SitesBLAST
Comparing H281DRAFT_05115 H281DRAFT_05115 dihydrolipoamide dehydrogenase 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
64% identity, 100% coverage: 3:476/476 of query aligns to 1:473/473 of 6aonA
- active site: P43 (≠ L45), C47 (= C49), C52 (= C54), S55 (= S57), V191 (= V194), E195 (= E198), H450 (= H453), H452 (= H455), E457 (= E460)
- binding calcium ion: A218 (≠ G221), A220 (= A223), Q222 (= Q225)
- binding flavin-adenine dinucleotide: I8 (= I10), G11 (= G13), P12 (= P14), G13 (= G15), D32 (≠ E34), A33 (≠ K35), W34 (= W36), G45 (= G47), T46 (= T48), C47 (= C49), G51 (= G53), C52 (= C54), K56 (= K58), K119 (≠ H121), G120 (= G122), T151 (= T154), G152 (= G155), N171 (= N174), I192 (= I195), R280 (= R283), Y283 (≠ N286), G319 (= G322), D320 (= D323), M326 (= M329), L327 (= L330), A328 (= A331), H329 (= H332)
6awaA 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from pseudomonas putida in complex with fad and adenosine-5'-monophosphate.
56% identity, 100% coverage: 1:476/476 of query aligns to 1:472/475 of 6awaA
- active site: L45 (= L45), C49 (= C49), C54 (= C54), S57 (= S57), V191 (= V194), E195 (= E198), F449 (≠ H453), H451 (= H455), E456 (= E460)
- binding adenosine monophosphate: I187 (= I190), E211 (= E214), A212 (= A215), L213 (= L216), V245 (= V248), V277 (≠ I281)
- binding flavin-adenine dinucleotide: I10 (= I10), G13 (= G13), P14 (= P14), G15 (= G15), E34 (= E34), K35 (= K35), T48 (= T48), C49 (= C49), G53 (= G53), C54 (= C54), K58 (= K58), H121 (= H121), G122 (= G122), S151 (≠ T154), G152 (= G155), I192 (= I195), R279 (= R283), G318 (= G322), D319 (= D323), M325 (= M329), L326 (= L330), A327 (= A331), Y358 (= Y362)
Sites not aligning to the query:
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
56% identity, 100% coverage: 1:476/476 of query aligns to 3:474/477 of 5u8uD
- active site: P16 (= P14), L47 (= L45), C51 (= C49), C56 (= C54), S59 (= S57), G85 (≠ N83), V86 (= V84), V193 (= V194), E197 (= E198), S333 (≠ E335), F451 (≠ H453), H453 (= H455), E458 (= E460)
- binding flavin-adenine dinucleotide: I12 (= I10), G15 (= G13), P16 (= P14), G17 (= G15), E36 (= E34), K37 (= K35), G49 (= G47), T50 (= T48), C51 (= C49), G55 (= G53), C56 (= C54), K60 (= K58), H123 (= H121), G124 (= G122), A152 (= A153), S153 (≠ T154), G154 (= G155), I194 (= I195), R281 (= R283), G320 (= G322), D321 (= D323), M327 (= M329), L328 (= L330), A329 (= A331), H330 (= H332), H453 (= H455), P454 (= P456)
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)
56% identity, 100% coverage: 1:476/476 of query aligns to 1:472/478 of P14218
- M1 (= M1) modified: Initiator methionine, Removed
- 34:49 (vs. 34:49, 50% 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 (= D323) binding
- A327 (= A331) binding
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
56% identity, 100% coverage: 2:476/476 of query aligns to 1:471/473 of 5u8wA
- active site: P13 (= P14), L44 (= L45), C48 (= C49), C53 (= C54), S56 (= S57), G82 (≠ N83), V83 (= V84), V190 (= V194), E194 (= E198), S330 (≠ E335), F448 (≠ H453), H450 (= H455), E455 (= E460)
- binding flavin-adenine dinucleotide: I9 (= I10), G12 (= G13), P13 (= P14), G14 (= G15), E33 (= E34), K34 (= K35), G46 (= G47), T47 (= T48), C48 (= C49), G52 (= G53), C53 (= C54), K57 (= K58), H120 (= H121), G121 (= G122), A149 (= A153), S150 (≠ T154), G151 (= G155), S170 (≠ N174), G317 (= G322), D318 (= D323), M324 (= M329), L325 (= L330), A326 (= A331), H327 (= H332), Y357 (= Y362), H450 (= H455), P451 (= P456)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (= I190), G189 (= G193), V190 (= V194), I191 (= I195), E194 (= E198), E210 (= E214), A211 (= A215), L212 (= L216), A275 (≠ S280), V276 (≠ I281), G277 (= G282), R278 (= R283), M324 (= M329), L325 (= L330), V355 (= V360), Y357 (= Y362)
Sites not aligning to the query:
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
56% identity, 100% coverage: 3:476/476 of query aligns to 1:470/472 of 5u8vA
- active site: P12 (= P14), L43 (= L45), C47 (= C49), C52 (= C54), S55 (= S57), G81 (≠ N83), V82 (= V84), V189 (= V194), E193 (= E198), S329 (≠ E335), F447 (≠ H453), H449 (= H455), E454 (= E460)
- binding flavin-adenine dinucleotide: I8 (= I10), G11 (= G13), P12 (= P14), G13 (= G15), E32 (= E34), G45 (= G47), T46 (= T48), C47 (= C49), G51 (= G53), C52 (= C54), K56 (= K58), H119 (= H121), G120 (= G122), A148 (= A153), S149 (≠ T154), G150 (= G155), S169 (≠ N174), I190 (= I195), R277 (= R283), G316 (= G322), D317 (= D323), M323 (= M329), L324 (= L330), A325 (= A331), H326 (= H332), H449 (= H455), P450 (= P456)
- binding nicotinamide-adenine-dinucleotide: I185 (= I190), G186 (= G191), G188 (= G193), V189 (= V194), I190 (= I195), L208 (= L213), E209 (= E214), A210 (= A215), V243 (= V248), V275 (≠ I281), G276 (= G282)
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: 1:476/476 of query aligns to 1:472/477 of P18925
- 34:49 (vs. 34:49, 56% identical) binding
- C49 (= C49) modified: Disulfide link with 54, Redox-active
- C54 (= C54) modified: Disulfide link with 49, Redox-active
- K58 (= K58) binding
- D319 (= D323) binding
- A327 (= A331) 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: 2:476/476 of query aligns to 1:471/472 of 3ladA
- active site: L44 (= L45), C48 (= C49), C53 (= C54), S56 (= S57), V190 (= V194), E194 (= E198), F448 (≠ H453), H450 (= H455), E455 (= E460)
- binding flavin-adenine dinucleotide: I9 (= I10), G10 (= G11), G12 (= G13), P13 (= P14), E33 (= E34), K34 (= K35), G46 (= G47), T47 (= T48), C48 (= C49), G52 (= G53), C53 (= C54), H120 (= H121), G121 (= G122), A149 (= A153), S150 (≠ T154), G151 (= G155), I191 (= I195), R278 (= R283), D318 (= D323), L325 (= L330), A326 (= A331)
6bz0A 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from acinetobacter baumannii in complex with fad.
55% identity, 99% coverage: 4:475/476 of query aligns to 1:467/469 of 6bz0A
- active site: C45 (= C49), C50 (= C54), S53 (= S57), V187 (= V194), E191 (= E198), H447 (= H455), E452 (= E460)
- binding flavin-adenine dinucleotide: I7 (= I10), G10 (= G13), P11 (= P14), G12 (= G15), E31 (= E34), K32 (= K35), R33 (≠ K37), G43 (= G47), T44 (= T48), C45 (= C49), G49 (= G53), C50 (= C54), K54 (= K58), T117 (= T125), G118 (= G126), S147 (≠ T154), G148 (= G155), S167 (≠ N174), I188 (= I195), R275 (= R283), Y278 (≠ N286), D315 (= D323), M321 (= M329), L322 (= L330), A323 (= A331), A326 (= A334), Y354 (= Y362)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
54% identity, 99% coverage: 4:476/476 of query aligns to 6:470/470 of 6uziC
- active site: C45 (= C49), C50 (= C54), S53 (= S57), V187 (= V194), E191 (= E198), H448 (= H455), E453 (= E460)
- binding flavin-adenine dinucleotide: I12 (= I10), G13 (= G11), G15 (= G13), P16 (= P14), G17 (= G15), E36 (= E34), K37 (= K35), G43 (= G47), T44 (= T48), C45 (= C49), G49 (= G53), C50 (= C54), S53 (= S57), K54 (= K58), V117 (≠ H121), G118 (= G122), T147 (= T154), G148 (= G155), I188 (= I195), R276 (= R283), D316 (= D323), M322 (= M329), L323 (= L330), A324 (= A331)
- binding zinc ion: H448 (= H455), E453 (= E460)
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
51% identity, 97% coverage: 5:468/476 of query aligns to 1:458/465 of 3urhB
- active site: Y35 (≠ L45), C39 (= C49), C44 (= C54), S47 (= S57), V183 (= V194), E187 (= E198), H443 (= H453), H445 (= H455), E450 (= E460)
- binding flavin-adenine dinucleotide: I6 (= I10), G7 (= G11), G9 (= G13), P10 (= P14), G11 (= G15), E30 (= E34), K31 (= K35), G37 (= G47), T38 (= T48), C39 (= C49), G43 (= G53), C44 (= C54), K48 (= K58), T111 (≠ H121), G112 (= G122), A140 (= A153), T141 (= T154), G142 (= G155), I184 (= I195), R273 (= R283), G312 (= G322), D313 (= D323), M319 (= M329), L320 (= L330), A321 (= A331), H322 (= H332)
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: 2:476/476 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 (= D323) binding
- MLAH 354:357 (= MLAH 329:332) 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: 2:476/476 of query aligns to 1:467/467 of 1dxlA
- active site: L38 (= L45), C42 (= C49), C47 (= C54), S50 (= S57), Y184 (≠ V194), E188 (= E198), H444 (= H453), H446 (= H455), E451 (= E460)
- binding flavin-adenine dinucleotide: I9 (= I10), P13 (= P14), G14 (= G15), E33 (= E34), K34 (= K35), R35 (≠ W36), G40 (= G47), T41 (= T48), C42 (= C49), G46 (= G53), C47 (= C54), K51 (= K58), Y114 (≠ H121), G115 (= G122), T144 (= T154), G145 (= G155), Y184 (≠ V194), I185 (= I195), R274 (= R283), D314 (= D323), M320 (= M329), L321 (= L330), A322 (= A331), H323 (= H332)
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, 97% coverage: 6:468/476 of query aligns to 43:500/509 of P09622
- 71:80 (vs. 34:49, 44% identical) binding
- K72 (= K35) 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 (≠ H72) to T: in dbSNP:rs1130477
- G154 (= G122) binding
- TGS 183:185 (= TGS 154:156) binding
- 220:227 (vs. 191:198, 88% identical) binding
- E243 (= E214) binding
- V278 (= V248) binding
- G314 (= G282) binding
- D355 (= D323) binding
- MLAH 361:364 (= MLAH 329:332) binding
- E375 (= E343) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (= H351) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (= D416) 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 (= E434) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ F441) 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 (= D447) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (= R450) 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 (= H453) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
- P488 (= P456) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
- S491 (= S459) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
- E492 (= E460) mutation to Q: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- R495 (= R463) 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)
48% identity, 97% coverage: 6:468/476 of query aligns to 6:463/472 of 1zmdA
- active site: L39 (= L45), C43 (= C49), C48 (= C54), S51 (= S57), V186 (= V194), E190 (= E198), H448 (= H453), H450 (= H455), E455 (= E460)
- binding flavin-adenine dinucleotide: I10 (= I10), G11 (= G11), G13 (= G13), P14 (= P14), G15 (= G15), E34 (= E34), K35 (= K35), N36 (≠ W36), G41 (= G47), T42 (= T48), C43 (= C49), G47 (= G53), C48 (= C54), K52 (= K58), Y116 (≠ H121), G117 (= G122), T146 (= T154), G147 (= G155), S166 (≠ N174), R278 (= R283), F281 (≠ N286), G317 (= G322), D318 (= D323), M324 (= M329), L325 (= L330), A326 (= A331), H327 (= H332)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (= I190), G183 (= G191), G185 (= G193), V186 (= V194), I187 (= I195), E190 (= E198), E206 (= E214), F207 (≠ A215), L208 (= L216), I276 (= I281), G277 (= G282), R278 (= R283), M324 (= M329), L325 (= L330), V355 (= V360), Y357 (= Y362)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
48% identity, 97% coverage: 6:468/476 of query aligns to 6:463/472 of 1zmcA
- active site: L39 (= L45), C43 (= C49), C48 (= C54), S51 (= S57), V186 (= V194), E190 (= E198), H448 (= H453), H450 (= H455), E455 (= E460)
- binding flavin-adenine dinucleotide: I10 (= I10), G11 (= G11), G13 (= G13), P14 (= P14), G15 (= G15), E34 (= E34), K35 (= K35), N36 (≠ W36), G41 (= G47), T42 (= T48), C43 (= C49), G47 (= G53), C48 (= C54), K52 (= K58), Y116 (≠ H121), G117 (= G122), T146 (= T154), G147 (= G155), S166 (≠ N174), I187 (= I195), F281 (≠ N286), G317 (= G322), D318 (= D323), M324 (= M329), L325 (= L330), A326 (= A331), H327 (= H332)
- binding nicotinamide-adenine-dinucleotide: G183 (= G191), G185 (= G193), V205 (≠ L213), E206 (= E214), F207 (≠ A215), L208 (= L216), K240 (= K247), V241 (= V248), I276 (= I281), G277 (= G282), R278 (= R283), R297 (= R302), M324 (= M329)
6hg8B Crystal structure of the r460g disease-causing mutant of the human dihydrolipoamide dehydrogenase.
47% identity, 97% coverage: 6:468/476 of query aligns to 16:473/482 of 6hg8B
- active site: C53 (= C49), C58 (= C54), S61 (= S57), V196 (= V194), E200 (= E198), H460 (= H455), E465 (= E460)
- binding flavin-adenine dinucleotide: I20 (= I10), G23 (= G13), P24 (= P14), G25 (= G15), E44 (= E34), K45 (= K35), N46 (≠ W36), G51 (= G47), T52 (= T48), C53 (= C49), G57 (= G53), C58 (= C54), K62 (= K58), Y126 (≠ H121), G127 (= G122), T156 (= T154), G157 (= G155), I197 (= I195), R288 (= R283), F291 (≠ N286), G327 (= G322), D328 (= D323), M334 (= M329), L335 (= L330), A336 (= A331), H337 (= H332)
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
49% identity, 99% coverage: 5:476/476 of query aligns to 2:455/455 of 2yquB
- active site: P11 (= P14), L36 (= L45), C40 (= C49), C45 (= C54), S48 (= S57), G72 (≠ N83), V73 (= V84), V177 (= V194), E181 (= E198), S314 (≠ E335), H432 (= H453), H434 (= H455), E439 (= E460)
- binding carbonate ion: A310 (= A331), S314 (≠ E335), S423 (≠ A444), D426 (= D447)
- binding flavin-adenine dinucleotide: G8 (= G11), G10 (= G13), P11 (= P14), G12 (= G15), E31 (= E34), K32 (= K35), G38 (= G47), T39 (= T48), C40 (= C49), R42 (≠ N51), G44 (= G53), C45 (= C54), K49 (= K58), T110 (≠ H121), A111 (≠ G122), T137 (= T154), G138 (= G155), I178 (= I195), Y265 (≠ N286), G301 (= G322), D302 (= D323), M308 (= M329), L309 (= L330), A310 (= A331), H311 (= H332)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
49% identity, 99% coverage: 5:476/476 of query aligns to 2:455/455 of 2yquA
- active site: P11 (= P14), L36 (= L45), C40 (= C49), C45 (= C54), S48 (= S57), G72 (≠ N83), V73 (= V84), V177 (= V194), E181 (= E198), S314 (≠ E335), H432 (= H453), H434 (= H455), E439 (= E460)
- binding flavin-adenine dinucleotide: G8 (= G11), G10 (= G13), P11 (= P14), G12 (= G15), E31 (= E34), K32 (= K35), G38 (= G47), T39 (= T48), C40 (= C49), R42 (≠ N51), G44 (= G53), C45 (= C54), K49 (= K58), T110 (≠ H121), A111 (≠ G122), T137 (= T154), G138 (= G155), S157 (≠ N174), I178 (= I195), Y265 (≠ N286), G301 (= G322), D302 (= D323), M308 (= M329), L309 (= L330), A310 (= A331)
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
49% identity, 98% coverage: 5:472/476 of query aligns to 2:451/452 of 2eq7A
- active site: P11 (= P14), L36 (= L45), C40 (= C49), C45 (= C54), S48 (= S57), G72 (≠ N83), V73 (= V84), V177 (= V194), E181 (= E198), S314 (≠ E335), H432 (= H453), H434 (= H455), E439 (= E460)
- binding flavin-adenine dinucleotide: G10 (= G13), P11 (= P14), G12 (= G15), E31 (= E34), K32 (= K35), G38 (= G47), T39 (= T48), C40 (= C49), R42 (≠ N51), G44 (= G53), C45 (= C54), K49 (= K58), T110 (≠ H121), A111 (≠ G122), T137 (= T154), G138 (= G155), S157 (≠ N174), I178 (= I195), R262 (= R283), Y265 (≠ N286), D302 (= D323), M308 (= M329), L309 (= L330), A310 (= A331), H311 (= H332), Y341 (= Y362)
- binding nicotinamide-adenine-dinucleotide: W146 (≠ N163), G174 (= G191), G176 (= G193), V177 (= V194), I178 (= I195), E197 (= E214), Y198 (≠ A215), V231 (= V248), V260 (≠ I281), G261 (= G282), R262 (= R283), M308 (= M329), L309 (= L330), V339 (= V360)
Query Sequence
>H281DRAFT_05115 H281DRAFT_05115 dihydrolipoamide dehydrogenase
MSKEFDVVVIGAGPGGYIAAIRAAQLGKTVACIEKWKNPAGTLKLGGTCLNVGCIPSKAL
LASSEEFENASHHLADHGISVENVKVDISKMMARKDGIVEKMTKGIEFLFRKNKITWLKG
HGKFTGKTDAGVQIEVSGEGETEVVTAKNVIIATGSKARHLPNIPVDNKIVADNEGALAF
DTAPKKLAVIGAGVIGLELGSVWRRLGAEVTVLEALPEFLGAADQALAKEAAKQFKKQGL
DIHVGVKVGEVSTTENSVTINYTDKDGNAQKLEADRLIVSIGRVPNTDNLGLEAIGLKAN
ERGFIDVDDHCATAVPNVYAIGDVVRGPMLAHKAEDEGVLVAEIIDGQKPHIDYNCIPWV
IYTEPEIAWVGKTEQQLKAEGREVKTGQFPFMANGRALGINKADGFVKMIADAKTDELLG
VHIISANASDLIAEAVVAMEFKAASEDIGRICHPHPSLSEVMREAALAVDKRALNM
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