SitesBLAST
Comparing WP_018125192.1 NCBI__GCF_000375485.1:WP_018125192.1 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)
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
40% identity, 98% coverage: 3:444/453 of query aligns to 2:444/455 of 2yquB
- active site: P11 (= P12), L36 (= L36), C40 (= C40), C45 (= C45), S48 (≠ T48), G72 (≠ E73), V73 (= V74), V177 (≠ F180), E181 (= E184), S314 (= S315), H432 (≠ F432), H434 (= H434), E439 (= E439)
- binding carbonate ion: A310 (= A311), S314 (= S315), S423 (≠ T423), D426 (= D426)
- binding flavin-adenine dinucleotide: G8 (= G9), G10 (= G11), P11 (= P12), G12 (= G13), E31 (= E32), K32 (= K33), G38 (= G38), T39 (= T39), C40 (= C40), R42 (≠ N42), G44 (= G44), C45 (= C45), K49 (= K49), T110 (≠ L111), A111 (≠ G112), T137 (= T140), G138 (= G141), I178 (= I181), Y265 (≠ V268), G301 (= G302), D302 (= D303), M308 (≠ Q309), L309 (= L310), A310 (= A311), H311 (= H312)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
40% identity, 98% coverage: 3:444/453 of query aligns to 2:444/455 of 2yquA
- active site: P11 (= P12), L36 (= L36), C40 (= C40), C45 (= C45), S48 (≠ T48), G72 (≠ E73), V73 (= V74), V177 (≠ F180), E181 (= E184), S314 (= S315), H432 (≠ F432), H434 (= H434), E439 (= E439)
- binding flavin-adenine dinucleotide: G8 (= G9), G10 (= G11), P11 (= P12), G12 (= G13), E31 (= E32), K32 (= K33), G38 (= G38), T39 (= T39), C40 (= C40), R42 (≠ N42), G44 (= G44), C45 (= C45), K49 (= K49), T110 (≠ L111), A111 (≠ G112), T137 (= T140), G138 (= G141), S157 (= S160), I178 (= I181), Y265 (≠ V268), G301 (= G302), D302 (= D303), M308 (≠ Q309), L309 (= L310), A310 (= A311)
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
40% identity, 98% coverage: 3:444/453 of query aligns to 2:444/452 of 2eq7A
- active site: P11 (= P12), L36 (= L36), C40 (= C40), C45 (= C45), S48 (≠ T48), G72 (≠ E73), V73 (= V74), V177 (≠ F180), E181 (= E184), S314 (= S315), H432 (≠ F432), H434 (= H434), E439 (= E439)
- binding flavin-adenine dinucleotide: G10 (= G11), P11 (= P12), G12 (= G13), E31 (= E32), K32 (= K33), G38 (= G38), T39 (= T39), C40 (= C40), R42 (≠ N42), G44 (= G44), C45 (= C45), K49 (= K49), T110 (≠ L111), A111 (≠ G112), T137 (= T140), G138 (= G141), S157 (= S160), I178 (= I181), R262 (= R265), Y265 (≠ V268), D302 (= D303), M308 (≠ Q309), L309 (= L310), A310 (= A311), H311 (= H312), Y341 (= Y343)
- binding nicotinamide-adenine-dinucleotide: W146 (≠ G149), G174 (= G177), G176 (= G179), V177 (≠ F180), I178 (= I181), E197 (≠ D200), Y198 (≠ A201), V231 (= V234), V260 (= V263), G261 (= G264), R262 (= R265), M308 (≠ Q309), L309 (= L310), V339 (= V341)
P18925 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Azotobacter vinelandii (see 2 papers)
37% identity, 98% coverage: 3:444/453 of query aligns to 5:461/477 of P18925
- 34:49 (vs. 32:40, 44% identical) binding FAD
- C49 (= C40) modified: Disulfide link with 54, Redox-active
- C54 (= C45) modified: Disulfide link with 49, Redox-active
- K58 (= K49) binding FAD
- D319 (= D303) binding FAD
- A327 (= A311) binding FAD
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)
37% identity, 98% coverage: 3:444/453 of query aligns to 4:460/472 of 3ladA
- active site: L44 (= L36), C48 (= C40), C53 (= C45), S56 (≠ T48), V190 (≠ F180), E194 (= E184), F448 (= F432), H450 (= H434), E455 (= E439)
- binding flavin-adenine dinucleotide: I9 (= I8), G10 (= G9), G12 (= G11), P13 (= P12), E33 (= E32), K34 (= K33), G46 (= G38), T47 (= T39), C48 (= C40), G52 (= G44), C53 (= C45), H120 (≠ L111), G121 (= G112), A149 (= A139), S150 (≠ T140), G151 (= G141), I191 (= I181), R278 (= R265), D318 (= D303), L325 (= L310), A326 (= A311)
6awaA 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from pseudomonas putida in complex with fad and adenosine-5'-monophosphate.
37% identity, 98% coverage: 3:444/453 of query aligns to 5:461/475 of 6awaA
- active site: L45 (= L36), C49 (= C40), C54 (= C45), S57 (≠ T48), V191 (≠ F180), E195 (= E184), F449 (= F432), H451 (= H434), E456 (= E439)
- binding adenosine monophosphate: I187 (≠ V176), E211 (≠ D200), A212 (= A201), L213 (≠ M202), V245 (= V234), V277 (= V263)
- binding flavin-adenine dinucleotide: I10 (= I8), G13 (= G11), P14 (= P12), G15 (= G13), E34 (= E32), K35 (= K33), T48 (= T39), C49 (= C40), G53 (= G44), C54 (= C45), K58 (= K49), H121 (≠ L111), G122 (= G112), S151 (≠ T140), G152 (= G141), I192 (= I181), R279 (= R265), G318 (= G302), D319 (= D303), M325 (≠ Q309), L326 (= L310), A327 (= A311), Y358 (= Y343)
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)
36% identity, 98% coverage: 3:444/453 of query aligns to 5:461/478 of P14218
- 34:49 (vs. 32:40, 44% identical) binding FAD
- C49 (= C40) modified: Disulfide link with 54, Redox-active
- C54 (= C45) modified: Disulfide link with 49, Redox-active
- K58 (= K49) binding FAD
- G122 (= G112) binding FAD
- D319 (= D303) binding FAD
- A327 (= A311) binding FAD
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
36% identity, 98% coverage: 3:444/453 of query aligns to 7:463/477 of 5u8uD
- active site: P16 (= P12), L47 (= L36), C51 (= C40), C56 (= C45), S59 (≠ T48), G85 (vs. gap), V86 (= V74), V193 (≠ F180), E197 (= E184), S333 (= S315), F451 (= F432), H453 (= H434), E458 (= E439)
- binding flavin-adenine dinucleotide: I12 (= I8), G15 (= G11), P16 (= P12), G17 (= G13), E36 (= E32), K37 (= K33), G49 (= G38), T50 (= T39), C51 (= C40), G55 (= G44), C56 (= C45), K60 (= K49), H123 (≠ L111), G124 (= G112), A152 (= A139), S153 (≠ T140), G154 (= G141), I194 (= I181), R281 (= R265), G320 (= G302), D321 (= D303), M327 (≠ Q309), L328 (= L310), A329 (= A311), H330 (= H312), H453 (= H434), P454 (= P435)
Sites not aligning to the query:
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
36% identity, 98% coverage: 3:444/453 of query aligns to 3:459/472 of 5u8vA
- active site: P12 (= P12), L43 (= L36), C47 (= C40), C52 (= C45), S55 (≠ T48), G81 (vs. gap), V82 (= V74), V189 (≠ F180), E193 (= E184), S329 (= S315), F447 (= F432), H449 (= H434), E454 (= E439)
- binding flavin-adenine dinucleotide: I8 (= I8), G11 (= G11), P12 (= P12), G13 (= G13), E32 (= E32), G45 (= G38), T46 (= T39), C47 (= C40), G51 (= G44), C52 (= C45), K56 (= K49), H119 (≠ L111), G120 (= G112), A148 (= A139), S149 (≠ T140), G150 (= G141), S169 (= S160), I190 (= I181), R277 (= R265), G316 (= G302), D317 (= D303), M323 (≠ Q309), L324 (= L310), A325 (= A311), H326 (= H312), H449 (= H434), P450 (= P435)
- binding nicotinamide-adenine-dinucleotide: I185 (≠ V176), G186 (= G177), G188 (= G179), V189 (≠ F180), I190 (= I181), L208 (≠ V199), E209 (≠ D200), A210 (= A201), V243 (= V234), V275 (= V263), G276 (= G264)
Sites not aligning to the query:
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
36% identity, 98% coverage: 3:444/453 of query aligns to 4:460/473 of 5u8wA
- active site: P13 (= P12), L44 (= L36), C48 (= C40), C53 (= C45), S56 (≠ T48), G82 (vs. gap), V83 (= V74), V190 (≠ F180), E194 (= E184), S330 (= S315), F448 (= F432), H450 (= H434), E455 (= E439)
- binding flavin-adenine dinucleotide: I9 (= I8), G12 (= G11), P13 (= P12), G14 (= G13), E33 (= E32), K34 (= K33), G46 (= G38), T47 (= T39), C48 (= C40), G52 (= G44), C53 (= C45), K57 (= K49), H120 (≠ L111), G121 (= G112), A149 (= A139), S150 (≠ T140), G151 (= G141), S170 (= S160), G317 (= G302), D318 (= D303), M324 (≠ Q309), L325 (= L310), A326 (= A311), H327 (= H312), Y357 (= Y343), H450 (= H434), P451 (= P435)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (≠ V176), G189 (= G179), V190 (≠ F180), I191 (= I181), E194 (= E184), E210 (≠ D200), A211 (= A201), L212 (≠ M202), A275 (= A262), V276 (= V263), G277 (= G264), R278 (= R265), M324 (≠ Q309), L325 (= L310), V355 (= V341), Y357 (= Y343)
Sites not aligning to the query:
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
35% identity, 98% coverage: 3:444/453 of query aligns to 7:458/470 of 6uziC
- active site: C45 (= C40), C50 (= C45), S53 (≠ T48), V187 (≠ F180), E191 (= E184), H448 (= H434), E453 (= E439)
- binding flavin-adenine dinucleotide: I12 (= I8), G13 (= G9), G15 (= G11), P16 (= P12), G17 (= G13), E36 (= E32), K37 (= K33), G43 (= G38), T44 (= T39), C45 (= C40), G49 (= G44), C50 (= C45), S53 (≠ T48), K54 (= K49), V117 (≠ L111), G118 (= G112), T147 (= T140), G148 (= G141), I188 (= I181), R276 (= R265), D316 (= D303), M322 (≠ Q309), L323 (= L310), A324 (= A311)
- binding zinc ion: H448 (= H434), E453 (= E439)
P09622 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; EC 1.8.1.4 from Homo sapiens (Human) (see 14 papers)
36% identity, 97% coverage: 4:444/453 of query aligns to 43:497/509 of P09622
- 71:80 (vs. 32:40, 70% identical) binding FAD
- K72 (= K33) to E: in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX; dbSNP:rs121964987
- K89 (= K49) binding FAD; mutation to E: Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- K104 (≠ E59) to T: in dbSNP:rs1130477
- G154 (= G112) binding FAD
- TGS 183:185 (= TGS 140:142) binding FAD
- 220:227 (vs. 177:184, 75% identical) binding NAD(+)
- E243 (≠ D200) binding NAD(+)
- V278 (= V234) binding NAD(+)
- G314 (= G264) binding NAD(+)
- D355 (= D303) binding FAD
- MLAH 361:364 (≠ QLAH 309:312) binding FAD
- E375 (≠ S323) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (≠ A332) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (≠ N395) 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 (≠ P413) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ E420) 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 (= D426) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (≠ G429) 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 (≠ F432) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
- P488 (= P435) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
- S491 (≠ D438) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
- E492 (= E439) mutation to Q: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- R495 (≠ L442) 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.
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
36% identity, 97% coverage: 4:444/453 of query aligns to 6:460/472 of 1zmdA
- active site: L39 (= L36), C43 (= C40), C48 (= C45), S51 (≠ T48), V186 (≠ F180), E190 (= E184), H448 (≠ F432), H450 (= H434), E455 (= E439)
- binding flavin-adenine dinucleotide: I10 (= I8), G11 (= G9), G13 (= G11), P14 (= P12), G15 (= G13), E34 (= E32), K35 (= K33), N36 (≠ G34), G41 (= G38), T42 (= T39), C43 (= C40), G47 (= G44), C48 (= C45), K52 (= K49), Y116 (≠ L111), G117 (= G112), T146 (= T140), G147 (= G141), S166 (= S160), R278 (= R265), F281 (≠ V268), G317 (= G302), D318 (= D303), M324 (≠ Q309), L325 (= L310), A326 (= A311), H327 (= H312)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (≠ V176), G183 (= G177), G185 (= G179), V186 (≠ F180), I187 (= I181), E190 (= E184), E206 (≠ D200), F207 (≠ A201), L208 (≠ M202), I276 (≠ V263), G277 (= G264), R278 (= R265), M324 (≠ Q309), L325 (= L310), V355 (= V341), Y357 (= Y343)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
36% identity, 97% coverage: 4:444/453 of query aligns to 6:460/472 of 1zmcA
- active site: L39 (= L36), C43 (= C40), C48 (= C45), S51 (≠ T48), V186 (≠ F180), E190 (= E184), H448 (≠ F432), H450 (= H434), E455 (= E439)
- binding flavin-adenine dinucleotide: I10 (= I8), G11 (= G9), G13 (= G11), P14 (= P12), G15 (= G13), E34 (= E32), K35 (= K33), N36 (≠ G34), G41 (= G38), T42 (= T39), C43 (= C40), G47 (= G44), C48 (= C45), K52 (= K49), Y116 (≠ L111), G117 (= G112), T146 (= T140), G147 (= G141), S166 (= S160), I187 (= I181), F281 (≠ V268), G317 (= G302), D318 (= D303), M324 (≠ Q309), L325 (= L310), A326 (= A311), H327 (= H312)
- binding nicotinamide-adenine-dinucleotide: G183 (= G177), G185 (= G179), V205 (= V199), E206 (≠ D200), F207 (≠ A201), L208 (≠ M202), K240 (≠ R233), V241 (= V234), I276 (≠ V263), G277 (= G264), R278 (= R265), R297 (= R283), M324 (≠ Q309)
6hg8B Crystal structure of the r460g disease-causing mutant of the human dihydrolipoamide dehydrogenase.
36% identity, 97% coverage: 4:441/453 of query aligns to 16:467/482 of 6hg8B
- active site: C53 (= C40), C58 (= C45), S61 (≠ T48), V196 (≠ F180), E200 (= E184), H460 (= H434), E465 (= E439)
- binding flavin-adenine dinucleotide: I20 (= I8), G23 (= G11), P24 (= P12), G25 (= G13), E44 (= E32), K45 (= K33), N46 (≠ G34), G51 (= G38), T52 (= T39), C53 (= C40), G57 (= G44), C58 (= C45), K62 (= K49), Y126 (≠ L111), G127 (= G112), T156 (= T140), G157 (= G141), I197 (= I181), R288 (= R265), F291 (≠ V268), G327 (= G302), D328 (= D303), M334 (≠ Q309), L335 (= L310), A336 (= A311), H337 (= H312)
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
34% identity, 98% coverage: 3:444/453 of query aligns to 1:455/465 of 3urhB
- active site: Y35 (≠ L36), C39 (= C40), C44 (= C45), S47 (≠ T48), V183 (≠ F180), E187 (= E184), H443 (≠ F432), H445 (= H434), E450 (= E439)
- binding flavin-adenine dinucleotide: I6 (= I8), G7 (= G9), G9 (= G11), P10 (= P12), G11 (= G13), E30 (= E32), K31 (= K33), G37 (= G38), T38 (= T39), C39 (= C40), G43 (= G44), C44 (= C45), K48 (= K49), T111 (≠ L111), G112 (= G112), A140 (= A139), T141 (= T140), G142 (= G141), I184 (= I181), R273 (= R265), G312 (= G302), D313 (= D303), M319 (≠ Q309), L320 (= L310), A321 (= A311), H322 (= H312)
6bz0A 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from acinetobacter baumannii in complex with fad.
34% identity, 98% coverage: 3:444/453 of query aligns to 2:457/469 of 6bz0A
- active site: C45 (= C40), C50 (= C45), S53 (≠ T48), V187 (≠ F180), E191 (= E184), H447 (= H434), E452 (= E439)
- binding flavin-adenine dinucleotide: I7 (= I8), G10 (= G11), P11 (= P12), G12 (= G13), E31 (= E32), K32 (= K33), R33 (≠ G34), G43 (= G38), T44 (= T39), C45 (= C40), G49 (= G44), C50 (= C45), K54 (= K49), T117 (≠ L111), G118 (= G112), S147 (≠ T140), G148 (= G141), S167 (= S160), I188 (= I181), R275 (= R265), Y278 (≠ V268), D315 (= D303), M321 (≠ Q309), L322 (= L310), A323 (= A311), A326 (= A314), Y354 (= Y343)
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)
33% identity, 96% coverage: 5:441/453 of query aligns to 9:452/474 of P0A9P0
- K220 (= K215) modified: N6-acetyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
4jdrA Dihydrolipoamide dehydrogenase of pyruvate dehydrogenase from escherichia coli (see paper)
33% identity, 96% coverage: 5:441/453 of query aligns to 8:451/471 of 4jdrA
- active site: P15 (= P12), L40 (= L36), C44 (= C40), C49 (= C45), S52 (≠ T48), E77 (= E73), P78 (≠ V74), I184 (≠ F180), E188 (= E184), V324 (≠ S315), H442 (≠ F432), H444 (= H434), E449 (= E439)
- binding flavin-adenine dinucleotide: G12 (= G9), G14 (= G11), P15 (= P12), A16 (≠ G13), E35 (= E32), R36 (≠ K33), Y37 (≠ G34), V43 (≠ T39), C44 (= C40), G48 (= G44), C49 (= C45), K53 (= K49), L115 (= L111), G116 (= G112), A144 (≠ T140), G145 (= G141), I185 (= I181), G311 (= G302), D312 (= D303), M318 (≠ Q309), L319 (= L310), A320 (= A311), H321 (= H312)
Sites not aligning to the query:
2eq6A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8
37% identity, 98% coverage: 3:447/453 of query aligns to 4:450/460 of 2eq6A
- active site: V37 (≠ L36), C41 (= C40), C46 (= C45), T49 (= T48), A176 (≠ F180), E180 (= E184), H435 (≠ F432), H437 (= H434), E442 (= E439)
- binding flavin-adenine dinucleotide: I9 (= I8), G10 (= G9), G12 (= G11), P13 (= P12), G14 (= G13), E33 (= E32), A34 (≠ K33), G39 (= G38), V40 (≠ T39), C41 (= C40), G45 (= G44), C46 (= C45), K50 (= K49), F111 (≠ L111), A112 (≠ G112), A135 (= A139), T136 (= T140), G137 (= G141), S155 (= S160), R269 (≠ V268), D306 (= D303), L312 (≠ Q309), L313 (= L310), A314 (= A311), H315 (= H312), Y344 (= Y343)
Sites not aligning to the query:
Query Sequence
>WP_018125192.1 NCBI__GCF_000375485.1:WP_018125192.1
MAYDIAVIGAGPGGYDAATEAASFGLKVALVEKGDLGGTCLNWGCIPTKVILGATSAVEE
LASQRKMKVADGEVNIDYAALATRKDKLIAGTRKAMVQRLKQLGVDLYTGLGRIPTSGKV
SVETPEGTQEIEAANIIVATGSKPTFFPGLAPDGERVMDSNDFLAMTEMPESLIVVGAGF
IGLEMAQAAHRMGAKVTVVDAMDRVAPLEDPEVSKTLQSIFKRWKWDVRLGVRVQSVKTE
SDKAVLTLEGGDVVEADKALVAVGRGPVSNNLGLEELGATLERGTIKVNEYLEAAPGIYA
IGDVNGIIQLAHAASHQAHYAASRIAGKTEAAYESGPVPSVLYGAPETMRVGLMPEQLRV
EGRPCETSKFAFAGNPIAQSHASTQGFCKVIWSDNKVVGVTAVGHDASRLTTPATMIVQE
GWTPNDIHGTIFPHPSLDEALLNALKAERTECK
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