see 14 papers)
57% identity, 97% coverage: 7:461/469 of query aligns to 43:500/509 of P09622
- 71:80 (vs. 35:44, 70% identical) binding
- K72 (= K36) 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 (≠ H67) to T: in dbSNP:rs1130477
- G154 (= G117) binding
- TGS 183:185 (= TGS 146:148) binding
- 220:227 (vs. 183:190, 75% identical) binding
- E243 (= E206) binding
- V278 (= V240) binding
- G314 (= G275) binding
- D355 (= D316) binding
- MLAH 361:364 (= MLAH 322:325) binding
- E375 (= E336) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (= H344) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (= D409) 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 (= E427) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ F434) 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 (= D440) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (= R443) 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 (= H446) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
- P488 (= P449) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
- S491 (≠ G452) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
- E492 (= E453) mutation to Q: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- R495 (≠ K456) 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.
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
57% identity, 97% coverage: 7:461/469 of query aligns to 6:463/472 of 1zmdA
- active site: L39 (= L40), C43 (= C44), C48 (= C49), S51 (= S52), V186 (= V186), E190 (= E190), H448 (= H446), H450 (= H448), E455 (= E453)
- binding flavin-adenine dinucleotide: I10 (= I11), G11 (= G12), G13 (= G14), P14 (= P15), G15 (= G16), E34 (= E35), K35 (= K36), N36 (≠ R37), G41 (= G42), T42 (= T43), C43 (= C44), G47 (= G48), C48 (= C49), K52 (= K53), Y116 (≠ A116), G117 (= G117), T146 (= T146), G147 (= G147), S166 (= S166), R278 (= R276), F281 (≠ Y279), G317 (= G315), D318 (= D316), M324 (= M322), L325 (= L323), A326 (= A324), H327 (= H325)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (= I182), G183 (= G183), G185 (= G185), V186 (= V186), I187 (= I187), E190 (= E190), E206 (= E206), F207 (= F207), L208 (= L208), I276 (= I274), G277 (= G275), R278 (= R276), M324 (= M322), L325 (= L323), V355 (= V353), Y357 (= Y355)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
57% identity, 97% coverage: 7:461/469 of query aligns to 6:463/472 of 1zmcA
- active site: L39 (= L40), C43 (= C44), C48 (= C49), S51 (= S52), V186 (= V186), E190 (= E190), H448 (= H446), H450 (= H448), E455 (= E453)
- binding flavin-adenine dinucleotide: I10 (= I11), G11 (= G12), G13 (= G14), P14 (= P15), G15 (= G16), E34 (= E35), K35 (= K36), N36 (≠ R37), G41 (= G42), T42 (= T43), C43 (= C44), G47 (= G48), C48 (= C49), K52 (= K53), Y116 (≠ A116), G117 (= G117), T146 (= T146), G147 (= G147), S166 (= S166), I187 (= I187), F281 (≠ Y279), G317 (= G315), D318 (= D316), M324 (= M322), L325 (= L323), A326 (= A324), H327 (= H325)
- binding nicotinamide-adenine-dinucleotide: G183 (= G183), G185 (= G185), V205 (= V205), E206 (= E206), F207 (= F207), L208 (= L208), K240 (= K239), V241 (= V240), I276 (= I274), G277 (= G275), R278 (= R276), R297 (= R295), M324 (= M322)
6hg8B Crystal structure of the r460g disease-causing mutant of the human dihydrolipoamide dehydrogenase.
57% identity, 97% coverage: 7:461/469 of query aligns to 16:473/482 of 6hg8B
- active site: C53 (= C44), C58 (= C49), S61 (= S52), V196 (= V186), E200 (= E190), H460 (= H448), E465 (= E453)
- binding flavin-adenine dinucleotide: I20 (= I11), G23 (= G14), P24 (= P15), G25 (= G16), E44 (= E35), K45 (= K36), N46 (≠ R37), G51 (= G42), T52 (= T43), C53 (= C44), G57 (= G48), C58 (= C49), K62 (= K53), Y126 (≠ A116), G127 (= G117), T156 (= T146), G157 (= G147), I197 (= I187), R288 (= R276), F291 (≠ Y279), G327 (= G315), D328 (= D316), M334 (= M322), L335 (= L323), A336 (= A324), H337 (= H325)
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)
55% identity, 99% coverage: 3:468/469 of query aligns to 24:498/499 of P09624
- 56:65 (vs. 35:44, 90% identical) binding
- C65 (= C44) modified: Disulfide link with 70, Redox-active
- C70 (= C49) modified: Disulfide link with 65, Redox-active
- K74 (= K53) binding
- G139 (= G117) binding
- D346 (= D316) binding
- MLAH 352:355 (= MLAH 322:325) binding
- H478 (= H448) 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+
55% identity, 99% coverage: 3:468/469 of query aligns to 3:477/478 of 1v59A
- active site: L40 (= L40), C44 (= C44), C49 (= C49), S52 (= S52), I193 (≠ V186), E197 (= E190), T349 (≠ G340), H455 (= H446), H457 (= H448), E462 (= E453)
- binding flavin-adenine dinucleotide: G14 (= G14), P15 (= P15), A16 (≠ G16), E35 (= E35), K36 (= K36), R37 (= R37), G42 (= G42), T43 (= T43), C44 (= C44), G48 (= G48), C49 (= C49), K53 (= K53), N117 (≠ A116), G118 (= G117), T153 (= T146), G154 (= G147), R285 (= R276), Y288 (= Y279), G324 (= G315), D325 (= D316), M331 (= M322), L332 (= L323), A333 (= A324), H334 (= H325), Y364 (= Y355)
- binding nicotinamide-adenine-dinucleotide: I189 (= I182), G190 (= G183), E213 (= E206), F214 (= F207), K246 (= K239), V283 (≠ I274)
1jehA Crystal structure of yeast e3, lipoamide dehydrogenase (see paper)
55% identity, 99% coverage: 3:468/469 of query aligns to 3:477/478 of 1jehA
- active site: L40 (= L40), C44 (= C44), C49 (= C49), S52 (= S52), I193 (≠ V186), E197 (= E190), T349 (≠ G340), H455 (= H446), H457 (= H448), E462 (= E453)
- binding flavin-adenine dinucleotide: I11 (= I11), G14 (= G14), P15 (= P15), A16 (≠ G16), V34 (≠ I34), E35 (= E35), K36 (= K36), R37 (= R37), G42 (= G42), T43 (= T43), C44 (= C44), G48 (= G48), C49 (= C49), K53 (= K53), G118 (= G117), T153 (= T146), G154 (= G147), I194 (= I187), R285 (= R276), Y288 (= Y279), L292 (= L283), G324 (= G315), D325 (= D316), M331 (= M322), L332 (= L323), A333 (= A324), H334 (= H325)
2qaeA Crystal structure analysis of trypanosoma cruzi lipoamide dehydrogenase
56% identity, 96% coverage: 20:468/469 of query aligns to 17:464/465 of 2qaeA
- active site: L37 (= L40), C41 (= C44), C46 (= C49), S49 (= S52), V184 (= V186), E188 (= E190), H442 (= H446), H444 (= H448), E449 (= E453)
- binding flavin-adenine dinucleotide: E32 (= E35), K33 (= K36), R34 (= R37), G39 (= G42), T40 (= T43), C41 (= C44), G45 (= G48), C46 (= C49), K50 (= K53), E114 (≠ A116), G115 (= G117), T144 (= T146), G145 (= G147), S164 (= S166), I185 (= I187), F274 (≠ Y279), G310 (= G315), D311 (= D316), M318 (= M322), L319 (= L323), A320 (= A324), H321 (= H325)
Sites not aligning to the query:
6aonA 1.72 angstrom resolution crystal structure of 2-oxoglutarate dehydrogenase complex subunit dihydrolipoamide dehydrogenase from bordetella pertussis in complex with fad
53% identity, 99% coverage: 5:468/469 of query aligns to 2:472/473 of 6aonA
- active site: P43 (≠ L40), C47 (= C44), C52 (= C49), S55 (= S52), V191 (= V186), E195 (= E190), H450 (= H446), H452 (= H448), E457 (= E453)
- binding calcium ion: A218 (≠ P213), A220 (≠ N215), Q222 (≠ G217)
- binding flavin-adenine dinucleotide: I8 (= I11), G11 (= G14), P12 (= P15), G13 (= G16), D32 (≠ E35), A33 (≠ K36), W34 (≠ R37), G45 (= G42), T46 (= T43), C47 (= C44), G51 (= G48), C52 (= C49), K56 (= K53), K119 (≠ A116), G120 (= G117), T151 (= T146), G152 (= G147), N171 (≠ S166), I192 (= I187), R280 (= R276), Y283 (= Y279), G319 (= G315), D320 (= D316), M326 (= M322), L327 (= L323), A328 (= A324), H329 (= H325)
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
53% identity, 99% coverage: 6:468/469 of query aligns to 2:454/455 of 2yquB
- active site: P11 (= P15), L36 (= L40), C40 (= C44), C45 (= C49), S48 (= S52), G72 (≠ K78), V73 (= V79), V177 (= V186), E181 (= E190), S314 (≠ E328), H432 (= H446), H434 (= H448), E439 (= E453)
- binding carbonate ion: A310 (= A324), S314 (≠ E328), S423 (≠ A437), D426 (= D440)
- binding flavin-adenine dinucleotide: G8 (= G12), G10 (= G14), P11 (= P15), G12 (= G16), E31 (= E35), K32 (= K36), G38 (= G42), T39 (= T43), C40 (= C44), R42 (≠ N46), G44 (= G48), C45 (= C49), K49 (= K53), T110 (≠ A116), A111 (≠ G117), T137 (= T146), G138 (= G147), I178 (= I187), Y265 (= Y279), G301 (= G315), D302 (= D316), M308 (= M322), L309 (= L323), A310 (= A324), H311 (= H325)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
53% identity, 99% coverage: 6:468/469 of query aligns to 2:454/455 of 2yquA
- active site: P11 (= P15), L36 (= L40), C40 (= C44), C45 (= C49), S48 (= S52), G72 (≠ K78), V73 (= V79), V177 (= V186), E181 (= E190), S314 (≠ E328), H432 (= H446), H434 (= H448), E439 (= E453)
- binding flavin-adenine dinucleotide: G8 (= G12), G10 (= G14), P11 (= P15), G12 (= G16), E31 (= E35), K32 (= K36), G38 (= G42), T39 (= T43), C40 (= C44), R42 (≠ N46), G44 (= G48), C45 (= C49), K49 (= K53), T110 (≠ A116), A111 (≠ G117), T137 (= T146), G138 (= G147), S157 (= S166), I178 (= I187), Y265 (= Y279), G301 (= G315), D302 (= D316), M308 (= M322), L309 (= L323), A310 (= A324)
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
53% identity, 98% coverage: 6:466/469 of query aligns to 2:452/452 of 2eq7A
- active site: P11 (= P15), L36 (= L40), C40 (= C44), C45 (= C49), S48 (= S52), G72 (≠ K78), V73 (= V79), V177 (= V186), E181 (= E190), S314 (≠ E328), H432 (= H446), H434 (= H448), E439 (= E453)
- binding flavin-adenine dinucleotide: G10 (= G14), P11 (= P15), G12 (= G16), E31 (= E35), K32 (= K36), G38 (= G42), T39 (= T43), C40 (= C44), R42 (≠ N46), G44 (= G48), C45 (= C49), K49 (= K53), T110 (≠ A116), A111 (≠ G117), T137 (= T146), G138 (= G147), S157 (= S166), I178 (= I187), R262 (= R276), Y265 (= Y279), D302 (= D316), M308 (= M322), L309 (= L323), A310 (= A324), H311 (= H325), Y341 (= Y355)
- binding nicotinamide-adenine-dinucleotide: W146 (≠ G155), G174 (= G183), G176 (= G185), V177 (= V186), I178 (= I187), E197 (= E206), Y198 (≠ F207), V231 (= V240), V260 (≠ I274), G261 (= G275), R262 (= R276), M308 (= M322), L309 (= L323), V339 (= V353)
P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 from Pseudomonas fluorescens (see 2 papers)
51% identity, 99% coverage: 6:468/469 of query aligns to 5:471/478 of P14218
- 34:49 (vs. 35:44, 44% identical) binding
- C49 (= C44) modified: Disulfide link with 54, Redox-active
- C54 (= C49) modified: Disulfide link with 49, Redox-active
- K58 (= K53) binding
- G122 (= G117) binding
- D319 (= D316) binding
- A327 (= A324) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
P18925 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Azotobacter vinelandii (see 2 papers)
51% identity, 99% coverage: 6:468/469 of query aligns to 5:471/477 of P18925
- 34:49 (vs. 35:44, 44% identical) binding
- C49 (= C44) modified: Disulfide link with 54, Redox-active
- C54 (= C49) modified: Disulfide link with 49, Redox-active
- K58 (= K53) binding
- D319 (= D316) binding
- A327 (= A324) binding
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
51% identity, 99% coverage: 6:468/469 of query aligns to 4:470/473 of 5u8wA
- active site: P13 (= P15), L44 (= L40), C48 (= C44), C53 (= C49), S56 (= S52), G82 (≠ K78), V83 (= V79), V190 (= V186), E194 (= E190), S330 (≠ E328), F448 (≠ H446), H450 (= H448), E455 (= E453)
- binding flavin-adenine dinucleotide: I9 (= I11), G12 (= G14), P13 (= P15), G14 (= G16), E33 (= E35), K34 (= K36), G46 (= G42), T47 (= T43), C48 (= C44), G52 (= G48), C53 (= C49), K57 (= K53), H120 (≠ A116), G121 (= G117), A149 (= A145), S150 (≠ T146), G151 (= G147), S170 (= S166), G317 (= G315), D318 (= D316), M324 (= M322), L325 (= L323), A326 (= A324), H327 (= H325), Y357 (= Y355), H450 (= H448), P451 (= P449)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (= I182), G189 (= G185), V190 (= V186), I191 (= I187), E194 (= E190), E210 (= E206), A211 (≠ F207), L212 (= L208), A275 (= A273), V276 (≠ I274), G277 (= G275), R278 (= R276), M324 (= M322), L325 (= L323), V355 (= V353), Y357 (= Y355)
Sites not aligning to the query:
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
51% identity, 99% coverage: 6:468/469 of query aligns to 7:473/477 of 5u8uD
- active site: P16 (= P15), L47 (= L40), C51 (= C44), C56 (= C49), S59 (= S52), G85 (≠ K78), V86 (= V79), V193 (= V186), E197 (= E190), S333 (≠ E328), F451 (≠ H446), H453 (= H448), E458 (= E453)
- binding flavin-adenine dinucleotide: I12 (= I11), G15 (= G14), P16 (= P15), G17 (= G16), E36 (= E35), K37 (= K36), G49 (= G42), T50 (= T43), C51 (= C44), G55 (= G48), C56 (= C49), K60 (= K53), H123 (≠ A116), G124 (= G117), A152 (= A145), S153 (≠ T146), G154 (= G147), I194 (= I187), R281 (= R276), G320 (= G315), D321 (= D316), M327 (= M322), L328 (= L323), A329 (= A324), H330 (= H325), H453 (= H448), P454 (= P449)
Sites not aligning to the query:
Query Sequence
>WP_011386317.1 NCBI__GCF_000009985.1:WP_011386317.1
MSDTSFDVVIIGGGPGGYVAAIRAAQLGLKTACIEKRGSLGGTCLNVGCIPSKALLTASH
HYHAAAHELGSFGIKVAKVEMDVAGMMGHKDKVVSDNTKGIEFLFKKNKVTYIVGAGAIT
APGQIEVTAKDGAKSNVAAKHIVIATGSDVTPLPGVEIDEEVIISSTGALALSKTPKHMV
VIGGGVIGLELGTVWGRLGAKVTVVEFLDRILPFNDGEVSKQMQRLLAKQGMEFKLGTKV
TGIAKKGKTATVTVEPAAGGAAEKIEADSVLVAIGRKPYTEGLGLDKVGVALDKRGFVQI
DGHFRTNVPGIYAIGDVVGGAMLAHKAEEEGVALAEILAGQHGHVNYEAIPAVVYTWPEV
ASVGKTEEQLKAEGIAYKAGKFPFTANGRARSMNEVDGFVKVLACATTDKVLGAHIVGPN
AGDLIAEVVLAMEFGAASEDIARTCHAHPGLGEAVKEACLAVDGRPLHT
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