SitesBLAST
Comparing Dsui_2219 FitnessBrowser__PS:Dsui_2219 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)
6aonA 1.72 angstrom resolution crystal structure of 2-oxoglutarate dehydrogenase complex subunit dihydrolipoamide dehydrogenase from bordetella pertussis in complex with fad
67% identity, 100% coverage: 3:474/474 of query aligns to 1:473/473 of 6aonA
- active site: P43 (≠ L47), C47 (= C51), C52 (= C56), S55 (= S59), V191 (= V192), E195 (= E196), H450 (= H451), H452 (= H453), E457 (= E458)
- binding calcium ion: A218 (= A219), A220 (= A221), Q222 (= Q223)
- binding flavin-adenine dinucleotide: I8 (= I10), G11 (= G13), P12 (= P14), G13 (= G15), D32 (≠ E34), A33 (≠ S35), W34 (≠ Y38), G45 (= G49), T46 (= T50), C47 (= C51), G51 (= G55), C52 (= C56), K56 (= K60), K119 (≠ H123), G120 (= G124), T151 (= T152), G152 (= G153), N171 (= N172), I192 (= I193), R280 (= R281), Y283 (≠ N284), G319 (= G320), D320 (= D321), M326 (= M327), L327 (= L328), A328 (= A329), H329 (= H330)
P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 from Pseudomonas fluorescens (see 2 papers)
56% identity, 100% coverage: 1:474/474 of query aligns to 1:472/478 of P14218
- M1 (= M1) modified: Initiator methionine, Removed
- 34:49 (vs. 34:51, 44% identical) binding
- C49 (= C51) modified: Disulfide link with 54, Redox-active
- C54 (= C56) modified: Disulfide link with 49, Redox-active
- K58 (= K60) binding
- G122 (= G124) binding
- D319 (= D321) binding
- A327 (= A329) binding
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
56% identity, 100% coverage: 1:474/474 of query aligns to 3:474/477 of 5u8uD
- active site: P16 (= P14), L47 (= L47), C51 (= C51), C56 (= C56), S59 (= S59), G85 (≠ A85), V86 (≠ P86), V193 (= V192), E197 (= E196), S333 (≠ M333), F451 (≠ H451), H453 (= H453), E458 (= E458)
- binding flavin-adenine dinucleotide: I12 (= I10), G15 (= G13), P16 (= P14), G17 (= G15), E36 (= E34), K37 (≠ S35), G49 (= G49), T50 (= T50), C51 (= C51), G55 (= G55), C56 (= C56), K60 (= K60), H123 (= H123), G124 (= G124), A152 (= A151), S153 (≠ T152), G154 (= G153), I194 (= I193), R281 (= R281), G320 (= G320), D321 (= D321), M327 (= M327), L328 (= L328), A329 (= A329), H330 (= H330), H453 (= H453), P454 (= P454)
Sites not aligning to the query:
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
56% identity, 100% coverage: 2:474/474 of query aligns to 1:471/473 of 5u8wA
- active site: P13 (= P14), L44 (= L47), C48 (= C51), C53 (= C56), S56 (= S59), G82 (≠ A85), V83 (≠ P86), V190 (= V192), E194 (= E196), S330 (≠ M333), F448 (≠ H451), H450 (= H453), E455 (= E458)
- binding flavin-adenine dinucleotide: I9 (= I10), G12 (= G13), P13 (= P14), G14 (= G15), E33 (= E34), K34 (≠ S35), G46 (= G49), T47 (= T50), C48 (= C51), G52 (= G55), C53 (= C56), K57 (= K60), H120 (= H123), G121 (= G124), A149 (= A151), S150 (≠ T152), G151 (= G153), S170 (≠ N172), G317 (= G320), D318 (= D321), M324 (= M327), L325 (= L328), A326 (= A329), H327 (= H330), Y357 (= Y360), H450 (= H453), P451 (= P454)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (= I188), G189 (= G191), V190 (= V192), I191 (= I193), E194 (= E196), E210 (= E212), A211 (= A213), L212 (≠ S214), A275 (≠ S278), V276 (= V279), G277 (= G280), R278 (= R281), M324 (= M327), L325 (= L328), V355 (= V358), Y357 (= Y360)
Sites not aligning to the query:
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
56% identity, 100% coverage: 3:474/474 of query aligns to 1:470/472 of 5u8vA
- active site: P12 (= P14), L43 (= L47), C47 (= C51), C52 (= C56), S55 (= S59), G81 (≠ A85), V82 (≠ P86), V189 (= V192), E193 (= E196), S329 (≠ M333), F447 (≠ H451), H449 (= H453), E454 (= E458)
- binding flavin-adenine dinucleotide: I8 (= I10), G11 (= G13), P12 (= P14), G13 (= G15), E32 (= E34), G45 (= G49), T46 (= T50), C47 (= C51), G51 (= G55), C52 (= C56), K56 (= K60), H119 (= H123), G120 (= G124), A148 (= A151), S149 (≠ T152), G150 (= G153), S169 (≠ N172), I190 (= I193), R277 (= R281), G316 (= G320), D317 (= D321), M323 (= M327), L324 (= L328), A325 (= A329), H326 (= H330), H449 (= H453), P450 (= P454)
- binding nicotinamide-adenine-dinucleotide: I185 (= I188), G186 (= G189), G188 (= G191), V189 (= V192), I190 (= I193), L208 (= L211), E209 (= E212), A210 (= A213), V243 (≠ L246), V275 (= V279), G276 (= G280)
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.
54% identity, 100% coverage: 1:473/474 of query aligns to 1:471/475 of 6awaA
- active site: L45 (= L47), C49 (= C51), C54 (= C56), S57 (= S59), V191 (= V192), E195 (= E196), F449 (≠ H451), H451 (= H453), E456 (= E458)
- binding adenosine monophosphate: I187 (= I188), E211 (= E212), A212 (= A213), L213 (≠ S214), V245 (≠ L246), V277 (= V279)
- binding flavin-adenine dinucleotide: I10 (= I10), G13 (= G13), P14 (= P14), G15 (= G15), E34 (= E34), K35 (≠ S35), T48 (= T50), C49 (= C51), G53 (= G55), C54 (= C56), K58 (= K60), H121 (= H123), G122 (= G124), S151 (≠ T152), G152 (= G153), I192 (= I193), R279 (= R281), G318 (= G320), D319 (= D321), M325 (= M327), L326 (= L328), A327 (= A329), Y358 (= Y360)
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)
54% identity, 100% coverage: 1:473/474 of query aligns to 1:471/477 of P18925
- 34:49 (vs. 34:51, 44% identical) binding
- C49 (= C51) modified: Disulfide link with 54, Redox-active
- C54 (= C56) modified: Disulfide link with 49, Redox-active
- K58 (= K60) binding
- D319 (= D321) binding
- A327 (= A329) 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)
54% identity, 100% coverage: 2:473/474 of query aligns to 1:470/472 of 3ladA
- active site: L44 (= L47), C48 (= C51), C53 (= C56), S56 (= S59), V190 (= V192), E194 (= E196), F448 (≠ H451), H450 (= H453), E455 (= E458)
- binding flavin-adenine dinucleotide: I9 (= I10), G10 (= G11), G12 (= G13), P13 (= P14), E33 (= E34), K34 (≠ S35), G46 (= G49), T47 (= T50), C48 (= C51), G52 (= G55), C53 (= C56), H120 (= H123), G121 (= G124), A149 (= A151), S150 (≠ T152), G151 (= G153), I191 (= I193), R278 (= R281), D318 (= D321), L325 (= L328), A326 (= A329)
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
51% identity, 99% coverage: 5:473/474 of query aligns to 1:465/465 of 3urhB
- active site: Y35 (≠ L47), C39 (= C51), C44 (= C56), S47 (= S59), V183 (= V192), E187 (= E196), H443 (= H451), H445 (= H453), E450 (= E458)
- binding flavin-adenine dinucleotide: I6 (= I10), G7 (= G11), G9 (= G13), P10 (= P14), G11 (= G15), E30 (= E34), K31 (≠ S35), G37 (= G49), T38 (= T50), C39 (= C51), G43 (= G55), C44 (= C56), K48 (= K60), T111 (≠ H123), G112 (= G124), A140 (= A151), T141 (= T152), G142 (= G153), I184 (= I193), R273 (= R281), G312 (= G320), D313 (= D321), M319 (= M327), L320 (= L328), A321 (= A329), H322 (= H330)
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)
49% identity, 100% coverage: 2:474/474 of query aligns to 35:501/501 of P31023
- 67:76 (vs. 34:51, 33% identical) binding
- C76 (= C51) modified: Disulfide link with 81, Redox-active
- C81 (= C56) modified: Disulfide link with 76, Redox-active
- G149 (= G124) binding
- D348 (= D321) binding
- MLAH 354:357 (= MLAH 327:330) binding
Sites not aligning to the query:
- 1:31 modified: transit peptide, Mitochondrion
1dxlA Dihydrolipoamide dehydrogenase of glycine decarboxylase from pisum sativum (see paper)
49% identity, 100% coverage: 2:474/474 of query aligns to 1:467/467 of 1dxlA
- active site: L38 (= L47), C42 (= C51), C47 (= C56), S50 (= S59), Y184 (≠ V192), E188 (= E196), H444 (= H451), H446 (= H453), E451 (= E458)
- binding flavin-adenine dinucleotide: I9 (= I10), P13 (= P14), G14 (= G15), E33 (= E34), K34 (≠ S35), R35 (≠ N36), G40 (= G49), T41 (= T50), C42 (= C51), G46 (= G55), C47 (= C56), K51 (= K60), Y114 (≠ H123), G115 (= G124), T144 (= T152), G145 (= G153), Y184 (≠ V192), I185 (= I193), R274 (= R281), D314 (= D321), M320 (= M327), L321 (= L328), A322 (= A329), H323 (= H330)
6bz0A 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from acinetobacter baumannii in complex with fad.
51% identity, 99% coverage: 4:473/474 of query aligns to 1:467/469 of 6bz0A
- active site: C45 (= C51), C50 (= C56), S53 (= S59), V187 (= V192), E191 (= E196), H447 (= H453), E452 (= E458)
- binding flavin-adenine dinucleotide: I7 (= I10), G10 (= G13), P11 (= P14), G12 (= G15), E31 (= E34), K32 (≠ S35), R33 (≠ N36), G43 (= G49), T44 (= T50), C45 (= C51), G49 (= G55), C50 (= C56), K54 (= K60), T117 (≠ H123), G118 (= G124), S147 (≠ T152), G148 (= G153), S167 (≠ N172), I188 (= I193), R275 (= R281), Y278 (≠ N284), D315 (= D321), M321 (= M327), L322 (= L328), A323 (= A329), A326 (= A332), Y354 (= Y360)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
51% identity, 99% coverage: 4:474/474 of query aligns to 6:470/470 of 6uziC
- active site: C45 (= C51), C50 (= C56), S53 (= S59), V187 (= V192), E191 (= E196), H448 (= H453), E453 (= E458)
- binding flavin-adenine dinucleotide: I12 (= I10), G13 (= G11), G15 (= G13), P16 (= P14), G17 (= G15), E36 (= E34), K37 (≠ S35), G43 (= G49), T44 (= T50), C45 (= C51), G49 (= G55), C50 (= C56), S53 (= S59), K54 (= K60), V117 (≠ H123), G118 (= G124), T147 (= T152), G148 (= G153), I188 (= I193), R276 (= R281), D316 (= D321), M322 (= M327), L323 (= L328), A324 (= A329)
- binding zinc ion: H448 (= H453), E453 (= E458)
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)
49% identity, 100% coverage: 1:473/474 of query aligns to 23:498/499 of P09624
- 56:65 (vs. 34:51, 33% identical) binding
- C65 (= C51) modified: Disulfide link with 70, Redox-active
- C70 (= C56) modified: Disulfide link with 65, Redox-active
- K74 (= K60) binding
- G139 (= G124) binding
- D346 (= D321) binding
- MLAH 352:355 (= MLAH 327:330) binding
- H478 (= H453) 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+
49% identity, 100% coverage: 1:473/474 of query aligns to 2:477/478 of 1v59A
- active site: L40 (= L47), C44 (= C51), C49 (= C56), S52 (= S59), I193 (≠ V192), E197 (= E196), T349 (≠ G345), H455 (= H451), H457 (= H453), E462 (= E458)
- binding flavin-adenine dinucleotide: G14 (= G13), P15 (= P14), A16 (≠ G15), E35 (= E34), K36 (≠ S35), R37 (≠ E44), G42 (= G49), T43 (= T50), C44 (= C51), G48 (= G55), C49 (= C56), K53 (= K60), N117 (≠ H123), G118 (= G124), T153 (= T152), G154 (= G153), R285 (= R281), Y288 (≠ N284), G324 (= G320), D325 (= D321), M331 (= M327), L332 (= L328), A333 (= A329), H334 (= H330), Y364 (= Y360)
- binding nicotinamide-adenine-dinucleotide: I189 (= I188), G190 (= G189), E213 (= E212), F214 (≠ A213), K246 (= K245), V283 (= V279)
1jehA Crystal structure of yeast e3, lipoamide dehydrogenase (see paper)
49% identity, 100% coverage: 1:473/474 of query aligns to 2:477/478 of 1jehA
- active site: L40 (= L47), C44 (= C51), C49 (= C56), S52 (= S59), I193 (≠ V192), E197 (= E196), T349 (≠ G345), H455 (= H451), H457 (= H453), E462 (= E458)
- binding flavin-adenine dinucleotide: I11 (= I10), G14 (= G13), P15 (= P14), A16 (≠ G15), V34 (≠ C33), E35 (= E34), K36 (≠ S35), R37 (≠ E44), G42 (= G49), T43 (= T50), C44 (= C51), G48 (= G55), C49 (= C56), K53 (= K60), G118 (= G124), T153 (= T152), G154 (= G153), I194 (= I193), R285 (= R281), Y288 (≠ N284), L292 (= L288), G324 (= G320), D325 (= D321), M331 (= M327), L332 (= L328), A333 (= A329), H334 (= H330)
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
46% identity, 97% coverage: 6:466/474 of query aligns to 6:463/472 of 1zmdA
- active site: L39 (= L47), C43 (= C51), C48 (= C56), S51 (= S59), V186 (= V192), E190 (= E196), H448 (= H451), H450 (= H453), E455 (= E458)
- binding flavin-adenine dinucleotide: I10 (= I10), G11 (= G11), G13 (= G13), P14 (= P14), G15 (= G15), E34 (= E34), K35 (≠ S35), N36 (= N36), G41 (= G49), T42 (= T50), C43 (= C51), G47 (= G55), C48 (= C56), K52 (= K60), Y116 (≠ H123), G117 (= G124), T146 (= T152), G147 (= G153), S166 (≠ N172), R278 (= R281), F281 (≠ N284), G317 (= G320), D318 (= D321), M324 (= M327), L325 (= L328), A326 (= A329), H327 (= H330)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (= I188), G183 (= G189), G185 (= G191), V186 (= V192), I187 (= I193), E190 (= E196), E206 (= E212), F207 (= F217), L208 (= L218), I276 (≠ V279), G277 (= G280), R278 (= R281), M324 (= M327), L325 (= L328), V355 (= V358), Y357 (= Y360)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
46% identity, 97% coverage: 6:466/474 of query aligns to 6:463/472 of 1zmcA
- active site: L39 (= L47), C43 (= C51), C48 (= C56), S51 (= S59), V186 (= V192), E190 (= E196), H448 (= H451), H450 (= H453), E455 (= E458)
- binding flavin-adenine dinucleotide: I10 (= I10), G11 (= G11), G13 (= G13), P14 (= P14), G15 (= G15), E34 (= E34), K35 (≠ S35), N36 (= N36), G41 (= G49), T42 (= T50), C43 (= C51), G47 (= G55), C48 (= C56), K52 (= K60), Y116 (≠ H123), G117 (= G124), T146 (= T152), G147 (= G153), S166 (≠ N172), I187 (= I193), F281 (≠ N284), G317 (= G320), D318 (= D321), M324 (= M327), L325 (= L328), A326 (= A329), H327 (= H330)
- binding nicotinamide-adenine-dinucleotide: G183 (= G189), G185 (= G191), V205 (≠ L211), E206 (= E212), F207 (= F217), L208 (= L218), K240 (= K245), V241 (≠ L246), I276 (≠ V279), G277 (= G280), R278 (= R281), R297 (= R300), M324 (= M327)
P09622 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; EC 1.8.1.4 from Homo sapiens (Human) (see 14 papers)
46% identity, 97% coverage: 6:466/474 of query aligns to 43:500/509 of P09622
- 71:80 (vs. 34:51, 39% identical) binding
- K72 (≠ S35) to E: in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX; dbSNP:rs121964987
- K89 (= K60) binding ; mutation to E: Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- K104 (≠ H74) to T: in dbSNP:rs1130477
- G154 (= G124) binding
- TGS 183:185 (= TGS 152:154) binding
- 220:227 (vs. 189:196, 88% identical) binding
- E243 (= E212) binding
- V278 (≠ L246) binding
- G314 (= G280) binding
- D355 (= D321) binding
- MLAH 361:364 (= MLAH 327:330) binding
- E375 (= E341) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (= H349) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (= D414) 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 (= E432) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ F439) 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 (= D445) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (= R448) 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 (= H451) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
- P488 (= P454) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
- S491 (= S457) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
- E492 (= E458) mutation to Q: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- R495 (≠ H461) 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.
46% identity, 97% coverage: 6:466/474 of query aligns to 16:473/482 of 6hg8B
- active site: C53 (= C51), C58 (= C56), S61 (= S59), V196 (= V192), E200 (= E196), H460 (= H453), E465 (= E458)
- binding flavin-adenine dinucleotide: I20 (= I10), G23 (= G13), P24 (= P14), G25 (= G15), E44 (= E34), K45 (≠ S35), N46 (= N36), G51 (= G49), T52 (= T50), C53 (= C51), G57 (= G55), C58 (= C56), K62 (= K60), Y126 (≠ H123), G127 (= G124), T156 (= T152), G157 (= G153), I197 (= I193), R288 (= R281), F291 (≠ N284), G327 (= G320), D328 (= D321), M334 (= M327), L335 (= L328), A336 (= A329), H337 (= H330)
Query Sequence
>Dsui_2219 FitnessBrowser__PS:Dsui_2219
MSKQFDVLVIGGGPGGYVAAIRAAQLGFSVACCESNPYADPKGEPRLGGTCLNVGCIPSK
ALLHTSHLFEEAGHAFAAQGIQVSAPKIDVPTMIGRKTAVVTQLTSGIKGLFKKNKVTQL
NGHGSFVGQGGAGWQVKVGDEVVEAKQVIVATGSKARHLPGIAVDQKIVLDNEGALEQQS
VPKKLAIIGAGVIGLEMGSVWRRLGSEVTILEASPDFLAAADQDVAKEALKLFTKQGLNI
QMGVKLGETKVSKKGVSIAYTDKDGKEQKLDAERLIVSVGRVPNTDGLNAEKIGLKLNER
GQIEVDGHCRTNLPGVWAVGDVVSGPMLAHKAMEEAVMVAELMAGQAGHCNFDTIPWVIY
TSPEIAWVGKTEQQLKADGVAYKAGKIPFLANGRALGMGDPTGFVKMLACAKTDRILGVH
IIGPNASELIAEAVVTMEFGGASEDLARICHAHPTLSEAVHEAALACDKRPLHF
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