SitesBLAST
Comparing AZOBR_RS03960 FitnessBrowser__azobra:AZOBR_RS03960 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: 6:465/466 of query aligns to 1:465/465 of 3urhB
- active site: Y35 (≠ L40), C39 (= C44), C44 (= C49), S47 (= S52), V183 (= V183), E187 (= E187), H443 (= H443), H445 (= H445), E450 (= E450)
- binding flavin-adenine dinucleotide: I6 (≠ V11), 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 (= A142), T141 (= T143), G142 (= G144), I184 (= I184), R273 (= R273), G312 (= G312), D313 (= D313), M319 (= M319), L320 (= L320), A321 (= A321), H322 (= H322)
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)
61% identity, 99% coverage: 7:466/466 of query aligns to 39:501/501 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 (= D313) binding
- MLAH 354:357 (= MLAH 319:322) binding
Sites not aligning to the query:
- 1:31 modified: transit peptide, Mitochondrion
1dxlA Dihydrolipoamide dehydrogenase of glycine decarboxylase from pisum sativum (see paper)
61% identity, 99% coverage: 7:466/466 of query aligns to 5:467/467 of 1dxlA
- active site: L38 (= L40), C42 (= C44), C47 (= C49), S50 (= S52), Y184 (≠ V183), E188 (= E187), H444 (= H443), H446 (= H445), E451 (= E450)
- binding flavin-adenine dinucleotide: I9 (≠ V11), 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 (= T143), G145 (= G144), Y184 (≠ V183), I185 (= I184), R274 (= R273), D314 (= D313), M320 (= M319), L321 (= L320), A322 (= A321), H323 (= H322)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
57% identity, 99% coverage: 4:466/466 of query aligns to 5:470/470 of 6uziC
- active site: C45 (= C44), C50 (= C49), S53 (= S52), V187 (= V183), E191 (= E187), H448 (= H445), E453 (= E450)
- binding flavin-adenine dinucleotide: I12 (≠ V11), 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 (= T143), G148 (= G144), I188 (= I184), R276 (= R273), D316 (= D313), M322 (= M319), L323 (= L320), A324 (= A321)
- binding zinc ion: H448 (= H445), E453 (= E450)
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
57% identity, 99% coverage: 6:466/466 of query aligns to 2:455/455 of 2yquB
- active site: P11 (= P15), L36 (= L40), C40 (= C44), C45 (= C49), S48 (= S52), G72 (= G78), V73 (= V79), V177 (= V183), E181 (= E187), S314 (≠ E325), H432 (= H443), H434 (= H445), E439 (= E450)
- binding carbonate ion: A310 (= A321), S314 (≠ E325), S423 (= S434), D426 (= D437)
- 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 (= T143), G138 (= G144), I178 (= I184), Y265 (≠ F276), G301 (= G312), D302 (= D313), M308 (= M319), L309 (= L320), A310 (= A321), H311 (= H322)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
57% identity, 99% coverage: 6:466/466 of query aligns to 2:455/455 of 2yquA
- active site: P11 (= P15), L36 (= L40), C40 (= C44), C45 (= C49), S48 (= S52), G72 (= G78), V73 (= V79), V177 (= V183), E181 (= E187), S314 (≠ E325), H432 (= H443), H434 (= H445), E439 (= E450)
- 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 (= T143), G138 (= G144), S157 (= S163), I178 (= I184), Y265 (≠ F276), G301 (= G312), D302 (= D313), M308 (= M319), L309 (= L320), A310 (= A321)
P09622 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; EC 1.8.1.4 from Homo sapiens (Human) (see 14 papers)
58% identity, 97% coverage: 7:458/466 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 (vs. gap) to T: in dbSNP:rs1130477
- G154 (= G117) binding
- TGS 183:185 (= TGS 143:145) binding
- 220:227 (vs. 180:187, 75% identical) binding
- E243 (= E203) binding
- V278 (= V237) binding
- G314 (= G272) binding
- D355 (= D313) binding
- MLAH 361:364 (= MLAH 319:322) binding
- E375 (= E333) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (= H341) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (= D406) 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 (= E424) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ F431) 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 (= D437) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (= R440) 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 (= H443) 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.
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
58% identity, 97% coverage: 6:458/466 of query aligns to 2:447/452 of 2eq7A
- active site: P11 (= P15), L36 (= L40), C40 (= C44), C45 (= C49), S48 (= S52), G72 (= G78), V73 (= V79), V177 (= V183), E181 (= E187), S314 (≠ E325), H432 (= H443), H434 (= H445), E439 (= E450)
- 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 (= T143), G138 (= G144), S157 (= S163), I178 (= I184), R262 (= R273), Y265 (≠ F276), D302 (= D313), M308 (= M319), L309 (= L320), A310 (= A321), H311 (= H322), Y341 (= Y352)
- binding nicotinamide-adenine-dinucleotide: W146 (≠ G152), G174 (= G180), G176 (= G182), V177 (= V183), I178 (= I184), E197 (= E203), Y198 (≠ F204), V231 (= V237), V260 (≠ I271), G261 (= G272), R262 (= R273), M308 (= M319), L309 (= L320), V339 (= V350)
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
58% identity, 97% coverage: 7:458/466 of query aligns to 6:463/472 of 1zmdA
- active site: L39 (= L40), C43 (= C44), C48 (= C49), S51 (= S52), V186 (= V183), E190 (= E187), H448 (= H443), H450 (= H445), E455 (= E450)
- binding flavin-adenine dinucleotide: I10 (≠ V11), 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 (= T143), G147 (= G144), S166 (= S163), R278 (= R273), F281 (= F276), G317 (= G312), D318 (= D313), M324 (= M319), L325 (= L320), A326 (= A321), H327 (= H322)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (= I179), G183 (= G180), G185 (= G182), V186 (= V183), I187 (= I184), E190 (= E187), E206 (= E203), F207 (= F204), L208 (= L205), I276 (= I271), G277 (= G272), R278 (= R273), M324 (= M319), L325 (= L320), V355 (= V350), Y357 (= Y352)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
58% identity, 97% coverage: 7:458/466 of query aligns to 6:463/472 of 1zmcA
- active site: L39 (= L40), C43 (= C44), C48 (= C49), S51 (= S52), V186 (= V183), E190 (= E187), H448 (= H443), H450 (= H445), E455 (= E450)
- binding flavin-adenine dinucleotide: I10 (≠ V11), 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 (= T143), G147 (= G144), S166 (= S163), I187 (= I184), F281 (= F276), G317 (= G312), D318 (= D313), M324 (= M319), L325 (= L320), A326 (= A321), H327 (= H322)
- binding nicotinamide-adenine-dinucleotide: G183 (= G180), G185 (= G182), V205 (= V202), E206 (= E203), F207 (= F204), L208 (= L205), K240 (= K236), V241 (= V237), I276 (= I271), G277 (= G272), R278 (= R273), R297 (= R292), M324 (= M319)
6hg8B Crystal structure of the r460g disease-causing mutant of the human dihydrolipoamide dehydrogenase.
58% identity, 97% coverage: 7:458/466 of query aligns to 16:473/482 of 6hg8B
- active site: C53 (= C44), C58 (= C49), S61 (= S52), V196 (= V183), E200 (= E187), H460 (= H445), E465 (= E450)
- binding flavin-adenine dinucleotide: I20 (≠ V11), 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 (= T143), G157 (= G144), I197 (= I184), R288 (= R273), F291 (= F276), G327 (= G312), D328 (= D313), M334 (= M319), L335 (= L320), A336 (= A321), H337 (= H322)
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: 5:465/466 of query aligns to 26:498/499 of P09624
- 56:65 (vs. 35:44, 80% 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 (= D313) binding
- MLAH 352:355 (= MLAH 319:322) binding
- H478 (= H445) 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: 5:465/466 of query aligns to 5:477/478 of 1v59A
- active site: L40 (= L40), C44 (= C44), C49 (= C49), S52 (= S52), I193 (≠ V183), E197 (= E187), T349 (≠ G337), H455 (= H443), H457 (= H445), E462 (= E450)
- 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 (= T143), G154 (= G144), R285 (= R273), Y288 (≠ F276), G324 (= G312), D325 (= D313), M331 (= M319), L332 (= L320), A333 (= A321), H334 (= H322), Y364 (= Y352)
- binding nicotinamide-adenine-dinucleotide: I189 (= I179), G190 (= G180), E213 (= E203), F214 (= F204), K246 (= K236), V283 (≠ I271)
1jehA Crystal structure of yeast e3, lipoamide dehydrogenase (see paper)
55% identity, 99% coverage: 5:465/466 of query aligns to 5:477/478 of 1jehA
- active site: L40 (= L40), C44 (= C44), C49 (= C49), S52 (= S52), I193 (≠ V183), E197 (= E187), T349 (≠ G337), H455 (= H443), H457 (= H445), E462 (= E450)
- binding flavin-adenine dinucleotide: I11 (≠ V11), G14 (= G14), P15 (= P15), A16 (≠ G16), V34 (= V34), E35 (= E35), K36 (= K36), R37 (= R37), G42 (= G42), T43 (= T43), C44 (= C44), G48 (= G48), C49 (= C49), K53 (= K53), G118 (= G117), T153 (= T143), G154 (= G144), I194 (= I184), R285 (= R273), Y288 (≠ F276), L292 (= L280), G324 (= G312), D325 (= D313), M331 (= M319), L332 (= L320), A333 (= A321), H334 (= H322)
2qaeA Crystal structure analysis of trypanosoma cruzi lipoamide dehydrogenase
54% identity, 96% coverage: 21:466/466 of query aligns to 18:465/465 of 2qaeA
- active site: L37 (= L40), C41 (= C44), C46 (= C49), S49 (= S52), V184 (= V183), E188 (= E187), H442 (= H443), H444 (= H445), E449 (= E450)
- 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 (= T143), G145 (= G144), S164 (= S163), I185 (= I184), F274 (= F276), G310 (= G312), D311 (= D313), M318 (= M319), L319 (= L320), A320 (= A321), H321 (= H322)
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: 6:466/466 of query aligns to 3:473/473 of 6aonA
- active site: P43 (≠ L40), C47 (= C44), C52 (= C49), S55 (= S52), V191 (= V183), E195 (= E187), H450 (= H443), H452 (= H445), E457 (= E450)
- binding calcium ion: A218 (≠ P210), A220 (≠ M212), Q222 (≠ G214)
- binding flavin-adenine dinucleotide: I8 (≠ V11), 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 (vs. gap), G120 (vs. gap), T151 (= T143), G152 (= G144), N171 (≠ S163), I192 (= I184), R280 (= R273), Y283 (≠ F276), G319 (= G312), D320 (= D313), M326 (= M319), L327 (= L320), A328 (= A321), H329 (= H322)
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
52% identity, 99% coverage: 6:466/466 of query aligns to 3:470/472 of 5u8vA
- active site: P12 (= P15), L43 (= L40), C47 (= C44), C52 (= C49), S55 (= S52), G81 (= G78), V82 (= V79), V189 (= V183), E193 (= E187), S329 (≠ E325), F447 (≠ H443), H449 (= H445), E454 (= E450)
- binding flavin-adenine dinucleotide: I8 (≠ V11), G11 (= G14), P12 (= P15), G13 (= G16), E32 (= E35), G45 (= G42), T46 (= T43), C47 (= C44), G51 (= G48), C52 (= C49), K56 (= K53), H119 (≠ A116), G120 (= G117), A148 (= A142), S149 (≠ T143), G150 (= G144), S169 (= S163), I190 (= I184), R277 (= R273), G316 (= G312), D317 (= D313), M323 (= M319), L324 (= L320), A325 (= A321), H326 (= H322), H449 (= H445), P450 (= P446)
- binding nicotinamide-adenine-dinucleotide: I185 (= I179), G186 (= G180), G188 (= G182), V189 (= V183), I190 (= I184), L208 (≠ V202), E209 (= E203), A210 (≠ F204), V243 (= V237), V275 (≠ I271), G276 (= G272)
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)
52% identity, 99% coverage: 6:466/466 of query aligns to 5:472/478 of P14218
- 34:49 (vs. 35:44, 50% 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 (= D313) binding
- A327 (= A321) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
52% identity, 99% coverage: 6:466/466 of query aligns to 4:471/473 of 5u8wA
- active site: P13 (= P15), L44 (= L40), C48 (= C44), C53 (= C49), S56 (= S52), G82 (= G78), V83 (= V79), V190 (= V183), E194 (= E187), S330 (≠ E325), F448 (≠ H443), H450 (= H445), E455 (= E450)
- binding flavin-adenine dinucleotide: I9 (≠ V11), 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 (= A142), S150 (≠ T143), G151 (= G144), S170 (= S163), G317 (= G312), D318 (= D313), M324 (= M319), L325 (= L320), A326 (= A321), H327 (= H322), Y357 (= Y352), H450 (= H445), P451 (= P446)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (= I179), G189 (= G182), V190 (= V183), I191 (= I184), E194 (= E187), E210 (= E203), A211 (≠ F204), L212 (= L205), A275 (= A270), V276 (≠ I271), G277 (= G272), R278 (= R273), M324 (= M319), L325 (= L320), V355 (= V350), Y357 (= Y352)
Sites not aligning to the query:
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
52% identity, 99% coverage: 6:466/466 of query aligns to 7:474/477 of 5u8uD
- active site: P16 (= P15), L47 (= L40), C51 (= C44), C56 (= C49), S59 (= S52), G85 (= G78), V86 (= V79), V193 (= V183), E197 (= E187), S333 (≠ E325), F451 (≠ H443), H453 (= H445), E458 (= E450)
- binding flavin-adenine dinucleotide: I12 (≠ V11), 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 (= A142), S153 (≠ T143), G154 (= G144), I194 (= I184), R281 (= R273), G320 (= G312), D321 (= D313), M327 (= M319), L328 (= L320), A329 (= A321), H330 (= H322), H453 (= H445), P454 (= P446)
Sites not aligning to the query:
Query Sequence
>AZOBR_RS03960 FitnessBrowser__azobra:AZOBR_RS03960
MAESTFDVVVVGGGPGGYVCAIRAAQLGFKVACVEKRSALGGTCLNVGCIPSKALLAASE
KYEEAKHGLAKFGIKVDGVELDLPGMLSHKDKVVKENTGGIEFLFKKNKIAWLKGAGRIT
APNTVEVEGVGTITASKAIVIATGSEVTPLPGIEIDEQKIVSSTGALELPEVPKRLVVIG
GGVIGLELGSVWGRLGAEVTVVEFLDRILPTMDGEVSKQMQRILGKQGMTFKLGSKVTGA
KVTNTGVTLSVEPAAGGTAEEIKADVVLVAIGRRAFTNGLGLDAVGVEMDNRGRVKIGKH
FETNVPGIYAIGDVVEGPMLAHKAEEEGVALAELLAGQAGHVNHDLVPGVVYTWPEVAAV
GKTEEELKAAGTAYKAGKFPFTANGRARASGTTDGFVKILADARTDKVLGVHMVGPNVSE
MVAELAVAMEFSASAEDIARTCHAHPTLSEVTKEAALAVDGRALHI
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