SitesBLAST
Comparing GFF1504 FitnessBrowser__WCS417:GFF1504 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
32% identity, 97% coverage: 6:456/464 of query aligns to 1:456/465 of 3urhB
- active site: Y35 (≠ V40), C39 (= C44), C44 (≠ T49), S47 (= S52), V183 (= V185), E187 (= E189), H443 (≠ F443), H445 (≠ Y445), E450 (= E450)
- binding flavin-adenine dinucleotide: I6 (≠ L11), G7 (= G12), G9 (= G14), P10 (= P15), G11 (≠ A16), E30 (≠ D35), K31 (≠ S36), G37 (= G42), T38 (≠ N43), C39 (= C44), G43 (= G48), C44 (≠ T49), K48 (= K53), T111 (= T115), G112 (= G116), A140 (= A144), T141 (= T145), G142 (= G146), I184 (= I186), R273 (= R270), G312 (= G309), D313 (= D310), M319 (≠ S316), L320 (= L317), A321 (= A318), H322 (≠ S319)
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
33% identity, 89% coverage: 6:419/464 of query aligns to 2:411/452 of 2eq7A
- active site: P11 (= P15), L36 (≠ V40), C40 (= C44), C45 (≠ T49), S48 (= S52), G72 (≠ P77), V73 (≠ R78), V177 (= V185), E181 (= E189), S314 (≠ H322)
- binding flavin-adenine dinucleotide: G10 (= G14), P11 (= P15), G12 (≠ A16), E31 (≠ D35), K32 (≠ S36), G38 (= G42), T39 (≠ N43), C40 (= C44), R42 (≠ H46), G44 (= G48), C45 (≠ T49), K49 (= K53), T110 (= T115), A111 (≠ G116), T137 (= T145), G138 (= G146), S157 (= S165), I178 (= I186), R262 (= R270), Y265 (≠ N273), D302 (= D310), M308 (≠ S316), L309 (= L317), A310 (= A318), H311 (≠ S319), Y341 (= Y349)
- binding nicotinamide-adenine-dinucleotide: W146 (≠ D154), G174 (= G182), G176 (= G184), V177 (= V185), I178 (= I186), E197 (≠ D205), Y198 (≠ N206), V231 (≠ Y239), V260 (≠ N268), G261 (= G269), R262 (= R270), M308 (≠ S316), L309 (= L317), V339 (≠ G347)
Sites not aligning to the query:
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
33% identity, 89% coverage: 6:419/464 of query aligns to 2:411/455 of 2yquB
- active site: P11 (= P15), L36 (≠ V40), C40 (= C44), C45 (≠ T49), S48 (= S52), G72 (≠ P77), V73 (≠ R78), V177 (= V185), E181 (= E189), S314 (≠ H322)
- binding carbonate ion: A310 (= A318), S314 (≠ H322)
- binding flavin-adenine dinucleotide: G8 (= G12), G10 (= G14), P11 (= P15), G12 (≠ A16), E31 (≠ D35), K32 (≠ S36), G38 (= G42), T39 (≠ N43), C40 (= C44), R42 (≠ H46), G44 (= G48), C45 (≠ T49), K49 (= K53), T110 (= T115), A111 (≠ G116), T137 (= T145), G138 (= G146), I178 (= I186), Y265 (≠ N273), G301 (= G309), D302 (= D310), M308 (≠ S316), L309 (= L317), A310 (= A318), H311 (≠ S319)
Sites not aligning to the query:
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
33% identity, 89% coverage: 6:419/464 of query aligns to 2:411/455 of 2yquA
- active site: P11 (= P15), L36 (≠ V40), C40 (= C44), C45 (≠ T49), S48 (= S52), G72 (≠ P77), V73 (≠ R78), V177 (= V185), E181 (= E189), S314 (≠ H322)
- binding flavin-adenine dinucleotide: G8 (= G12), G10 (= G14), P11 (= P15), G12 (≠ A16), E31 (≠ D35), K32 (≠ S36), G38 (= G42), T39 (≠ N43), C40 (= C44), R42 (≠ H46), G44 (= G48), C45 (≠ T49), K49 (= K53), T110 (= T115), A111 (≠ G116), T137 (= T145), G138 (= G146), S157 (= S165), I178 (= I186), Y265 (≠ N273), G301 (= G309), D302 (= D310), M308 (≠ S316), L309 (= L317), A310 (= A318)
Sites not aligning to the query:
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
30% identity, 99% coverage: 5:462/464 of query aligns to 6:465/470 of 6uziC
- active site: C45 (= C44), C50 (≠ T49), S53 (= S52), V187 (= V185), E191 (= E189), H448 (≠ Y445), E453 (= E450)
- binding flavin-adenine dinucleotide: I12 (≠ L11), G13 (= G12), G15 (= G14), P16 (= P15), G17 (≠ A16), E36 (≠ D35), K37 (≠ S36), G43 (= G42), T44 (≠ N43), C45 (= C44), G49 (= G48), C50 (≠ T49), S53 (= S52), K54 (= K53), V117 (≠ T115), G118 (= G116), T147 (= T145), G148 (= G146), I188 (= I186), R276 (= R270), D316 (= D310), M322 (≠ S316), L323 (= L317), A324 (= A318)
- binding zinc ion: H448 (≠ Y445), E453 (= E450)
6aonA 1.72 angstrom resolution crystal structure of 2-oxoglutarate dehydrogenase complex subunit dihydrolipoamide dehydrogenase from bordetella pertussis in complex with fad
32% identity, 97% coverage: 5:456/464 of query aligns to 2:463/473 of 6aonA
- active site: P43 (≠ V40), C47 (= C44), C52 (≠ T49), S55 (= S52), V191 (= V185), E195 (= E189), H450 (≠ N440), H452 (≠ Y445), E457 (= E450)
- binding calcium ion: A218 (≠ S212), A220 (≠ L214), Q222 (≠ S216)
- binding flavin-adenine dinucleotide: I8 (≠ L11), G11 (= G14), P12 (= P15), G13 (≠ A16), D32 (= D35), A33 (≠ S36), W34 (≠ R37), G45 (= G42), T46 (≠ N43), C47 (= C44), G51 (= G48), C52 (≠ T49), K56 (= K53), K119 (≠ T115), G120 (= G116), T151 (= T145), G152 (= G146), N171 (≠ S165), I192 (= I186), R280 (= R270), Y283 (≠ N273), G319 (= G309), D320 (= D310), M326 (≠ S316), L327 (= L317), A328 (= A318), H329 (≠ S319)
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
31% identity, 97% coverage: 7:456/464 of query aligns to 5:451/455 of 1ebdA
- active site: P13 (= P15), L37 (≠ V40), C41 (= C44), C46 (≠ T49), S49 (= S52), N74 (≠ P77), V75 (≠ R78), Y180 (≠ V185), E184 (= E189), S320 (≠ H322), H438 (≠ F443), H440 (≠ Y445), E445 (= E450)
- binding flavin-adenine dinucleotide: G10 (= G12), G12 (= G14), P13 (= P15), V32 (= V34), E33 (≠ D35), K34 (≠ R37), G39 (= G42), V40 (≠ N43), C41 (= C44), G45 (= G48), C46 (≠ T49), K50 (= K53), E112 (≠ T115), A113 (≠ G116), T141 (= T145), G142 (= G146), Y180 (≠ V185), I181 (= I186), R268 (= R270), D308 (= D310), A314 (≠ S316), L315 (= L317), A316 (= A318)
P11959 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
31% identity, 97% coverage: 7:456/464 of query aligns to 11:457/470 of P11959
- 39:47 (vs. 35:44, 30% identical) binding
- K56 (= K53) binding
- D314 (= D310) binding
- A322 (= A318) binding
1v59A Crystal structure of yeast lipoamide dehydrogenase complexed with NAD+
30% identity, 98% coverage: 5:458/464 of query aligns to 5:473/478 of 1v59A
- active site: L40 (≠ V40), C44 (= C44), C49 (≠ T49), S52 (= S52), I193 (≠ V185), E197 (= E189), T349 (≠ D334), H455 (≠ N440), H457 (≠ Y445), E462 (= E450)
- binding flavin-adenine dinucleotide: G14 (= G14), P15 (= P15), A16 (= A16), E35 (≠ D35), K36 (≠ S36), R37 (= R37), G42 (= G42), T43 (≠ N43), C44 (= C44), G48 (= G48), C49 (≠ T49), K53 (= K53), N117 (≠ T115), G118 (= G116), T153 (= T145), G154 (= G146), R285 (= R270), Y288 (≠ N273), G324 (= G309), D325 (= D310), M331 (≠ S316), L332 (= L317), A333 (= A318), H334 (≠ S319), Y364 (= Y349)
- binding nicotinamide-adenine-dinucleotide: I189 (≠ Y181), G190 (= G182), E213 (≠ D205), F214 (≠ N206), K246 (≠ N229), V283 (≠ N268)
1jehA Crystal structure of yeast e3, lipoamide dehydrogenase (see paper)
30% identity, 98% coverage: 5:458/464 of query aligns to 5:473/478 of 1jehA
- active site: L40 (≠ V40), C44 (= C44), C49 (≠ T49), S52 (= S52), I193 (≠ V185), E197 (= E189), T349 (≠ D334), H455 (≠ N440), H457 (≠ Y445), E462 (= E450)
- binding flavin-adenine dinucleotide: I11 (≠ L11), G14 (= G14), P15 (= P15), A16 (= A16), V34 (= V34), E35 (≠ D35), K36 (≠ S36), R37 (= R37), G42 (= G42), T43 (≠ N43), C44 (= C44), G48 (= G48), C49 (≠ T49), K53 (= K53), G118 (= G116), T153 (= T145), G154 (= G146), I194 (= I186), R285 (= R270), Y288 (≠ N273), L292 (= L277), G324 (= G309), D325 (= D310), M331 (≠ S316), L332 (= L317), A333 (= A318), H334 (≠ S319)
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
30% identity, 97% coverage: 5:455/464 of query aligns to 4:460/472 of 1zmdA
- active site: L39 (≠ V40), C43 (= C44), C48 (≠ T49), S51 (= S52), V186 (= V185), E190 (= E189), H448 (≠ N440), H450 (≠ Y445), E455 (= E450)
- binding flavin-adenine dinucleotide: I10 (≠ L11), G11 (= G12), G13 (= G14), P14 (= P15), G15 (≠ A16), E34 (≠ D35), K35 (≠ S36), N36 (≠ R37), G41 (= G42), T42 (≠ N43), C43 (= C44), G47 (= G48), C48 (≠ T49), K52 (= K53), Y116 (≠ T115), G117 (= G116), T146 (= T145), G147 (= G146), S166 (= S165), R278 (= R270), F281 (≠ N273), G317 (= G309), D318 (= D310), M324 (≠ S316), L325 (= L317), A326 (= A318), H327 (≠ S319)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (≠ Y181), G183 (= G182), G185 (= G184), V186 (= V185), I187 (= I186), E190 (= E189), E206 (≠ D205), F207 (≠ N206), L208 (≠ R207), I276 (≠ N268), G277 (= G269), R278 (= R270), M324 (≠ S316), L325 (= L317), V355 (≠ G347), Y357 (= Y349)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
30% identity, 97% coverage: 5:455/464 of query aligns to 4:460/472 of 1zmcA
- active site: L39 (≠ V40), C43 (= C44), C48 (≠ T49), S51 (= S52), V186 (= V185), E190 (= E189), H448 (≠ N440), H450 (≠ Y445), E455 (= E450)
- binding flavin-adenine dinucleotide: I10 (≠ L11), G11 (= G12), G13 (= G14), P14 (= P15), G15 (≠ A16), E34 (≠ D35), K35 (≠ S36), N36 (≠ R37), G41 (= G42), T42 (≠ N43), C43 (= C44), G47 (= G48), C48 (≠ T49), K52 (= K53), Y116 (≠ T115), G117 (= G116), T146 (= T145), G147 (= G146), S166 (= S165), I187 (= I186), F281 (≠ N273), G317 (= G309), D318 (= D310), M324 (≠ S316), L325 (= L317), A326 (= A318), H327 (≠ S319)
- binding nicotinamide-adenine-dinucleotide: G183 (= G182), G185 (= G184), V205 (= V204), E206 (≠ D205), F207 (≠ N206), L208 (≠ R207), K240 (≠ E238), V241 (≠ Y239), I276 (≠ N268), G277 (= G269), R278 (= R270), R297 (= R289), M324 (≠ S316)
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)
30% identity, 98% coverage: 5:458/464 of query aligns to 26:494/499 of P09624
- 56:65 (vs. 35:44, 40% identical) binding
- C65 (= C44) modified: Disulfide link with 70, Redox-active
- C70 (≠ T49) modified: Disulfide link with 65, Redox-active
- K74 (= K53) binding
- G139 (= G116) binding
- D346 (= D310) binding
- MLAH 352:355 (≠ SLAS 316:319) binding
- H478 (≠ Y445) active site, Proton acceptor
Sites not aligning to the query:
- 1:21 modified: transit peptide, Mitochondrion
2qaeA Crystal structure analysis of trypanosoma cruzi lipoamide dehydrogenase
31% identity, 94% coverage: 20:456/464 of query aligns to 17:455/465 of 2qaeA
- active site: L37 (≠ V40), C41 (= C44), C46 (≠ T49), S49 (= S52), V184 (= V185), E188 (= E189), H442 (≠ N444), H444 (≠ Y445), E449 (= E450)
- binding flavin-adenine dinucleotide: E32 (≠ D35), K33 (≠ S36), R34 (= R37), G39 (= G42), T40 (≠ N43), C41 (= C44), G45 (= G48), C46 (≠ T49), K50 (= K53), E114 (≠ T115), G115 (= G116), T144 (= T145), G145 (= G146), S164 (= S165), I185 (= I186), F274 (≠ N273), G310 (= G309), D311 (= D310), M318 (≠ S316), L319 (= L317), A320 (= A318), H321 (≠ S319)
Sites not aligning to the query:
P09622 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; EC 1.8.1.4 from Homo sapiens (Human) (see 14 papers)
31% identity, 97% coverage: 5:455/464 of query aligns to 41:497/509 of P09622
- 71:80 (vs. 35:44, 30% identical) binding
- K72 (≠ S36) 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 (≠ E76) to T: in dbSNP:rs1130477
- G154 (= G116) binding
- TGS 183:185 (= TGS 145:147) binding
- 220:227 (vs. 182:189, 88% identical) binding
- E243 (≠ D205) binding
- V278 (≠ Y239) binding
- G314 (= G269) binding
- D355 (= D310) binding
- MLAH 361:364 (≠ SLAS 316:319) binding
- E375 (≠ G330) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (≠ W338) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (≠ L403) 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 (≠ I421) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ Q428) 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 (≠ T434) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (≠ Y437) 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 (≠ N440) 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 (≠ A449) 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 (= R453) 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)
30% identity, 97% coverage: 7:456/464 of query aligns to 39:491/501 of P31023
- 67:76 (vs. 35:44, 40% identical) binding
- C76 (= C44) modified: Disulfide link with 81, Redox-active
- C81 (≠ T49) modified: Disulfide link with 76, Redox-active
- G149 (= G116) binding
- D348 (= D310) binding
- MLAH 354:357 (≠ SLAS 316:319) binding
Sites not aligning to the query:
- 1:31 modified: transit peptide, Mitochondrion
1dxlA Dihydrolipoamide dehydrogenase of glycine decarboxylase from pisum sativum (see paper)
30% identity, 97% coverage: 7:456/464 of query aligns to 5:457/467 of 1dxlA
- active site: L38 (≠ V40), C42 (= C44), C47 (≠ T49), S50 (= S52), Y184 (≠ V185), E188 (= E189), H444 (≠ N440), H446 (≠ Y445), E451 (= E450)
- binding flavin-adenine dinucleotide: I9 (≠ L11), P13 (= P15), G14 (≠ A16), E33 (≠ D35), K34 (≠ S36), R35 (= R37), G40 (= G42), T41 (≠ N43), C42 (= C44), G46 (= G48), C47 (≠ T49), K51 (= K53), Y114 (≠ T115), G115 (= G116), T144 (= T145), G145 (= G146), Y184 (≠ V185), I185 (= I186), R274 (= R270), D314 (= D310), M320 (≠ S316), L321 (= L317), A322 (= A318), H323 (≠ S319)
P0A9P0 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes; Glycine cleavage system L protein; EC 1.8.1.4 from Escherichia coli (strain K12) (see 2 papers)
32% identity, 97% coverage: 8:456/464 of query aligns to 9:456/474 of P0A9P0
- K220 (≠ Q220) modified: N6-acetyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
6hg8B Crystal structure of the r460g disease-causing mutant of the human dihydrolipoamide dehydrogenase.
30% identity, 97% coverage: 5:452/464 of query aligns to 14:467/482 of 6hg8B
- active site: C53 (= C44), C58 (≠ T49), S61 (= S52), V196 (= V185), E200 (= E189), H460 (≠ Y445), E465 (= E450)
- binding flavin-adenine dinucleotide: I20 (≠ L11), G23 (= G14), P24 (= P15), G25 (≠ A16), E44 (≠ D35), K45 (≠ S36), N46 (≠ R37), G51 (= G42), T52 (≠ N43), C53 (= C44), G57 (= G48), C58 (≠ T49), K62 (= K53), Y126 (≠ T115), G127 (= G116), T156 (= T145), G157 (= G146), I197 (= I186), R288 (= R270), F291 (≠ N273), G327 (= G309), D328 (= D310), M334 (≠ S316), L335 (= L317), A336 (= A318), H337 (≠ S319)
4jdrA Dihydrolipoamide dehydrogenase of pyruvate dehydrogenase from escherichia coli (see paper)
32% identity, 97% coverage: 8:456/464 of query aligns to 8:455/471 of 4jdrA
- active site: P15 (= P15), L40 (≠ V40), C44 (= C44), C49 (≠ T49), S52 (= S52), E77 (= E76), P78 (= P77), I184 (≠ V185), E188 (= E189), V324 (≠ H322), H442 (≠ F443), H444 (≠ Y445), E449 (= E450)
- binding flavin-adenine dinucleotide: G12 (= G12), G14 (= G14), P15 (= P15), A16 (= A16), E35 (≠ D35), R36 (≠ S36), Y37 (≠ R37), V43 (≠ N43), C44 (= C44), G48 (= G48), C49 (≠ T49), K53 (= K53), L115 (≠ T115), G116 (= G116), A144 (≠ T145), G145 (= G146), I185 (= I186), G311 (= G309), D312 (= D310), M318 (≠ S316), L319 (= L317), A320 (= A318), H321 (≠ S319)
Sites not aligning to the query:
Query Sequence
>GFF1504 FitnessBrowser__WCS417:GFF1504
MAVYNYDVVVLGSGPAGEGAAMNAAKAGRKVAMVDSRRQVGGNCTHLGTIPSKALRHSVR
QIMQFNTNPMFRAIGEPRWFSFPDVLKSAEKVISKQVASRTGYYARNRVDLFFGTGSFAD
EQTIEVVCPNGVVEKLVAKHIIIATGSRPYRPADIDFHHPRIYDSDTILSLGHTPRKLII
YGAGVIGCEYASIFSGLGVLVELVDNRDQLLSFLDSEISQALSYHFSNNNITVRHNEEYE
RVEGLDNGVILHLKSGKKIKADALLWCNGRTGNTDKLGMENIGVKVNSRGQIEVDENYRT
CVTNIYGAGDVIGWPSLASAAHDQGRSAAGSIVDNGSWRYVNDVPTGIYTIPEISSIGKN
EHELTKAKVPYEVGKAFFKSMARAQIAGEPQGMLKILFHRETLEVLGVHCFGYQASEIVH
IGQAIMNQPGELNTLKYFVNTTFNYPTMAEAYRVAAYDGLNRLF
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