SitesBLAST
Comparing SMc02487 FitnessBrowser__Smeli:SMc02487 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
100% identity, 99% coverage: 3:467/468 of query aligns to 1:465/465 of 3urhB
- active site: Y35 (= Y37), C39 (= C41), C44 (= C46), S47 (= S49), V183 (= V185), E187 (= E189), H443 (= H445), H445 (= H447), E450 (= E452)
- binding flavin-adenine dinucleotide: I6 (= I8), G7 (= G9), G9 (= G11), P10 (= P12), G11 (= G13), E30 (= E32), K31 (= K33), G37 (= G39), T38 (= T40), C39 (= C41), G43 (= G45), C44 (= C46), K48 (= K50), T111 (= T113), G112 (= G114), A140 (= A142), T141 (= T143), G142 (= G144), I184 (= I186), R273 (= R275), G312 (= G314), D313 (= D315), M319 (= M321), L320 (= L322), A321 (= A323), H322 (= H324)
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)
57% identity, 99% coverage: 4:468/468 of query aligns to 39:501/501 of P31023
- 67:76 (vs. 32:41, 70% identical) binding
- C76 (= C41) modified: Disulfide link with 81, Redox-active
- C81 (= C46) modified: Disulfide link with 76, Redox-active
- G149 (= G114) binding
- D348 (= D315) binding
- MLAH 354:357 (= MLAH 321:324) binding
Sites not aligning to the query:
- 1:31 modified: transit peptide, Mitochondrion
1dxlA Dihydrolipoamide dehydrogenase of glycine decarboxylase from pisum sativum (see paper)
57% identity, 99% coverage: 4:468/468 of query aligns to 5:467/467 of 1dxlA
- active site: L38 (≠ Y37), C42 (= C41), C47 (= C46), S50 (= S49), Y184 (≠ V185), E188 (= E189), H444 (= H445), H446 (= H447), E451 (= E452)
- binding flavin-adenine dinucleotide: I9 (= I8), P13 (= P12), G14 (= G13), E33 (= E32), K34 (= K33), R35 (= R34), G40 (= G39), T41 (= T40), C42 (= C41), G46 (= G45), C47 (= C46), K51 (= K50), Y114 (≠ T113), G115 (= G114), T144 (= T143), G145 (= G144), Y184 (≠ V185), I185 (= I186), R274 (= R275), D314 (= D315), M320 (= M321), L321 (= L322), A322 (= A323), H323 (= H324)
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
56% identity, 98% coverage: 4:463/468 of query aligns to 6:466/472 of 1zmdA
- active site: L39 (≠ Y37), C43 (= C41), C48 (= C46), S51 (= S49), V186 (= V185), E190 (= E189), H448 (= H445), H450 (= H447), E455 (= E452)
- binding flavin-adenine dinucleotide: I10 (= I8), G11 (= G9), G13 (= G11), P14 (= P12), G15 (= G13), E34 (= E32), K35 (= K33), N36 (≠ R34), G41 (= G39), T42 (= T40), C43 (= C41), G47 (= G45), C48 (= C46), K52 (= K50), Y116 (≠ T113), G117 (= G114), T146 (= T143), G147 (= G144), S166 (= S165), R278 (= R275), F281 (≠ S278), G317 (= G314), D318 (= D315), M324 (= M321), L325 (= L322), A326 (= A323), H327 (= H324)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (≠ V181), G183 (= G182), G185 (= G184), V186 (= V185), I187 (= I186), E190 (= E189), E206 (= E205), F207 (= F206), L208 (= L207), I276 (≠ T273), G277 (= G274), R278 (= R275), M324 (= M321), L325 (= L322), V355 (= V352), Y357 (= Y354)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
56% identity, 98% coverage: 4:463/468 of query aligns to 6:466/472 of 1zmcA
- active site: L39 (≠ Y37), C43 (= C41), C48 (= C46), S51 (= S49), V186 (= V185), E190 (= E189), H448 (= H445), H450 (= H447), E455 (= E452)
- binding flavin-adenine dinucleotide: I10 (= I8), G11 (= G9), G13 (= G11), P14 (= P12), G15 (= G13), E34 (= E32), K35 (= K33), N36 (≠ R34), G41 (= G39), T42 (= T40), C43 (= C41), G47 (= G45), C48 (= C46), K52 (= K50), Y116 (≠ T113), G117 (= G114), T146 (= T143), G147 (= G144), S166 (= S165), I187 (= I186), F281 (≠ S278), G317 (= G314), D318 (= D315), M324 (= M321), L325 (= L322), A326 (= A323), H327 (= H324)
- binding nicotinamide-adenine-dinucleotide: G183 (= G182), G185 (= G184), V205 (= V204), E206 (= E205), F207 (= F206), L208 (= L207), K240 (= K238), V241 (= V239), I276 (≠ T273), G277 (= G274), R278 (= R275), R297 (= R294), M324 (= M321)
P09622 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; EC 1.8.1.4 from Homo sapiens (Human) (see 14 papers)
56% identity, 98% coverage: 4:463/468 of query aligns to 43:503/509 of P09622
- 71:80 (vs. 32:41, 70% identical) binding
- K72 (= K33) to E: in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX; dbSNP:rs121964987
- K89 (= K50) binding ; mutation to E: Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- K104 (vs. gap) to T: in dbSNP:rs1130477
- G154 (= G114) binding
- TGS 183:185 (= TGS 143:145) binding
- 220:227 (vs. 182:189, 75% identical) binding
- E243 (= E205) binding
- V278 (= V239) binding
- G314 (= G274) binding
- D355 (= D315) binding
- MLAH 361:364 (= MLAH 321:324) binding
- E375 (= E335) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (= H343) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (= D408) 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 (= E426) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ F433) 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 (= D439) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (= R442) 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 (= H445) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
- P488 (= P448) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
- S491 (= S451) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
- E492 (= E452) mutation to Q: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- R495 (≠ K455) 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.
56% identity, 98% coverage: 4:463/468 of query aligns to 16:476/482 of 6hg8B
- active site: C53 (= C41), C58 (= C46), S61 (= S49), V196 (= V185), E200 (= E189), H460 (= H447), E465 (= E452)
- binding flavin-adenine dinucleotide: I20 (= I8), G23 (= G11), P24 (= P12), G25 (= G13), E44 (= E32), K45 (= K33), N46 (≠ R34), G51 (= G39), T52 (= T40), C53 (= C41), G57 (= G45), C58 (= C46), K62 (= K50), Y126 (≠ T113), G127 (= G114), T156 (= T143), G157 (= G144), I197 (= I186), R288 (= R275), F291 (≠ S278), G327 (= G314), D328 (= D315), M334 (= M321), L335 (= L322), A336 (= A323), H337 (= H324)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
55% identity, 100% coverage: 3:468/468 of query aligns to 7:470/470 of 6uziC
- active site: C45 (= C41), C50 (= C46), S53 (= S49), V187 (= V185), E191 (= E189), H448 (= H447), E453 (= E452)
- binding flavin-adenine dinucleotide: I12 (= I8), G13 (= G9), G15 (= G11), P16 (= P12), G17 (= G13), E36 (= E32), K37 (= K33), G43 (= G39), T44 (= T40), C45 (= C41), G49 (= G45), C50 (= C46), S53 (= S49), K54 (= K50), V117 (≠ T113), G118 (= G114), T147 (= T143), G148 (= G144), I188 (= I186), R276 (= R275), D316 (= D315), M322 (= M321), L323 (= L322), A324 (= A323)
- binding zinc ion: H448 (= H447), E453 (= E452)
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
55% identity, 100% coverage: 3:468/468 of query aligns to 2:455/455 of 2yquB
- active site: P11 (= P12), L36 (≠ Y37), C40 (= C41), C45 (= C46), S48 (= S49), G72 (≠ N75), V73 (≠ P76), V177 (= V185), E181 (= E189), S314 (≠ E327), H432 (= H445), H434 (= H447), E439 (= E452)
- binding carbonate ion: A310 (= A323), S314 (≠ E327), S423 (= S436), D426 (= D439)
- binding flavin-adenine dinucleotide: G8 (= G9), G10 (= G11), P11 (= P12), G12 (= G13), E31 (= E32), K32 (= K33), G38 (= G39), T39 (= T40), C40 (= C41), R42 (≠ N43), G44 (= G45), C45 (= C46), K49 (= K50), T110 (= T113), A111 (≠ G114), T137 (= T143), G138 (= G144), I178 (= I186), Y265 (≠ S278), G301 (= G314), D302 (= D315), M308 (= M321), L309 (= L322), A310 (= A323), H311 (= H324)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
55% identity, 100% coverage: 3:468/468 of query aligns to 2:455/455 of 2yquA
- active site: P11 (= P12), L36 (≠ Y37), C40 (= C41), C45 (= C46), S48 (= S49), G72 (≠ N75), V73 (≠ P76), V177 (= V185), E181 (= E189), S314 (≠ E327), H432 (= H445), H434 (= H447), E439 (= E452)
- binding flavin-adenine dinucleotide: G8 (= G9), G10 (= G11), P11 (= P12), G12 (= G13), E31 (= E32), K32 (= K33), G38 (= G39), T39 (= T40), C40 (= C41), R42 (≠ N43), G44 (= G45), C45 (= C46), K49 (= K50), T110 (= T113), A111 (≠ G114), T137 (= T143), G138 (= G144), S157 (= S165), I178 (= I186), Y265 (≠ S278), G301 (= G314), D302 (= D315), M308 (= M321), L309 (= L322), A310 (= A323)
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
54% identity, 99% coverage: 3:465/468 of query aligns to 2:452/452 of 2eq7A
- active site: P11 (= P12), L36 (≠ Y37), C40 (= C41), C45 (= C46), S48 (= S49), G72 (≠ N75), V73 (≠ P76), V177 (= V185), E181 (= E189), S314 (≠ E327), H432 (= H445), H434 (= H447), E439 (= E452)
- binding flavin-adenine dinucleotide: G10 (= G11), P11 (= P12), G12 (= G13), E31 (= E32), K32 (= K33), G38 (= G39), T39 (= T40), C40 (= C41), R42 (≠ N43), G44 (= G45), C45 (= C46), K49 (= K50), T110 (= T113), A111 (≠ G114), T137 (= T143), G138 (= G144), S157 (= S165), I178 (= I186), R262 (= R275), Y265 (≠ S278), D302 (= D315), M308 (= M321), L309 (= L322), A310 (= A323), H311 (= H324), Y341 (= Y354)
- binding nicotinamide-adenine-dinucleotide: W146 (≠ G152), G174 (= G182), G176 (= G184), V177 (= V185), I178 (= I186), E197 (= E205), Y198 (≠ F206), V231 (= V239), V260 (≠ T273), G261 (= G274), R262 (= R275), M308 (= M321), L309 (= L322), V339 (= V352)
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)
51% identity, 100% coverage: 2:467/468 of query aligns to 26:498/499 of P09624
- 56:65 (vs. 32:41, 70% identical) binding
- C65 (= C41) modified: Disulfide link with 70, Redox-active
- C70 (= C46) modified: Disulfide link with 65, Redox-active
- K74 (= K50) binding
- G139 (= G114) binding
- D346 (= D315) binding
- MLAH 352:355 (= MLAH 321:324) binding
- H478 (= H447) 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+
51% identity, 100% coverage: 2:467/468 of query aligns to 5:477/478 of 1v59A
- active site: L40 (≠ Y37), C44 (= C41), C49 (= C46), S52 (= S49), I193 (≠ V185), E197 (= E189), T349 (≠ G339), H455 (= H445), H457 (= H447), E462 (= E452)
- binding flavin-adenine dinucleotide: G14 (= G11), P15 (= P12), A16 (≠ G13), E35 (= E32), K36 (= K33), R37 (= R34), G42 (= G39), T43 (= T40), C44 (= C41), G48 (= G45), C49 (= C46), K53 (= K50), N117 (≠ T113), G118 (= G114), T153 (= T143), G154 (= G144), R285 (= R275), Y288 (≠ S278), G324 (= G314), D325 (= D315), M331 (= M321), L332 (= L322), A333 (= A323), H334 (= H324), Y364 (= Y354)
- binding nicotinamide-adenine-dinucleotide: I189 (≠ V181), G190 (= G182), E213 (= E205), F214 (= F206), K246 (= K238), V283 (≠ T273)
1jehA Crystal structure of yeast e3, lipoamide dehydrogenase (see paper)
51% identity, 100% coverage: 2:467/468 of query aligns to 5:477/478 of 1jehA
- active site: L40 (≠ Y37), C44 (= C41), C49 (= C46), S52 (= S49), I193 (≠ V185), E197 (= E189), T349 (≠ G339), H455 (= H445), H457 (= H447), E462 (= E452)
- binding flavin-adenine dinucleotide: I11 (= I8), G14 (= G11), P15 (= P12), A16 (≠ G13), V34 (= V31), E35 (= E32), K36 (= K33), R37 (= R34), G42 (= G39), T43 (= T40), C44 (= C41), G48 (= G45), C49 (= C46), K53 (= K50), G118 (= G114), T153 (= T143), G154 (= G144), I194 (= I186), R285 (= R275), Y288 (≠ S278), L292 (= L282), G324 (= G314), D325 (= D315), M331 (= M321), L332 (= L322), A333 (= A323), H334 (= H324)
2qaeA Crystal structure analysis of trypanosoma cruzi lipoamide dehydrogenase
54% identity, 96% coverage: 18:468/468 of query aligns to 18:465/465 of 2qaeA
- active site: L37 (≠ Y37), C41 (= C41), C46 (= C46), S49 (= S49), V184 (= V185), E188 (= E189), H442 (= H445), H444 (= H447), E449 (= E452)
- binding flavin-adenine dinucleotide: E32 (= E32), K33 (= K33), R34 (= R34), G39 (= G39), T40 (= T40), C41 (= C41), G45 (= G45), C46 (= C46), K50 (= K50), E114 (≠ T113), G115 (= G114), T144 (= T143), G145 (= G144), S164 (= S165), I185 (= I186), F274 (≠ S278), G310 (= G314), D311 (= D315), M318 (= M321), L319 (= L322), A320 (= A323), H321 (= H324)
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)
51% identity, 100% coverage: 3:468/468 of query aligns to 5:472/477 of P18925
- 34:49 (vs. 32:41, 38% identical) binding
- C49 (= C41) modified: Disulfide link with 54, Redox-active
- C54 (= C46) modified: Disulfide link with 49, Redox-active
- K58 (= K50) binding
- D319 (= D315) binding
- A327 (= A323) binding
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, 100% coverage: 3:468/468 of query aligns to 5:472/478 of P14218
- 34:49 (vs. 32:41, 38% identical) binding
- C49 (= C41) modified: Disulfide link with 54, Redox-active
- C54 (= C46) modified: Disulfide link with 49, Redox-active
- K58 (= K50) binding
- G122 (= G114) binding
- D319 (= D315) binding
- A327 (= A323) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
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)
51% identity, 100% coverage: 3:468/468 of query aligns to 4:471/472 of 3ladA
- active site: L44 (≠ Y37), C48 (= C41), C53 (= C46), S56 (= S49), V190 (= V185), E194 (= E189), F448 (≠ H445), H450 (= H447), E455 (= E452)
- binding flavin-adenine dinucleotide: I9 (= I8), G10 (= G9), G12 (= G11), P13 (= P12), E33 (= E32), K34 (= K33), G46 (= G39), T47 (= T40), C48 (= C41), G52 (= G45), C53 (= C46), H120 (≠ T113), G121 (= G114), A149 (= A142), S150 (≠ T143), G151 (= G144), I191 (= I186), R278 (= R275), D318 (= D315), L325 (= L322), A326 (= A323)
6awaA 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from pseudomonas putida in complex with fad and adenosine-5'-monophosphate.
51% identity, 100% coverage: 3:468/468 of query aligns to 5:472/475 of 6awaA
- active site: L45 (≠ Y37), C49 (= C41), C54 (= C46), S57 (= S49), V191 (= V185), E195 (= E189), F449 (≠ H445), H451 (= H447), E456 (= E452)
- binding adenosine monophosphate: I187 (≠ V181), E211 (= E205), A212 (≠ F206), L213 (= L207), V245 (= V239), V277 (≠ T273)
- binding flavin-adenine dinucleotide: I10 (= I8), G13 (= G11), P14 (= P12), G15 (= G13), E34 (= E32), K35 (= K33), T48 (= T40), C49 (= C41), G53 (= G45), C54 (= C46), K58 (= K50), H121 (≠ T113), G122 (= G114), S151 (≠ T143), G152 (= G144), I192 (= I186), R279 (= R275), G318 (= G314), D319 (= D315), M325 (= M321), L326 (= L322), A327 (= A323), Y358 (= Y354)
Sites not aligning to the query:
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
51% identity, 100% coverage: 3:468/468 of query aligns to 4:471/473 of 5u8wA
- active site: P13 (= P12), L44 (≠ Y37), C48 (= C41), C53 (= C46), S56 (= S49), G82 (≠ N75), V83 (≠ P76), V190 (= V185), E194 (= E189), S330 (≠ E327), F448 (≠ H445), H450 (= H447), E455 (= E452)
- binding flavin-adenine dinucleotide: I9 (= I8), G12 (= G11), P13 (= P12), G14 (= G13), E33 (= E32), K34 (= K33), G46 (= G39), T47 (= T40), C48 (= C41), G52 (= G45), C53 (= C46), K57 (= K50), H120 (≠ T113), G121 (= G114), A149 (= A142), S150 (≠ T143), G151 (= G144), S170 (= S165), G317 (= G314), D318 (= D315), M324 (= M321), L325 (= L322), A326 (= A323), H327 (= H324), Y357 (= Y354), H450 (= H447), P451 (= P448)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (≠ V181), G189 (= G184), V190 (= V185), I191 (= I186), E194 (= E189), E210 (= E205), A211 (≠ F206), L212 (= L207), A275 (= A272), V276 (≠ T273), G277 (= G274), R278 (= R275), M324 (= M321), L325 (= L322), V355 (= V352), Y357 (= Y354)
Sites not aligning to the query:
Query Sequence
>SMc02487 FitnessBrowser__Smeli:SMc02487
MAYDLIVIGSGPGGYVCAIKAAQLGMKVAVVEKRSTYGGTCLNVGCIPSKALLHASEMFH
QAQHGLEALGVEVANPKLNLQKMMAHKDATVKSNVDGVSFLFKKNKIDGFQGTGKVLGQG
KVSVTNEKGEEQVLEAKNVVIATGSDVAGIPGVEVAFDEKTIVSSTGALALEKVPASMIV
VGGGVIGLELGSVWARLGAKVTVVEFLDTILGGMDGEVAKQLQRMLTKQGIDFKLGAKVT
GAVKSGDGAKVTFEPVKGGEATTLDAEVVLIATGRKPSTDGLGLAKAGVVLDSRGRVEID
RHFQTSIAGVYAIGDVVRGPMLAHKAEDEGVAVAEIIAGQAGHVNYDVIPGVVYTQPEVA
SVGKTEEELKAAGVAYKIGKFPFTANGRARAMLQTDGFVKILADKETDRVLGGHIIGFGA
GEMIHEIAVLMEFGGSSEDLGRTCHAHPTMSEAVKEAALSTFFKPIHM
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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