SitesBLAST
Comparing WP_035700441.1 NCBI__GCF_000691145.1:WP_035700441.1 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)
P18925 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Azotobacter vinelandii (see 2 papers)
39% identity, 99% coverage: 1:454/460 of query aligns to 1:465/477 of P18925
- 34:49 (vs. 34:42, 38% identical) binding FAD
- C49 (= C42) modified: Disulfide link with 54, Redox-active
- C54 (= C47) modified: Disulfide link with 49, Redox-active
- K58 (= K51) binding FAD
- D319 (= D308) binding FAD
- A327 (= A316) 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)
39% identity, 98% coverage: 2:454/460 of query aligns to 1:464/472 of 3ladA
- active site: L44 (= L38), C48 (= C42), C53 (= C47), S56 (= S50), V190 (= V182), E194 (= E186), F448 (≠ H438), H450 (= H440), E455 (= E445)
- binding flavin-adenine dinucleotide: I9 (= I10), G10 (= G11), G12 (= G13), P13 (= P14), E33 (= E34), K34 (≠ E35), G46 (= G40), T47 (= T41), C48 (= C42), G52 (= G46), C53 (= C47), H120 (≠ R113), G121 (= G114), A149 (= A141), S150 (≠ T142), G151 (= G143), I191 (= I183), R278 (= R271), D318 (= D308), L325 (= L315), A326 (= A316)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
39% identity, 98% coverage: 5:457/460 of query aligns to 7:465/470 of 6uziC
- active site: C45 (= C42), C50 (= C47), S53 (= S50), V187 (= V182), E191 (= E186), H448 (= H440), E453 (= E445)
- binding flavin-adenine dinucleotide: I12 (= I10), G13 (= G11), G15 (= G13), P16 (= P14), G17 (= G15), E36 (= E34), K37 (≠ E35), G43 (= G40), T44 (= T41), C45 (= C42), G49 (= G46), C50 (= C47), S53 (= S50), K54 (= K51), V117 (≠ R113), G118 (= G114), T147 (= T142), G148 (= G143), I188 (= I183), R276 (= R271), D316 (= D308), M322 (≠ Q314), L323 (= L315), A324 (= A316)
- binding zinc ion: H448 (= H440), E453 (= E445)
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
39% identity, 99% coverage: 1:454/460 of query aligns to 3:467/477 of 5u8uD
- active site: P16 (= P14), L47 (= L38), C51 (= C42), C56 (= C47), S59 (= S50), G85 (≠ E75), V86 (≠ M76), V193 (= V182), E197 (= E186), S333 (≠ M320), F451 (≠ H438), H453 (= H440), E458 (= E445)
- binding flavin-adenine dinucleotide: I12 (= I10), G15 (= G13), P16 (= P14), G17 (= G15), E36 (= E34), K37 (≠ E35), G49 (= G40), T50 (= T41), C51 (= C42), G55 (= G46), C56 (= C47), K60 (= K51), H123 (≠ R113), G124 (= G114), A152 (= A141), S153 (≠ T142), G154 (= G143), I194 (= I183), R281 (= R271), G320 (= G307), D321 (= D308), M327 (≠ Q314), L328 (= L315), A329 (= A316), H330 (= H317), H453 (= H440), P454 (= P441)
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)
39% identity, 99% coverage: 1:454/460 of query aligns to 1:465/478 of P14218
- M1 (= M1) modified: Initiator methionine, Removed
- 34:49 (vs. 34:42, 38% identical) binding FAD
- C49 (= C42) modified: Disulfide link with 54, Redox-active
- C54 (= C47) modified: Disulfide link with 49, Redox-active
- K58 (= K51) binding FAD
- G122 (= G114) binding FAD
- D319 (= D308) binding FAD
- A327 (= A316) binding FAD
6bz0A 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from acinetobacter baumannii in complex with fad.
39% identity, 98% coverage: 5:454/460 of query aligns to 2:461/469 of 6bz0A
- active site: C45 (= C42), C50 (= C47), S53 (= S50), V187 (= V182), E191 (= E186), H447 (= H440), E452 (= E445)
- binding flavin-adenine dinucleotide: I7 (= I10), G10 (= G13), P11 (= P14), G12 (= G15), E31 (= E34), K32 (≠ E35), R33 (≠ D36), G43 (= G40), T44 (= T41), C45 (= C42), G49 (= G46), C50 (= C47), K54 (= K51), T117 (≠ R113), G118 (= G114), S147 (≠ T142), G148 (= G143), S167 (≠ T161), I188 (= I183), R275 (= R271), Y278 (≠ N274), D315 (= D308), M321 (≠ Q314), L322 (= L315), A323 (= A316), A326 (= A319), Y354 (= Y347)
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
38% identity, 98% coverage: 2:454/460 of query aligns to 1:464/473 of 5u8wA
- active site: P13 (= P14), L44 (= L38), C48 (= C42), C53 (= C47), S56 (= S50), G82 (≠ E75), V83 (≠ M76), V190 (= V182), E194 (= E186), S330 (≠ M320), F448 (≠ H438), H450 (= H440), E455 (= E445)
- binding flavin-adenine dinucleotide: I9 (= I10), G12 (= G13), P13 (= P14), G14 (= G15), E33 (= E34), K34 (≠ E35), G46 (= G40), T47 (= T41), C48 (= C42), G52 (= G46), C53 (= C47), K57 (= K51), H120 (≠ R113), G121 (= G114), A149 (= A141), S150 (≠ T142), G151 (= G143), S170 (≠ T161), G317 (= G307), D318 (= D308), M324 (≠ Q314), L325 (= L315), A326 (= A316), H327 (= H317), Y357 (= Y347), H450 (= H440), P451 (= P441)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (= I178), G189 (= G181), V190 (= V182), I191 (= I183), E194 (= E186), E210 (= E202), A211 (= A203), L212 (≠ A204), A275 (≠ C268), V276 (= V269), G277 (= G270), R278 (= R271), M324 (≠ Q314), L325 (= L315), V355 (≠ C345), Y357 (= Y347)
Sites not aligning to the query:
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
38% identity, 98% coverage: 3:454/460 of query aligns to 1:463/472 of 5u8vA
- active site: P12 (= P14), L43 (= L38), C47 (= C42), C52 (= C47), S55 (= S50), G81 (≠ E75), V82 (≠ M76), V189 (= V182), E193 (= E186), S329 (≠ M320), F447 (≠ H438), H449 (= H440), E454 (= E445)
- binding flavin-adenine dinucleotide: I8 (= I10), G11 (= G13), P12 (= P14), G13 (= G15), E32 (= E34), G45 (= G40), T46 (= T41), C47 (= C42), G51 (= G46), C52 (= C47), K56 (= K51), H119 (≠ R113), G120 (= G114), A148 (= A141), S149 (≠ T142), G150 (= G143), S169 (≠ T161), I190 (= I183), R277 (= R271), G316 (= G307), D317 (= D308), M323 (≠ Q314), L324 (= L315), A325 (= A316), H326 (= H317), H449 (= H440), P450 (= P441)
- binding nicotinamide-adenine-dinucleotide: I185 (= I178), G186 (= G179), G188 (= G181), V189 (= V182), I190 (= I183), L208 (≠ I201), E209 (= E202), A210 (= A203), V243 (≠ T234), V275 (= V269), G276 (= G270)
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.
38% identity, 99% coverage: 1:454/460 of query aligns to 1:465/475 of 6awaA
- active site: L45 (= L38), C49 (= C42), C54 (= C47), S57 (= S50), V191 (= V182), E195 (= E186), F449 (≠ H438), H451 (= H440), E456 (= E445)
- binding adenosine monophosphate: I187 (= I178), E211 (= E202), A212 (= A203), L213 (≠ A204), V245 (= V236), V277 (= V269)
- binding flavin-adenine dinucleotide: I10 (= I10), G13 (= G13), P14 (= P14), G15 (= G15), E34 (= E34), K35 (≠ E35), T48 (= T41), C49 (= C42), G53 (= G46), C54 (= C47), K58 (= K51), H121 (≠ R113), G122 (= G114), S151 (≠ T142), G152 (= G143), I192 (= I183), R279 (= R271), G318 (= G307), D319 (= D308), M325 (≠ Q314), L326 (= L315), A327 (= A316), Y358 (= Y347)
Sites not aligning to the query:
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
37% identity, 98% coverage: 5:457/460 of query aligns to 1:462/465 of 3urhB
- active site: Y35 (≠ L38), C39 (= C42), C44 (= C47), S47 (= S50), V183 (= V182), E187 (= E186), H443 (= H438), H445 (= H440), E450 (= E445)
- binding flavin-adenine dinucleotide: I6 (= I10), G7 (= G11), G9 (= G13), P10 (= P14), G11 (= G15), E30 (= E34), K31 (≠ E35), G37 (= G40), T38 (= T41), C39 (= C42), G43 (= G46), C44 (= C47), K48 (= K51), T111 (≠ R113), G112 (= G114), A140 (= A141), T141 (= T142), G142 (= G143), I184 (= I183), R273 (= R271), G312 (= G307), D313 (= D308), M319 (≠ Q314), L320 (= L315), A321 (= A316), H322 (= H317)
P11959 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
37% identity, 96% coverage: 9:451/460 of query aligns to 14:457/470 of P11959
- 39:47 (vs. 34:42, 56% identical) binding FAD
- K56 (= K51) binding FAD
- D314 (= D308) binding FAD
- A322 (= A316) binding FAD
1ebdA Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetylase (see paper)
37% identity, 96% coverage: 9:451/460 of query aligns to 8:451/455 of 1ebdA
- active site: P13 (= P14), L37 (= L38), C41 (= C42), C46 (= C47), S49 (= S50), N74 (≠ E75), V75 (≠ M76), Y180 (≠ V182), E184 (= E186), S320 (≠ M320), H438 (= H438), H440 (= H440), E445 (= E445)
- binding flavin-adenine dinucleotide: G10 (= G11), G12 (= G13), P13 (= P14), V32 (≠ I33), E33 (= E34), K34 (≠ E35), G39 (= G40), V40 (≠ T41), C41 (= C42), G45 (= G46), C46 (= C47), K50 (= K51), E112 (≠ R113), A113 (≠ G114), T141 (= T142), G142 (= G143), Y180 (≠ V182), I181 (= I183), R268 (= R271), D308 (= D308), A314 (≠ Q314), L315 (= L315), A316 (= A316)
2eq6A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8
39% identity, 98% coverage: 3:451/460 of query aligns to 2:448/460 of 2eq6A
- active site: V37 (≠ L38), C41 (= C42), C46 (= C47), T49 (≠ S50), A176 (≠ V182), E180 (= E186), H435 (= H438), H437 (= H440), E442 (= E445)
- binding flavin-adenine dinucleotide: I9 (= I10), G10 (= G11), G12 (= G13), P13 (= P14), G14 (= G15), E33 (= E34), A34 (≠ E35), G39 (= G40), V40 (≠ T41), C41 (= C42), G45 (= G46), C46 (= C47), K50 (= K51), F111 (≠ R113), A112 (≠ G114), A135 (= A141), T136 (= T142), G137 (= G143), S155 (≠ T161), R269 (≠ N274), D306 (= D308), L312 (≠ Q314), L313 (= L315), A314 (= A316), H315 (= H317), Y344 (= Y347)
Sites not aligning to the query:
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
38% identity, 97% coverage: 6:452/460 of query aligns to 6:462/472 of 1zmdA
- active site: L39 (= L38), C43 (= C42), C48 (= C47), S51 (= S50), V186 (= V182), E190 (= E186), H448 (= H438), H450 (= H440), E455 (= E445)
- binding flavin-adenine dinucleotide: I10 (= I10), G11 (= G11), G13 (= G13), P14 (= P14), G15 (= G15), E34 (= E34), K35 (≠ E35), N36 (≠ D36), G41 (= G40), T42 (= T41), C43 (= C42), G47 (= G46), C48 (= C47), K52 (= K51), Y116 (≠ R113), G117 (= G114), T146 (= T142), G147 (= G143), S166 (= S162), R278 (= R271), F281 (≠ N274), G317 (= G307), D318 (= D308), M324 (≠ Q314), L325 (= L315), A326 (= A316), H327 (= H317)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (= I178), G183 (= G179), G185 (= G181), V186 (= V182), I187 (= I183), E190 (= E186), E206 (= E202), F207 (≠ A203), L208 (≠ A204), I276 (≠ V269), G277 (= G270), R278 (= R271), M324 (≠ Q314), L325 (= L315), V355 (≠ C345), Y357 (= Y347)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
38% identity, 97% coverage: 6:452/460 of query aligns to 6:462/472 of 1zmcA
- active site: L39 (= L38), C43 (= C42), C48 (= C47), S51 (= S50), V186 (= V182), E190 (= E186), H448 (= H438), H450 (= H440), E455 (= E445)
- binding flavin-adenine dinucleotide: I10 (= I10), G11 (= G11), G13 (= G13), P14 (= P14), G15 (= G15), E34 (= E34), K35 (≠ E35), N36 (≠ D36), G41 (= G40), T42 (= T41), C43 (= C42), G47 (= G46), C48 (= C47), K52 (= K51), Y116 (≠ R113), G117 (= G114), T146 (= T142), G147 (= G143), S166 (= S162), I187 (= I183), F281 (≠ N274), G317 (= G307), D318 (= D308), M324 (≠ Q314), L325 (= L315), A326 (= A316), H327 (= H317)
- binding nicotinamide-adenine-dinucleotide: G183 (= G179), G185 (= G181), V205 (≠ I201), E206 (= E202), F207 (≠ A203), L208 (≠ A204), K240 (≠ T235), V241 (= V236), I276 (≠ V269), G277 (= G270), R278 (= R271), R297 (≠ F289), M324 (≠ Q314)
P09622 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; EC 1.8.1.4 from Homo sapiens (Human) (see 14 papers)
38% identity, 97% coverage: 6:452/460 of query aligns to 43:499/509 of P09622
- 71:80 (vs. 34:42, 60% identical) binding FAD
- K72 (≠ E35) to E: in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX; dbSNP:rs121964987
- K89 (= K51) binding FAD; mutation to E: Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- K104 (≠ E64) to T: in dbSNP:rs1130477
- G154 (= G114) binding FAD
- TGS 183:185 (= TGS 142:144) binding FAD
- 220:227 (vs. 179:186, 75% identical) binding NAD(+)
- E243 (= E202) binding NAD(+)
- V278 (= V236) binding NAD(+)
- G314 (= G270) binding NAD(+)
- D355 (= D308) binding FAD
- MLAH 361:364 (≠ QLAH 314:317) binding FAD
- E375 (≠ S328) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (≠ R336) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (≠ G401) 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 (= E419) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ L426) 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 (≠ E432) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (≠ K435) 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 (= H438) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
- P488 (= P441) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
- S491 (= S444) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
- E492 (= E445) mutation to Q: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- R495 (≠ Y448) 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.
38% identity, 97% coverage: 6:452/460 of query aligns to 16:472/482 of 6hg8B
- active site: C53 (= C42), C58 (= C47), S61 (= S50), V196 (= V182), E200 (= E186), H460 (= H440), E465 (= E445)
- binding flavin-adenine dinucleotide: I20 (= I10), G23 (= G13), P24 (= P14), G25 (= G15), E44 (= E34), K45 (≠ E35), N46 (≠ D36), G51 (= G40), T52 (= T41), C53 (= C42), G57 (= G46), C58 (= C47), K62 (= K51), Y126 (≠ R113), G127 (= G114), T156 (= T142), G157 (= G143), I197 (= I183), R288 (= R271), F291 (≠ N274), G327 (= G307), D328 (= D308), M334 (≠ Q314), L335 (= L315), A336 (= A316), H337 (= H317)
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
36% identity, 97% coverage: 5:452/460 of query aligns to 2:446/452 of 2eq7A
- active site: P11 (= P14), L36 (= L38), C40 (= C42), C45 (= C47), S48 (= S50), G72 (= G70), V73 (≠ I71), V177 (= V182), E181 (= E186), S314 (≠ M320), H432 (= H438), H434 (= H440), E439 (= E445)
- binding flavin-adenine dinucleotide: G10 (= G13), P11 (= P14), G12 (= G15), E31 (= E34), K32 (vs. gap), G38 (= G40), T39 (= T41), C40 (= C42), R42 (≠ N44), G44 (= G46), C45 (= C47), K49 (= K51), T110 (≠ R113), A111 (≠ G114), T137 (= T142), G138 (= G143), S157 (= S162), I178 (= I183), R262 (= R271), Y265 (≠ N274), D302 (= D308), M308 (≠ Q314), L309 (= L315), A310 (= A316), H311 (= H317), Y341 (= Y347)
- binding nicotinamide-adenine-dinucleotide: W146 (≠ I151), G174 (= G179), G176 (= G181), V177 (= V182), I178 (= I183), E197 (= E202), Y198 (≠ A203), V231 (= V236), V260 (= V269), G261 (= G270), R262 (= R271), M308 (≠ Q314), L309 (= L315), V339 (≠ C345)
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
36% identity, 97% coverage: 5:452/460 of query aligns to 2:446/455 of 2yquB
- active site: P11 (= P14), L36 (= L38), C40 (= C42), C45 (= C47), S48 (= S50), G72 (= G70), V73 (≠ I71), V177 (= V182), E181 (= E186), S314 (≠ M320), H432 (= H438), H434 (= H440), E439 (= E445)
- binding carbonate ion: A310 (= A316), S314 (≠ M320), S423 (≠ T429), D426 (≠ E432)
- binding flavin-adenine dinucleotide: G8 (= G11), G10 (= G13), P11 (= P14), G12 (= G15), E31 (= E34), K32 (vs. gap), G38 (= G40), T39 (= T41), C40 (= C42), R42 (≠ N44), G44 (= G46), C45 (= C47), K49 (= K51), T110 (≠ R113), A111 (≠ G114), T137 (= T142), G138 (= G143), I178 (= I183), Y265 (≠ N274), G301 (= G307), D302 (= D308), M308 (≠ Q314), L309 (= L315), A310 (= A316), H311 (= H317)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
36% identity, 97% coverage: 5:452/460 of query aligns to 2:446/455 of 2yquA
- active site: P11 (= P14), L36 (= L38), C40 (= C42), C45 (= C47), S48 (= S50), G72 (= G70), V73 (≠ I71), V177 (= V182), E181 (= E186), S314 (≠ M320), H432 (= H438), H434 (= H440), E439 (= E445)
- binding flavin-adenine dinucleotide: G8 (= G11), G10 (= G13), P11 (= P14), G12 (= G15), E31 (= E34), K32 (vs. gap), G38 (= G40), T39 (= T41), C40 (= C42), R42 (≠ N44), G44 (= G46), C45 (= C47), K49 (= K51), T110 (≠ R113), A111 (≠ G114), T137 (= T142), G138 (= G143), S157 (= S162), I178 (= I183), Y265 (≠ N274), G301 (= G307), D302 (= D308), M308 (≠ Q314), L309 (= L315), A310 (= A316)
Query Sequence
>WP_035700441.1 NCBI__GCF_000691145.1:WP_035700441.1
MTKTYDLTVIGGGPGGYTAALQAAERGHKVALIEEDFLGGTCLNRGCIPSKTLLKHAEVI
ESIEKAKSWGIETGEMVLSFDKMRKRKDDVIEKLRGGIAFLLKQGKIDVYNGRGTAVTKN
RIDIEKQDGSETIETKELIIATGSSPAIPPIPGLKEIQFDTSDTIFDIPDIPASVVIIGG
GVIGLELACIFQSLQSKVTIIEAAPSIIPQEDEEASKLLEKELKKKGIHIAKKTTVTEVT
ESEGVKAIHATDDKGETHIFTAERLLVCVGRRPNVSAVSQLDLQLDGPFIKVNDEMKTSV
EGVYAIGDVAGGYQLAHAAMAEAAVAVSNICGEPERMNHDIVPRCIYTLPEVASVGLTEK
EAKAKGLNVRAERFDLAASGKALAAGVQTGFIKLVYDTVYGEVIGATMVGPHVTEMISEA
SSFMYLEGTAEEMAKMIHPHPTISEGFYEAALDIVSKLRK
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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