SitesBLAST
Comparing RR42_RS21770 FitnessBrowser__Cup4G11:RR42_RS21770 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)
P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 from Pseudomonas fluorescens (see 2 papers)
41% identity, 100% coverage: 3:466/466 of query aligns to 2:472/478 of P14218
- 34:49 (vs. 35:43, 38% identical) binding
- C49 (= C43) modified: Disulfide link with 54, Redox-active
- C54 (= C48) modified: Disulfide link with 49, Redox-active
- K58 (= K52) binding
- G122 (= G115) binding
- D319 (= D312) binding
- A327 (= A320) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
41% identity, 100% coverage: 3:466/466 of query aligns to 4:474/477 of 5u8uD
- active site: P16 (= P15), L47 (= L39), C51 (= C43), C56 (= C48), S59 (≠ T51), G85 (≠ P76), V86 (≠ P77), V193 (≠ A184), E197 (= E188), S333 (= S324), F451 (≠ L443), H453 (= H445), E458 (= E450)
- binding flavin-adenine dinucleotide: I12 (≠ V11), G15 (= G14), P16 (= P15), G17 (= G16), E36 (= E35), K37 (= K36), G49 (= G41), T50 (≠ I42), C51 (= C43), G55 (= G47), C56 (= C48), K60 (= K52), H123 (= H114), G124 (= G115), A152 (= A143), S153 (≠ T144), G154 (= G145), I194 (= I185), R281 (≠ I273), G320 (= G311), D321 (= D312), M327 (≠ W318), L328 (= L319), A329 (= A320), H330 (= H321), H453 (= H445), P454 (= P446)
Sites not aligning to the query:
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
41% identity, 100% coverage: 3:466/466 of query aligns to 1:471/473 of 5u8wA
- active site: P13 (= P15), L44 (= L39), C48 (= C43), C53 (= C48), S56 (≠ T51), G82 (≠ P76), V83 (≠ P77), V190 (≠ A184), E194 (= E188), S330 (= S324), F448 (≠ L443), H450 (= H445), E455 (= E450)
- binding flavin-adenine dinucleotide: I9 (≠ V11), G12 (= G14), P13 (= P15), G14 (= G16), E33 (= E35), K34 (= K36), G46 (= G41), T47 (≠ I42), C48 (= C43), G52 (= G47), C53 (= C48), K57 (= K52), H120 (= H114), G121 (= G115), A149 (= A143), S150 (≠ T144), G151 (= G145), S170 (≠ Y164), G317 (= G311), D318 (= D312), M324 (≠ W318), L325 (= L319), A326 (= A320), H327 (= H321), Y357 (= Y352), H450 (= H445), P451 (= P446)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (≠ V180), G189 (= G183), V190 (≠ A184), I191 (= I185), E194 (= E188), E210 (= E204), A211 (≠ M205), L212 (≠ A206), A275 (= A270), V276 (≠ A271), G277 (= G272), R278 (≠ I273), M324 (≠ W318), L325 (= L319), V355 (≠ C350), Y357 (= Y352)
Sites not aligning to the query:
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
41% identity, 99% coverage: 4:466/466 of query aligns to 1:470/472 of 5u8vA
- active site: P12 (= P15), L43 (= L39), C47 (= C43), C52 (= C48), S55 (≠ T51), G81 (≠ P76), V82 (≠ P77), V189 (≠ A184), E193 (= E188), S329 (= S324), F447 (≠ L443), H449 (= H445), E454 (= E450)
- binding flavin-adenine dinucleotide: I8 (≠ V11), G11 (= G14), P12 (= P15), G13 (= G16), E32 (= E35), G45 (= G41), T46 (≠ I42), C47 (= C43), G51 (= G47), C52 (= C48), K56 (= K52), H119 (= H114), G120 (= G115), A148 (= A143), S149 (≠ T144), G150 (= G145), S169 (≠ Y164), I190 (= I185), R277 (≠ I273), G316 (= G311), D317 (= D312), M323 (≠ W318), L324 (= L319), A325 (= A320), H326 (= H321), H449 (= H445), P450 (= P446)
- binding nicotinamide-adenine-dinucleotide: I185 (≠ V180), G186 (= G181), G188 (= G183), V189 (≠ A184), I190 (= I185), L208 (≠ V203), E209 (= E204), A210 (≠ M205), V243 (≠ I238), V275 (≠ A271), G276 (= G272)
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)
40% identity, 100% coverage: 3:466/466 of query aligns to 2:472/477 of P18925
- 34:49 (vs. 35:43, 38% identical) binding
- C49 (= C43) modified: Disulfide link with 54, Redox-active
- C54 (= C48) modified: Disulfide link with 49, Redox-active
- K58 (= K52) binding
- D319 (= D312) binding
- A327 (= A320) 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)
40% identity, 100% coverage: 3:466/466 of query aligns to 1:471/472 of 3ladA
- active site: L44 (= L39), C48 (= C43), C53 (= C48), S56 (≠ T51), V190 (≠ A184), E194 (= E188), F448 (≠ L443), H450 (= H445), E455 (= E450)
- binding flavin-adenine dinucleotide: I9 (≠ V11), G10 (= G12), G12 (= G14), P13 (= P15), E33 (= E35), K34 (= K36), G46 (= G41), T47 (≠ I42), C48 (= C43), G52 (= G47), C53 (= C48), H120 (= H114), G121 (= G115), A149 (= A143), S150 (≠ T144), G151 (= G145), I191 (= I185), R278 (≠ I273), D318 (= D312), L325 (= L319), A326 (= A320)
6awaA 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from pseudomonas putida in complex with fad and adenosine-5'-monophosphate.
40% identity, 99% coverage: 6:466/466 of query aligns to 5:472/475 of 6awaA
- active site: L45 (= L39), C49 (= C43), C54 (= C48), S57 (≠ T51), V191 (≠ A184), E195 (= E188), F449 (≠ L443), H451 (= H445), E456 (= E450)
- binding adenosine monophosphate: I187 (≠ V180), E211 (= E204), A212 (≠ M205), L213 (≠ A206), V245 (≠ I238), V277 (≠ A271)
- binding flavin-adenine dinucleotide: I10 (≠ V11), G13 (= G14), P14 (= P15), G15 (= G16), E34 (= E35), K35 (= K36), T48 (≠ I42), C49 (= C43), G53 (= G47), C54 (= C48), K58 (= K52), H121 (= H114), G122 (= G115), S151 (≠ T144), G152 (= G145), I192 (= I185), R279 (≠ I273), G318 (= G311), D319 (= D312), M325 (≠ W318), L326 (= L319), A327 (= A320), Y358 (= Y352)
Sites not aligning to the query:
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)
39% identity, 99% coverage: 7:466/466 of query aligns to 39:501/501 of P31023
- 67:76 (vs. 35:43, 60% identical) binding
- C76 (= C43) modified: Disulfide link with 81, Redox-active
- C81 (= C48) modified: Disulfide link with 76, Redox-active
- G149 (= G115) binding
- D348 (= D312) binding
- MLAH 354:357 (≠ WLAH 318:321) binding
Sites not aligning to the query:
- 1:31 modified: transit peptide, Mitochondrion
1dxlA Dihydrolipoamide dehydrogenase of glycine decarboxylase from pisum sativum (see paper)
39% identity, 99% coverage: 7:466/466 of query aligns to 5:467/467 of 1dxlA
- active site: L38 (= L39), C42 (= C43), C47 (= C48), S50 (≠ T51), Y184 (≠ A184), E188 (= E188), H444 (≠ L443), H446 (= H445), E451 (= E450)
- binding flavin-adenine dinucleotide: I9 (≠ V11), P13 (= P15), G14 (= G16), E33 (= E35), K34 (= K36), R35 (vs. gap), G40 (= G41), T41 (≠ I42), C42 (= C43), G46 (= G47), C47 (= C48), K51 (= K52), Y114 (≠ H114), G115 (= G115), T144 (= T144), G145 (= G145), Y184 (≠ A184), I185 (= I185), R274 (≠ I273), D314 (= D312), M320 (≠ W318), L321 (= L319), A322 (= A320), H323 (= H321)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
37% identity, 99% coverage: 4:466/466 of query aligns to 5:470/470 of 6uziC
- active site: C45 (= C43), C50 (= C48), S53 (≠ T51), V187 (≠ A184), E191 (= E188), H448 (= H445), E453 (= E450)
- binding flavin-adenine dinucleotide: I12 (≠ V11), G13 (= G12), G15 (= G14), P16 (= P15), G17 (= G16), E36 (= E35), K37 (= K36), G43 (= G41), T44 (≠ I42), C45 (= C43), G49 (= G47), C50 (= C48), S53 (≠ T51), K54 (= K52), V117 (≠ H114), G118 (= G115), T147 (= T144), G148 (= G145), I188 (= I185), R276 (≠ I273), D316 (= D312), M322 (≠ W318), L323 (= L319), A324 (= A320)
- binding zinc ion: H448 (= H445), E453 (= E450)
6bz0A 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from acinetobacter baumannii in complex with fad.
40% identity, 99% coverage: 5:465/466 of query aligns to 1:467/469 of 6bz0A
- active site: C45 (= C43), C50 (= C48), S53 (≠ T51), V187 (≠ A184), E191 (= E188), H447 (= H445), E452 (= E450)
- binding flavin-adenine dinucleotide: I7 (≠ V11), G10 (= G14), P11 (= P15), G12 (= G16), E31 (= E35), K32 (= K36), R33 (vs. gap), G43 (= G41), T44 (≠ I42), C45 (= C43), G49 (= G47), C50 (= C48), K54 (= K52), T117 (≠ H114), G118 (= G115), S147 (≠ T144), G148 (= G145), S167 (≠ Y164), I188 (= I185), R275 (≠ I273), Y278 (≠ N276), D315 (= D312), M321 (≠ W318), L322 (= L319), A323 (= A320), A326 (= A323), Y354 (= Y352)
2eq6A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8
43% identity, 99% coverage: 4:466/466 of query aligns to 2:458/460 of 2eq6A
- active site: V37 (≠ L39), C41 (= C43), C46 (= C48), T49 (= T51), A176 (= A184), E180 (= E188), H435 (≠ L443), H437 (= H445), E442 (= E450)
- binding flavin-adenine dinucleotide: I9 (≠ V11), G10 (= G12), G12 (= G14), P13 (= P15), G14 (= G16), E33 (= E35), A34 (≠ K36), G39 (= G41), V40 (≠ I42), C41 (= C43), G45 (= G47), C46 (= C48), K50 (= K52), F111 (≠ H114), A112 (≠ G115), A135 (= A143), T136 (= T144), G137 (= G145), S155 (≠ Y164), R269 (≠ N276), D306 (= D312), L312 (≠ W318), L313 (= L319), A314 (= A320), H315 (= H321), Y344 (= Y352)
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)
38% identity, 99% coverage: 7:466/466 of query aligns to 43:509/509 of P09622
- 71:80 (vs. 35:43, 60% identical) binding
- K72 (= K36) to E: in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX; dbSNP:rs121964987
- K89 (= K52) binding ; mutation to E: Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- K104 (= K65) to T: in dbSNP:rs1130477
- G154 (= G115) binding
- TGS 183:185 (≠ TGA 144:146) binding
- 220:227 (vs. 181:188, 75% identical) binding
- E243 (= E204) binding
- V278 (≠ I238) binding
- G314 (= G272) binding
- D355 (= D312) binding
- MLAH 361:364 (≠ WLAH 318:321) binding
- E375 (= E332) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (= H340) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (≠ G406) 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 (≠ G424) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ L431) 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 (= D437) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (≠ A440) 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 (≠ L443) 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 (= S449) 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 (≠ H453) to G: in DLDD; loss of enzyme activity; reduced interaction with PDHX; dbSNP:rs121964989
- K505 (≠ R462) mutation to M: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
7kmyA Structure of mtb lpd bound to 010705 (see paper)
41% identity, 99% coverage: 4:466/466 of query aligns to 3:465/465 of 7kmyA
- active site: W38 (≠ L39), C42 (= C43), C47 (= C48), S50 (≠ T51), A182 (= A184), E186 (= E188), H442 (≠ L443), H444 (= H445), E449 (= E450)
- binding flavin-adenine dinucleotide: L10 (≠ V11), G11 (= G12), G13 (= G14), P14 (= P15), V33 (= V34), E34 (= E35), P35 (≠ K36), Y37 (≠ H38), G40 (= G41), V41 (≠ I42), C42 (= C43), G46 (= G47), C47 (= C48), K51 (= K52), Y113 (≠ H114), G114 (= G115), A142 (= A143), T143 (= T144), G144 (= G145), Y162 (= Y164), I183 (= I185), Y277 (≠ L280), G309 (= G311), D310 (= D312), Q316 (≠ W318), L317 (= L319), A318 (= A320)
- binding N~2~-methyl-N~2~-[(5-methyl-1H-indazol-7-yl)sulfonyl]-N-(1-methyl-2-oxo-1,2-dihydropyridin-4-yl)glycinamide: Y17 (= Y18), R94 (≠ L95), G97 (= G98), F100 (≠ H101), E322 (≠ S324), A382 (≠ G383), H444 (= H445), E449 (= E450), N464 (≠ H465)
4m52A Structure of mtb lpd bound to sl827 (see paper)
41% identity, 99% coverage: 4:466/466 of query aligns to 3:465/465 of 4m52A
- active site: W38 (≠ L39), C42 (= C43), C47 (= C48), S50 (≠ T51), A182 (= A184), E186 (= E188), H442 (≠ L443), H444 (= H445), E449 (= E450)
- binding flavin-adenine dinucleotide: L10 (≠ V11), G11 (= G12), G13 (= G14), P14 (= P15), V33 (= V34), E34 (= E35), P35 (≠ K36), Y37 (≠ H38), V41 (≠ I42), C42 (= C43), G46 (= G47), C47 (= C48), K51 (= K52), Y113 (≠ H114), G114 (= G115), A142 (= A143), T143 (= T144), Y162 (= Y164), I183 (= I185), F270 (≠ I273), Y277 (≠ L280), G309 (= G311), D310 (= D312), Q316 (≠ W318), L317 (= L319), A318 (= A320)
- binding N~2~-[(2-amino-5-bromopyridin-3-yl)sulfonyl]-N-(4-methoxyphenyl)-N~2~-methylglycinamide: P14 (= P15), Y17 (= Y18), R94 (≠ L95), F100 (≠ H101), E322 (≠ S324), A382 (≠ G383), H444 (= H445), N464 (≠ H465)
3ii4A Structure of mycobacterial lipoamide dehydrogenase bound to a triazaspirodimethoxybenzoyl inhibitor (see paper)
41% identity, 99% coverage: 4:466/466 of query aligns to 1:463/463 of 3ii4A
- active site: W36 (≠ L39), C40 (= C43), C45 (= C48), S48 (≠ T51), A180 (= A184), E184 (= E188), H440 (≠ L443), H442 (= H445), E447 (= E450)
- binding N-[2-(2,4-dichlorophenyl)ethyl]-2-{8-[(2,4-dimethoxyphenyl)carbonyl]-4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]dec-3-yl}acetamide: R146 (= R149), A180 (= A184), I181 (= I185), E184 (= E188), N208 (≠ V212), E209 (= E213), F268 (≠ I273), R287 (≠ K291), G311 (= G315), Q314 (≠ W318), L315 (= L319), R346 (≠ A349), A347 (≠ C350)
- binding flavin-adenine dinucleotide: L8 (≠ V11), G9 (= G12), G11 (= G14), P12 (= P15), G13 (= G16), V31 (= V34), E32 (= E35), P33 (≠ K36), Y35 (≠ H38), G38 (= G41), V39 (≠ I42), C40 (= C43), G44 (= G47), C45 (= C48), K49 (= K52), Y111 (≠ H114), G112 (= G115), A140 (= A143), T141 (= T144), G142 (= G145), Y160 (= Y164), I181 (= I185), Y275 (≠ L280), G307 (= G311), D308 (= D312), Q314 (≠ W318), L315 (= L319), A316 (= A320)
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
39% identity, 99% coverage: 6:465/466 of query aligns to 1:465/465 of 3urhB
- active site: Y35 (≠ L39), C39 (= C43), C44 (= C48), S47 (≠ T51), V183 (≠ A184), E187 (= E188), H443 (≠ L443), H445 (= H445), E450 (= E450)
- binding flavin-adenine dinucleotide: I6 (≠ V11), G7 (= G12), G9 (= G14), P10 (= P15), G11 (= G16), E30 (= E35), K31 (= K36), G37 (= G41), T38 (≠ I42), C39 (= C43), G43 (= G47), C44 (= C48), K48 (= K52), T111 (≠ H114), G112 (= G115), A140 (= A143), T141 (= T144), G142 (= G145), I184 (= I185), R273 (≠ I273), G312 (= G311), D313 (= D312), M319 (≠ W318), L320 (= L319), A321 (= A320), H322 (= H321)
6hg8B Crystal structure of the r460g disease-causing mutant of the human dihydrolipoamide dehydrogenase.
38% identity, 99% coverage: 7:466/466 of query aligns to 16:482/482 of 6hg8B
- active site: C53 (= C43), C58 (= C48), S61 (≠ T51), V196 (≠ A184), E200 (= E188), H460 (= H445), E465 (= E450)
- binding flavin-adenine dinucleotide: I20 (≠ V11), G23 (= G14), P24 (= P15), G25 (= G16), E44 (= E35), K45 (= K36), N46 (≠ A37), G51 (= G41), T52 (≠ I42), C53 (= C43), G57 (= G47), C58 (= C48), K62 (= K52), Y126 (≠ H114), G127 (= G115), T156 (= T144), G157 (= G145), I197 (= I185), R288 (≠ I273), F291 (≠ N276), G327 (= G311), D328 (= D312), M334 (≠ W318), L335 (= L319), A336 (= A320), H337 (= H321)
8u0qA Co-crystal structure of optimized analog tdi-13537 provided new insights into the potency determinants of the sulfonamide inhibitor series (see paper)
41% identity, 99% coverage: 4:466/466 of query aligns to 2:464/464 of 8u0qA
- binding flavin-adenine dinucleotide: L9 (≠ V11), G10 (= G12), G12 (= G14), P13 (= P15), G14 (= G16), V32 (= V34), E33 (= E35), P34 (≠ K36), Y36 (≠ H38), G39 (= G41), V40 (≠ I42), C41 (= C43), G45 (= G47), C46 (= C48), K50 (= K52), Y112 (≠ H114), G113 (= G115), A141 (= A143), T142 (= T144), G143 (= G145), Y161 (= Y164), I182 (= I185), Y276 (≠ L280), G308 (= G311), D309 (= D312), Q315 (≠ W318), L316 (= L319), A317 (= A320), H318 (= H321)
- binding N-(3-acetamidophenyl)-N~2~-[3-(difluoromethyl)-5-methylbenzene-1-sulfonyl]-N~2~-methylglycinamide: Y16 (= Y18), R93 (≠ L95), G96 (= G98), F99 (≠ H101), E321 (≠ S324), A381 (≠ G383), A383 (≠ G385), H443 (= H445), E448 (= E450), N463 (≠ H465), F464 (≠ I466)
8ct4A Cryo-em structure of mtb lpd bound to inhibitor complex with 2-((2- cyano-n,5-dimethyl-1h-indole)-7-sulfonamido)-n-(4-(oxetan-3-yl)-3,4- dihydro-2h-benzo[b] [1,4]oxazin-7-yl)acetamide
41% identity, 99% coverage: 4:466/466 of query aligns to 2:464/464 of 8ct4A
- binding flavin-adenine dinucleotide: L9 (≠ V11), G10 (= G12), G12 (= G14), P13 (= P15), E33 (= E35), P34 (≠ K36), Y36 (≠ H38), G39 (= G41), V40 (≠ I42), C41 (= C43), G45 (= G47), C46 (= C48), K50 (= K52), Y112 (≠ H114), G113 (= G115), T142 (= T144), G143 (= G145), Y161 (= Y164), I182 (= I185), Y276 (≠ L280), D309 (= D312), Q315 (≠ W318), L316 (= L319), A317 (= A320)
- binding N~2~-(2-cyano-5-methyl-1H-indole-7-sulfonyl)-N~2~-methyl-N-[4-(oxetan-3-yl)-3,4-dihydro-2H-1,4-benzoxazin-7-yl]glycinamide: Y16 (= Y18), R93 (≠ L95), F99 (≠ H101), E321 (≠ S324), F377 (= F379), A381 (≠ G383), A383 (≠ G385), H443 (= H445), E448 (= E450), A449 (= A451), E452 (= E454), N463 (≠ H465)
Query Sequence
>RR42_RS21770 FitnessBrowser__Cup4G11:RR42_RS21770
MANSSFDLIVVGGGPGGYVAAIRATQLGMKTALVEKAHLGGICLNWGCIPTKALLRSADV
LRLVKDAAAYGVHAAPPTADLPAMVARSRAVAAQLNKGVAHLMKKNGVTVLNGHGRLAGK
GKLEVTATDGKTRIVSSAHILLATGARARQLPALPADGKTVWTYRDALAPPVVPKRMLIV
GAGAIGIEFASFYRAVGAEVTVVEMAQRILPVEDADICAQVASSLTREGIVLHTGTGIQS
AERKGQGWSIELQGGKSGGARVDVDVVLVAAGIVGNVEDLGLERTAVKVEKTHIVTDGFG
RTDEPGVYAIGDVAGPPWLAHKASHEGVICVERIAGLHPHALDATRIPACTYSHPQVASV
GLTEAQARERGHPVKVGKFPFAGNGKAIAMGSTAGLVKVVFDAGSGELLGAHMVGDEVTE
MIQGYAIAQTLETTEADLMAAVLPHPTMSEAMHEAVLAAYGRALHI
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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