SitesBLAST
Comparing Ac3H11_2465 FitnessBrowser__acidovorax_3H11:Ac3H11_2465 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)
6aonA 1.72 angstrom resolution crystal structure of 2-oxoglutarate dehydrogenase complex subunit dihydrolipoamide dehydrogenase from bordetella pertussis in complex with fad
76% identity, 100% coverage: 3:475/475 of query aligns to 1:473/473 of 6aonA
- active site: P43 (= P45), C47 (= C49), C52 (= C54), S55 (= S57), V191 (= V193), E195 (= E197), H450 (= H452), H452 (= H454), E457 (= E459)
- binding calcium ion: A218 (≠ G220), A220 (≠ V222), Q222 (≠ E224)
- binding flavin-adenine dinucleotide: I8 (= I10), G11 (= G13), P12 (= P14), G13 (= G15), D32 (= D34), A33 (≠ E35), W34 (= W36), G45 (= G47), T46 (= T48), C47 (= C49), G51 (= G53), C52 (= C54), K56 (= K58), K119 (≠ R121), G120 (= G122), T151 (= T153), G152 (= G154), N171 (= N173), I192 (= I194), R280 (= R282), Y283 (≠ N285), G319 (= G321), D320 (= D322), M326 (= M328), L327 (= L329), A328 (= A330), H329 (= H331)
P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 from Pseudomonas fluorescens (see 2 papers)
54% identity, 100% coverage: 1:475/475 of query aligns to 1:472/478 of P14218
- M1 (= M1) modified: Initiator methionine, Removed
- 34:49 (vs. 34:49, 38% identical) binding
- C49 (= C49) modified: Disulfide link with 54, Redox-active
- C54 (= C54) modified: Disulfide link with 49, Redox-active
- K58 (= K58) binding
- G122 (= G122) binding
- D319 (= D322) binding
- A327 (= A330) binding
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
54% identity, 100% coverage: 1:475/475 of query aligns to 3:474/477 of 5u8uD
- active site: P16 (= P14), L47 (≠ P45), C51 (= C49), C56 (= C54), S59 (= S57), G85 (= G83), V86 (= V84), V193 (= V193), E197 (= E197), S333 (≠ E334), F451 (≠ H452), H453 (= H454), E458 (= E459)
- binding flavin-adenine dinucleotide: I12 (= I10), G15 (= G13), P16 (= P14), G17 (= G15), E36 (≠ D34), K37 (≠ E35), G49 (= G47), T50 (= T48), C51 (= C49), G55 (= G53), C56 (= C54), K60 (= K58), H123 (≠ R121), G124 (= G122), A152 (= A152), S153 (≠ T153), G154 (= G154), I194 (= I194), R281 (= R282), G320 (= G321), D321 (= D322), M327 (= M328), L328 (= L329), A329 (= A330), H330 (= H331), H453 (= H454), P454 (= P455)
Sites not aligning to the query:
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
54% identity, 100% coverage: 2:475/475 of query aligns to 1:471/473 of 5u8wA
- active site: P13 (= P14), L44 (≠ P45), C48 (= C49), C53 (= C54), S56 (= S57), G82 (= G83), V83 (= V84), V190 (= V193), E194 (= E197), S330 (≠ E334), F448 (≠ H452), H450 (= H454), E455 (= E459)
- binding flavin-adenine dinucleotide: I9 (= I10), G12 (= G13), P13 (= P14), G14 (= G15), E33 (≠ D34), K34 (≠ E35), G46 (= G47), T47 (= T48), C48 (= C49), G52 (= G53), C53 (= C54), K57 (= K58), H120 (≠ R121), G121 (= G122), A149 (= A152), S150 (≠ T153), G151 (= G154), S170 (≠ N173), G317 (= G321), D318 (= D322), M324 (= M328), L325 (= L329), A326 (= A330), H327 (= H331), Y357 (= Y361), H450 (= H454), P451 (= P455)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (= I189), G189 (= G192), V190 (= V193), I191 (= I194), E194 (= E197), E210 (= E213), A211 (≠ G214), L212 (= L215), A275 (≠ S279), V276 (≠ I280), G277 (= G281), R278 (= R282), M324 (= M328), L325 (= L329), V355 (= V359), Y357 (= Y361)
Sites not aligning to the query:
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
54% identity, 100% coverage: 3:475/475 of query aligns to 1:470/472 of 5u8vA
- active site: P12 (= P14), L43 (≠ P45), C47 (= C49), C52 (= C54), S55 (= S57), G81 (= G83), V82 (= V84), V189 (= V193), E193 (= E197), S329 (≠ E334), F447 (≠ H452), H449 (= H454), E454 (= E459)
- binding flavin-adenine dinucleotide: I8 (= I10), G11 (= G13), P12 (= P14), G13 (= G15), E32 (≠ D34), G45 (= G47), T46 (= T48), C47 (= C49), G51 (= G53), C52 (= C54), K56 (= K58), H119 (≠ R121), G120 (= G122), A148 (= A152), S149 (≠ T153), G150 (= G154), S169 (≠ N173), I190 (= I194), R277 (= R282), G316 (= G321), D317 (= D322), M323 (= M328), L324 (= L329), A325 (= A330), H326 (= H331), H449 (= H454), P450 (= P455)
- binding nicotinamide-adenine-dinucleotide: I185 (= I189), G186 (= G190), G188 (= G192), V189 (= V193), I190 (= I194), L208 (= L212), E209 (= E213), A210 (≠ G214), V243 (= V247), V275 (≠ I280), G276 (= G281)
Sites not aligning to the query:
6awaA 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from pseudomonas putida in complex with fad and adenosine-5'-monophosphate.
53% identity, 99% coverage: 1:469/475 of query aligns to 1:466/475 of 6awaA
- active site: L45 (≠ P45), C49 (= C49), C54 (= C54), S57 (= S57), V191 (= V193), E195 (= E197), F449 (≠ H452), H451 (= H454), E456 (= E459)
- binding adenosine monophosphate: I187 (= I189), E211 (= E213), A212 (≠ G214), L213 (= L215), V245 (= V247), V277 (≠ I280)
- binding flavin-adenine dinucleotide: I10 (= I10), G13 (= G13), P14 (= P14), G15 (= G15), E34 (≠ D34), K35 (≠ E35), T48 (= T48), C49 (= C49), G53 (= G53), C54 (= C54), K58 (= K58), H121 (≠ R121), G122 (= G122), S151 (≠ T153), G152 (= G154), I192 (= I194), R279 (= R282), G318 (= G321), D319 (= D322), M325 (= M328), L326 (= L329), A327 (= A330), Y358 (= Y361)
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)
52% identity, 100% coverage: 1:474/475 of query aligns to 1:471/477 of P18925
- 34:49 (vs. 34:49, 44% identical) binding
- C49 (= C49) modified: Disulfide link with 54, Redox-active
- C54 (= C54) modified: Disulfide link with 49, Redox-active
- K58 (= K58) binding
- D319 (= D322) binding
- A327 (= A330) binding
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)
52% identity, 100% coverage: 2:474/475 of query aligns to 1:470/472 of 3ladA
- active site: L44 (≠ P45), C48 (= C49), C53 (= C54), S56 (= S57), V190 (= V193), E194 (= E197), F448 (≠ H452), H450 (= H454), E455 (= E459)
- binding flavin-adenine dinucleotide: I9 (= I10), G10 (= G11), G12 (= G13), P13 (= P14), E33 (≠ D34), K34 (≠ E35), G46 (= G47), T47 (= T48), C48 (= C49), G52 (= G53), C53 (= C54), H120 (≠ R121), G121 (= G122), A149 (= A152), S150 (≠ T153), G151 (= G154), I191 (= I194), R278 (= R282), D318 (= D322), L325 (= L329), A326 (= A330)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
52% identity, 99% coverage: 4:475/475 of query aligns to 6:470/470 of 6uziC
- active site: C45 (= C49), C50 (= C54), S53 (= S57), V187 (= V193), E191 (= E197), H448 (= H454), E453 (= E459)
- binding flavin-adenine dinucleotide: I12 (= I10), G13 (= G11), G15 (= G13), P16 (= P14), G17 (= G15), E36 (≠ D34), K37 (≠ E35), G43 (= G47), T44 (= T48), C45 (= C49), G49 (= G53), C50 (= C54), S53 (= S57), K54 (= K58), V117 (≠ R121), G118 (= G122), T147 (= T153), G148 (= G154), I188 (= I194), R276 (= R282), D316 (= D322), M322 (= M328), L323 (= L329), A324 (= A330)
- binding zinc ion: H448 (= H454), E453 (= E459)
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
51% identity, 97% coverage: 5:467/475 of query aligns to 1:458/465 of 3urhB
- active site: Y35 (≠ P45), C39 (= C49), C44 (= C54), S47 (= S57), V183 (= V193), E187 (= E197), H443 (= H452), H445 (= H454), E450 (= E459)
- binding flavin-adenine dinucleotide: I6 (= I10), G7 (= G11), G9 (= G13), P10 (= P14), G11 (= G15), E30 (≠ D34), K31 (≠ E35), G37 (= G47), T38 (= T48), C39 (= C49), G43 (= G53), C44 (= C54), K48 (= K58), T111 (≠ R121), G112 (= G122), A140 (= A152), T141 (= T153), G142 (= G154), I184 (= I194), R273 (= R282), G312 (= G321), D313 (= D322), M319 (= M328), L320 (= L329), A321 (= A330), H322 (= H331)
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)
50% identity, 100% coverage: 2:475/475 of query aligns to 35:501/501 of P31023
- 67:76 (vs. 34:49, 44% identical) binding
- C76 (= C49) modified: Disulfide link with 81, Redox-active
- C81 (= C54) modified: Disulfide link with 76, Redox-active
- G149 (= G122) binding
- D348 (= D322) binding
- MLAH 354:357 (= MLAH 328:331) binding
Sites not aligning to the query:
- 1:31 modified: transit peptide, Mitochondrion
1dxlA Dihydrolipoamide dehydrogenase of glycine decarboxylase from pisum sativum (see paper)
50% identity, 100% coverage: 2:475/475 of query aligns to 1:467/467 of 1dxlA
- active site: L38 (≠ P45), C42 (= C49), C47 (= C54), S50 (= S57), Y184 (≠ V193), E188 (= E197), H444 (= H452), H446 (= H454), E451 (= E459)
- binding flavin-adenine dinucleotide: I9 (= I10), P13 (= P14), G14 (= G15), E33 (≠ D34), K34 (= K37), R35 (≠ N38), G40 (= G47), T41 (= T48), C42 (= C49), G46 (= G53), C47 (= C54), K51 (= K58), Y114 (≠ R121), G115 (= G122), T144 (= T153), G145 (= G154), Y184 (≠ V193), I185 (= I194), R274 (= R282), D314 (= D322), M320 (= M328), L321 (= L329), A322 (= A330), H323 (= H331)
6bz0A 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from acinetobacter baumannii in complex with fad.
49% identity, 99% coverage: 4:474/475 of query aligns to 1:467/469 of 6bz0A
- active site: C45 (= C49), C50 (= C54), S53 (= S57), V187 (= V193), E191 (= E197), H447 (= H454), E452 (= E459)
- binding flavin-adenine dinucleotide: I7 (= I10), G10 (= G13), P11 (= P14), G12 (= G15), E31 (≠ D34), K32 (≠ E35), R33 (≠ W36), G43 (= G47), T44 (= T48), C45 (= C49), G49 (= G53), C50 (= C54), K54 (= K58), T117 (≠ R121), G118 (= G122), S147 (≠ T153), G148 (= G154), S167 (≠ N173), I188 (= I194), R275 (= R282), Y278 (≠ N285), D315 (= D322), M321 (= M328), L322 (= L329), A323 (= A330), A326 (= A333), Y354 (= Y361)
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)
48% identity, 98% coverage: 1:467/475 of query aligns to 23:491/499 of P09624
- 56:65 (vs. 34:49, 44% identical) binding
- C65 (= C49) modified: Disulfide link with 70, Redox-active
- C70 (= C54) modified: Disulfide link with 65, Redox-active
- K74 (= K58) binding
- G139 (= G122) binding
- D346 (= D322) binding
- MLAH 352:355 (= MLAH 328:331) binding
- H478 (= H454) active site, Proton acceptor
Sites not aligning to the query:
- 1:21 modified: transit peptide, Mitochondrion
P09622 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; EC 1.8.1.4 from Homo sapiens (Human) (see 14 papers)
48% identity, 99% coverage: 6:475/475 of query aligns to 43:509/509 of P09622
- 71:80 (vs. 34:49, 25% identical) binding
- K72 (≠ E35) to E: in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX; dbSNP:rs121964987
- K89 (= K58) binding ; mutation to E: Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- K104 (= K72) to T: in dbSNP:rs1130477
- G154 (= G122) binding
- TGS 183:185 (= TGS 153:155) binding
- 220:227 (vs. 190:197, 75% identical) binding
- E243 (= E213) binding
- V278 (= V247) binding
- G314 (= G281) binding
- D355 (= D322) binding
- MLAH 361:364 (= MLAH 328:331) binding
- E375 (= E342) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (= H350) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (= D415) 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 (= E433) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ F440) 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 (= D446) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (= R449) 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 (= H452) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
- P488 (= P455) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
- S491 (= S458) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
- E492 (= E459) mutation to Q: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- R495 (≠ K462) to G: in DLDD; loss of enzyme activity; reduced interaction with PDHX; dbSNP:rs121964989
- K505 (≠ R471) mutation to M: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
1v59A Crystal structure of yeast lipoamide dehydrogenase complexed with NAD+
48% identity, 98% coverage: 1:467/475 of query aligns to 2:470/478 of 1v59A
- active site: L40 (≠ P45), C44 (= C49), C49 (= C54), S52 (= S57), I193 (≠ V193), E197 (= E197), T349 (≠ G346), H455 (= H452), H457 (= H454), E462 (= E459)
- binding flavin-adenine dinucleotide: G14 (= G13), P15 (= P14), A16 (≠ G15), E35 (≠ D34), K36 (= K37), R37 (≠ N38), G42 (= G47), T43 (= T48), C44 (= C49), G48 (= G53), C49 (= C54), K53 (= K58), N117 (≠ R121), G118 (= G122), T153 (= T153), G154 (= G154), R285 (= R282), Y288 (≠ N285), G324 (= G321), D325 (= D322), M331 (= M328), L332 (= L329), A333 (= A330), H334 (= H331), Y364 (= Y361)
- binding nicotinamide-adenine-dinucleotide: I189 (= I189), G190 (= G190), E213 (= E213), F214 (≠ G214), K246 (= K246), V283 (≠ I280)
1jehA Crystal structure of yeast e3, lipoamide dehydrogenase (see paper)
48% identity, 98% coverage: 1:467/475 of query aligns to 2:470/478 of 1jehA
- active site: L40 (≠ P45), C44 (= C49), C49 (= C54), S52 (= S57), I193 (≠ V193), E197 (= E197), T349 (≠ G346), H455 (= H452), H457 (= H454), E462 (= E459)
- binding flavin-adenine dinucleotide: I11 (= I10), G14 (= G13), P15 (= P14), A16 (≠ G15), V34 (≠ I33), E35 (≠ D34), K36 (= K37), R37 (≠ N38), G42 (= G47), T43 (= T48), C44 (= C49), G48 (= G53), C49 (= C54), K53 (= K58), G118 (= G122), T153 (= T153), G154 (= G154), I194 (= I194), R285 (= R282), Y288 (≠ N285), L292 (= L289), G324 (= G321), D325 (= D322), M331 (= M328), L332 (= L329), A333 (= A330), H334 (= H331)
6hg8B Crystal structure of the r460g disease-causing mutant of the human dihydrolipoamide dehydrogenase.
48% identity, 99% coverage: 6:475/475 of query aligns to 16:482/482 of 6hg8B
- active site: C53 (= C49), C58 (= C54), S61 (= S57), V196 (= V193), E200 (= E197), H460 (= H454), E465 (= E459)
- binding flavin-adenine dinucleotide: I20 (= I10), G23 (= G13), P24 (= P14), G25 (= G15), E44 (≠ D34), K45 (≠ E35), N46 (≠ W36), G51 (= G47), T52 (= T48), C53 (= C49), G57 (= G53), C58 (= C54), K62 (= K58), Y126 (≠ R121), G127 (= G122), T156 (= T153), G157 (= G154), I197 (= I194), R288 (= R282), F291 (≠ N285), G327 (= G321), D328 (= D322), M334 (= M328), L335 (= L329), A336 (= A330), H337 (= H331)
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
48% identity, 99% coverage: 6:475/475 of query aligns to 6:472/472 of 1zmdA
- active site: L39 (≠ P45), C43 (= C49), C48 (= C54), S51 (= S57), V186 (= V193), E190 (= E197), H448 (= H452), H450 (= H454), E455 (= E459)
- binding flavin-adenine dinucleotide: I10 (= I10), G11 (= G11), G13 (= G13), P14 (= P14), G15 (= G15), E34 (≠ D34), K35 (≠ E35), N36 (≠ W36), G41 (= G47), T42 (= T48), C43 (= C49), G47 (= G53), C48 (= C54), K52 (= K58), Y116 (≠ R121), G117 (= G122), T146 (= T153), G147 (= G154), S166 (≠ N173), R278 (= R282), F281 (≠ N285), G317 (= G321), D318 (= D322), M324 (= M328), L325 (= L329), A326 (= A330), H327 (= H331)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (= I189), G183 (= G190), G185 (= G192), V186 (= V193), I187 (= I194), E190 (= E197), E206 (= E213), F207 (= F218), L208 (= L219), I276 (= I280), G277 (= G281), R278 (= R282), M324 (= M328), L325 (= L329), V355 (= V359), Y357 (= Y361)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
48% identity, 99% coverage: 6:475/475 of query aligns to 6:472/472 of 1zmcA
- active site: L39 (≠ P45), C43 (= C49), C48 (= C54), S51 (= S57), V186 (= V193), E190 (= E197), H448 (= H452), H450 (= H454), E455 (= E459)
- binding flavin-adenine dinucleotide: I10 (= I10), G11 (= G11), G13 (= G13), P14 (= P14), G15 (= G15), E34 (≠ D34), K35 (≠ E35), N36 (≠ W36), G41 (= G47), T42 (= T48), C43 (= C49), G47 (= G53), C48 (= C54), K52 (= K58), Y116 (≠ R121), G117 (= G122), T146 (= T153), G147 (= G154), S166 (≠ N173), I187 (= I194), F281 (≠ N285), G317 (= G321), D318 (= D322), M324 (= M328), L325 (= L329), A326 (= A330), H327 (= H331)
- binding nicotinamide-adenine-dinucleotide: G183 (= G190), G185 (= G192), V205 (≠ L212), E206 (= E213), F207 (= F218), L208 (= L219), K240 (= K246), V241 (= V247), I276 (= I280), G277 (= G281), R278 (= R282), R297 (= R301), M324 (= M328)
Query Sequence
>Ac3H11_2465 FitnessBrowser__acidovorax_3H11:Ac3H11_2465
MSKQFDVIVIGGGPGGYIAAIRAAQLGFNVACIDEWKNGKGGPAPGGTCTNVGCIPSKAL
LQSSEHFEHANKHFAEHGITATGVKMDVAKMIARKDTVVKQNNDGILYLFKKNKVSFFHG
RGSFVKAAEGGYEIKVAGAAEESIVGKQIIIATGSNARALPGTPFDEELVLSNDGALRVG
AVPKKLGLIGSGVIGLEMGSVWRRLGAEVTILEGLPTFLGAVDEQIAKEAKKAFDKQGLK
IELGVKVGEIKTGKKGVSIAYTNAKGEAQSLDVDKLIVSIGRVPNTIGLNVEAVGLALDE
RGAIVVDGDCKTNLPGVWAVGDVVRGPMLAHKAEEEGVAVAERIAGQHGHVNFNTVPWVI
YTSPEIAWVGRTEQQLKADGVKYKAGTFPFLANGRARALGDTTGMVKMLADAETDEILGV
HIVGPQASELISEAVVAMEFKASSEDIARICHAHPSLSEATKEAALAVDKRTLNF
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