SitesBLAST
Comparing Echvi_0770 Echvi_0770 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)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
70% identity, 94% coverage: 31:494/494 of query aligns to 7:470/470 of 6uziC
- active site: C45 (= C69), C50 (= C74), S53 (= S77), V187 (= V211), E191 (= E215), H448 (= H472), E453 (= E477)
- binding flavin-adenine dinucleotide: I12 (= I36), G13 (= G37), G15 (= G39), P16 (= P40), G17 (= G41), E36 (= E60), K37 (= K61), G43 (= G67), T44 (= T68), C45 (= C69), G49 (= G73), C50 (= C74), S53 (= S77), K54 (= K78), V117 (= V141), G118 (= G142), T147 (= T171), G148 (= G172), I188 (= I212), R276 (= R300), D316 (= D340), M322 (= M346), L323 (= L347), A324 (= A348)
- binding zinc ion: H448 (= H472), E453 (= E477)
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
55% identity, 92% coverage: 31:485/494 of query aligns to 1:458/465 of 3urhB
- active site: Y35 (≠ L65), C39 (= C69), C44 (= C74), S47 (= S77), V183 (= V211), E187 (= E215), H443 (= H470), H445 (= H472), E450 (= E477)
- binding flavin-adenine dinucleotide: I6 (= I36), G7 (= G37), G9 (= G39), P10 (= P40), G11 (= G41), E30 (= E60), K31 (= K61), G37 (= G67), T38 (= T68), C39 (= C69), G43 (= G73), C44 (= C74), K48 (= K78), T111 (≠ V141), G112 (= G142), A140 (= A170), T141 (= T171), G142 (= G172), I184 (= I212), R273 (= R300), G312 (= G339), D313 (= D340), M319 (= M346), L320 (= L347), A321 (= A348), H322 (= H349)
6aonA 1.72 angstrom resolution crystal structure of 2-oxoglutarate dehydrogenase complex subunit dihydrolipoamide dehydrogenase from bordetella pertussis in complex with fad
51% identity, 94% coverage: 31:493/494 of query aligns to 3:472/473 of 6aonA
- active site: P43 (≠ L65), C47 (= C69), C52 (= C74), S55 (= S77), V191 (= V211), E195 (= E215), H450 (= H470), H452 (= H472), E457 (= E477)
- binding calcium ion: A218 (≠ P238), A220 (≠ M240), Q222 (≠ K242)
- binding flavin-adenine dinucleotide: I8 (= I36), G11 (= G39), P12 (= P40), G13 (= G41), D32 (≠ E60), A33 (≠ K61), W34 (≠ Y62), G45 (= G67), T46 (= T68), C47 (= C69), G51 (= G73), C52 (= C74), K56 (= K78), K119 (≠ V141), G120 (= G142), T151 (= T171), G152 (= G172), N171 (≠ S191), I192 (= I212), R280 (= R300), Y283 (= Y303), G319 (= G339), D320 (= D340), M326 (= M346), L327 (= L347), A328 (= A348), H329 (= H349)
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
52% identity, 94% coverage: 31:494/494 of query aligns to 2:455/455 of 2yquB
- active site: P11 (= P40), L36 (= L65), C40 (= C69), C45 (= C74), S48 (= S77), G72 (≠ D103), V73 (≠ L104), V177 (= V211), E181 (= E215), S314 (≠ E352), H432 (= H470), H434 (= H472), E439 (= E477)
- binding carbonate ion: A310 (= A348), S314 (≠ E352), S423 (= S461), D426 (= D464)
- binding flavin-adenine dinucleotide: G8 (= G37), G10 (= G39), P11 (= P40), G12 (= G41), E31 (= E60), K32 (= K61), G38 (= G67), T39 (= T68), C40 (= C69), R42 (≠ N71), G44 (= G73), C45 (= C74), K49 (= K78), T110 (≠ V141), A111 (≠ G142), T137 (= T171), G138 (= G172), I178 (= I212), Y265 (= Y303), G301 (= G339), D302 (= D340), M308 (= M346), L309 (= L347), A310 (= A348), H311 (= H349)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
52% identity, 94% coverage: 31:494/494 of query aligns to 2:455/455 of 2yquA
- active site: P11 (= P40), L36 (= L65), C40 (= C69), C45 (= C74), S48 (= S77), G72 (≠ D103), V73 (≠ L104), V177 (= V211), E181 (= E215), S314 (≠ E352), H432 (= H470), H434 (= H472), E439 (= E477)
- binding flavin-adenine dinucleotide: G8 (= G37), G10 (= G39), P11 (= P40), G12 (= G41), E31 (= E60), K32 (= K61), G38 (= G67), T39 (= T68), C40 (= C69), R42 (≠ N71), G44 (= G73), C45 (= C74), K49 (= K78), T110 (≠ V141), A111 (≠ G142), T137 (= T171), G138 (= G172), S157 (= S191), I178 (= I212), Y265 (= Y303), G301 (= G339), D302 (= D340), M308 (= M346), L309 (= L347), A310 (= A348)
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)
50% identity, 94% coverage: 32:494/494 of query aligns to 39:501/501 of P31023
- 67:76 (vs. 60:69, 70% identical) binding
- C76 (= C69) modified: Disulfide link with 81, Redox-active
- C81 (= C74) modified: Disulfide link with 76, Redox-active
- G149 (= G142) binding
- D348 (= D340) binding
- MLAH 354:357 (= MLAH 346:349) binding
Sites not aligning to the query:
- 1:31 modified: transit peptide, Mitochondrion
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
52% identity, 93% coverage: 31:489/494 of query aligns to 2:451/452 of 2eq7A
- active site: P11 (= P40), L36 (= L65), C40 (= C69), C45 (= C74), S48 (= S77), G72 (≠ D103), V73 (≠ L104), V177 (= V211), E181 (= E215), S314 (≠ E352), H432 (= H470), H434 (= H472), E439 (= E477)
- binding flavin-adenine dinucleotide: G10 (= G39), P11 (= P40), G12 (= G41), E31 (= E60), K32 (= K61), G38 (= G67), T39 (= T68), C40 (= C69), R42 (≠ N71), G44 (= G73), C45 (= C74), K49 (= K78), T110 (≠ V141), A111 (≠ G142), T137 (= T171), G138 (= G172), S157 (= S191), I178 (= I212), R262 (= R300), Y265 (= Y303), D302 (= D340), M308 (= M346), L309 (= L347), A310 (= A348), H311 (= H349), Y341 (= Y379)
- binding nicotinamide-adenine-dinucleotide: W146 (≠ F180), G174 (= G208), G176 (= G210), V177 (= V211), I178 (= I212), E197 (= E231), Y198 (≠ F232), V231 (= V265), V260 (≠ I298), G261 (= G299), R262 (= R300), M308 (= M346), L309 (= L347), V339 (= V377)
1dxlA Dihydrolipoamide dehydrogenase of glycine decarboxylase from pisum sativum (see paper)
50% identity, 94% coverage: 32:494/494 of query aligns to 5:467/467 of 1dxlA
- active site: L38 (= L65), C42 (= C69), C47 (= C74), S50 (= S77), Y184 (≠ V211), E188 (= E215), H444 (= H470), H446 (= H472), E451 (= E477)
- binding flavin-adenine dinucleotide: I9 (= I36), P13 (= P40), G14 (= G41), E33 (= E60), K34 (= K61), R35 (≠ Y62), G40 (= G67), T41 (= T68), C42 (= C69), G46 (= G73), C47 (= C74), K51 (= K78), Y114 (≠ V141), G115 (= G142), T144 (= T171), G145 (= G172), Y184 (≠ V211), I185 (= I212), R274 (= R300), D314 (= D340), M320 (= M346), L321 (= L347), A322 (= A348), H323 (= H349)
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
51% identity, 94% coverage: 32:493/494 of query aligns to 6:471/472 of 1zmdA
- active site: L39 (= L65), C43 (= C69), C48 (= C74), S51 (= S77), V186 (= V211), E190 (= E215), H448 (= H470), H450 (= H472), E455 (= E477)
- binding flavin-adenine dinucleotide: I10 (= I36), G11 (= G37), G13 (= G39), P14 (= P40), G15 (= G41), E34 (= E60), K35 (= K61), N36 (≠ Y62), G41 (= G67), T42 (= T68), C43 (= C69), G47 (= G73), C48 (= C74), K52 (= K78), Y116 (≠ V141), G117 (= G142), T146 (= T171), G147 (= G172), S166 (= S191), R278 (= R300), F281 (≠ Y303), G317 (= G339), D318 (= D340), M324 (= M346), L325 (= L347), A326 (= A348), H327 (= H349)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (= I207), G183 (= G208), G185 (= G210), V186 (= V211), I187 (= I212), E190 (= E215), E206 (= E231), F207 (= F232), L208 (≠ M233), I276 (= I298), G277 (= G299), R278 (= R300), M324 (= M346), L325 (= L347), V355 (= V377), Y357 (= Y379)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
51% identity, 94% coverage: 32:493/494 of query aligns to 6:471/472 of 1zmcA
- active site: L39 (= L65), C43 (= C69), C48 (= C74), S51 (= S77), V186 (= V211), E190 (= E215), H448 (= H470), H450 (= H472), E455 (= E477)
- binding flavin-adenine dinucleotide: I10 (= I36), G11 (= G37), G13 (= G39), P14 (= P40), G15 (= G41), E34 (= E60), K35 (= K61), N36 (≠ Y62), G41 (= G67), T42 (= T68), C43 (= C69), G47 (= G73), C48 (= C74), K52 (= K78), Y116 (≠ V141), G117 (= G142), T146 (= T171), G147 (= G172), S166 (= S191), I187 (= I212), F281 (≠ Y303), G317 (= G339), D318 (= D340), M324 (= M346), L325 (= L347), A326 (= A348), H327 (= H349)
- binding nicotinamide-adenine-dinucleotide: G183 (= G208), G185 (= G210), V205 (= V230), E206 (= E231), F207 (= F232), L208 (≠ M233), K240 (= K264), V241 (= V265), I276 (= I298), G277 (= G299), R278 (= R300), R297 (= R319), M324 (= M346)
P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 from Pseudomonas fluorescens (see 2 papers)
49% identity, 94% coverage: 31:494/494 of query aligns to 5:472/478 of P14218
- 34:49 (vs. 60:69, 50% identical) binding
- C49 (= C69) modified: Disulfide link with 54, Redox-active
- C54 (= C74) modified: Disulfide link with 49, Redox-active
- K58 (= K78) binding
- G122 (= G142) binding
- D319 (= D340) binding
- A327 (= A348) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
49% identity, 94% coverage: 31:494/494 of query aligns to 7:474/477 of 5u8uD
- active site: P16 (= P40), L47 (= L65), C51 (= C69), C56 (= C74), S59 (= S77), G85 (≠ D103), V86 (≠ L104), V193 (= V211), E197 (= E215), S333 (≠ E352), F451 (≠ H470), H453 (= H472), E458 (= E477)
- binding flavin-adenine dinucleotide: I12 (= I36), G15 (= G39), P16 (= P40), G17 (= G41), E36 (= E60), K37 (= K61), G49 (= G67), T50 (= T68), C51 (= C69), G55 (= G73), C56 (= C74), K60 (= K78), H123 (≠ V141), G124 (= G142), A152 (= A170), S153 (≠ T171), G154 (= G172), I194 (= I212), R281 (= R300), G320 (= G339), D321 (= D340), M327 (= M346), L328 (= L347), A329 (= A348), H330 (= H349), H453 (= H472), P454 (= P473)
Sites not aligning to the query:
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
49% identity, 94% coverage: 31:494/494 of query aligns to 4:471/473 of 5u8wA
- active site: P13 (= P40), L44 (= L65), C48 (= C69), C53 (= C74), S56 (= S77), G82 (≠ D103), V83 (≠ L104), V190 (= V211), E194 (= E215), S330 (≠ E352), F448 (≠ H470), H450 (= H472), E455 (= E477)
- binding flavin-adenine dinucleotide: I9 (= I36), G12 (= G39), P13 (= P40), G14 (= G41), E33 (= E60), K34 (= K61), G46 (= G67), T47 (= T68), C48 (= C69), G52 (= G73), C53 (= C74), K57 (= K78), H120 (≠ V141), G121 (= G142), A149 (= A170), S150 (≠ T171), G151 (= G172), S170 (= S191), G317 (= G339), D318 (= D340), M324 (= M346), L325 (= L347), A326 (= A348), H327 (= H349), Y357 (= Y379), H450 (= H472), P451 (= P473)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (= I207), G189 (= G210), V190 (= V211), I191 (= I212), E194 (= E215), E210 (= E231), A211 (≠ F232), L212 (≠ M233), A275 (≠ S297), V276 (≠ I298), G277 (= G299), R278 (= R300), M324 (= M346), L325 (= L347), V355 (= V377), Y357 (= Y379)
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)
50% identity, 94% coverage: 32:493/494 of query aligns to 43:508/509 of P09622
- 71:80 (vs. 60:69, 80% identical) binding
- K72 (= K61) to E: in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX; dbSNP:rs121964987
- K89 (= K78) binding ; mutation to E: Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- K104 (≠ H92) to T: in dbSNP:rs1130477
- G154 (= G142) binding
- TGS 183:185 (= TGS 171:173) binding
- 220:227 (vs. 208:215, 75% identical) binding
- E243 (= E231) binding
- V278 (= V265) binding
- G314 (= G299) binding
- D355 (= D340) binding
- MLAH 361:364 (= MLAH 346:349) binding
- E375 (= E360) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (= H368) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (= D433) 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 (= E451) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (= Y458) 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 (= D464) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (= R467) 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 (= H470) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
- P488 (= P473) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
- S491 (≠ T476) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
- E492 (= E477) mutation to Q: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- R495 (≠ K480) to G: in DLDD; loss of enzyme activity; reduced interaction with PDHX; dbSNP:rs121964989
- K505 (≠ R490) mutation to M: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
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)
49% identity, 94% coverage: 31:494/494 of query aligns to 4:471/472 of 3ladA
- active site: L44 (= L65), C48 (= C69), C53 (= C74), S56 (= S77), V190 (= V211), E194 (= E215), F448 (≠ H470), H450 (= H472), E455 (= E477)
- binding flavin-adenine dinucleotide: I9 (= I36), G10 (= G37), G12 (= G39), P13 (= P40), E33 (= E60), K34 (= K61), G46 (= G67), T47 (= T68), C48 (= C69), G52 (= G73), C53 (= C74), H120 (≠ V141), G121 (= G142), A149 (= A170), S150 (≠ T171), G151 (= G172), I191 (= I212), R278 (= R300), D318 (= D340), L325 (= L347), A326 (= A348)
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
49% identity, 94% coverage: 31:494/494 of query aligns to 3:470/472 of 5u8vA
- active site: P12 (= P40), L43 (= L65), C47 (= C69), C52 (= C74), S55 (= S77), G81 (≠ D103), V82 (≠ L104), V189 (= V211), E193 (= E215), S329 (≠ E352), F447 (≠ H470), H449 (= H472), E454 (= E477)
- binding flavin-adenine dinucleotide: I8 (= I36), G11 (= G39), P12 (= P40), G13 (= G41), E32 (= E60), G45 (= G67), T46 (= T68), C47 (= C69), G51 (= G73), C52 (= C74), K56 (= K78), H119 (≠ V141), G120 (= G142), A148 (= A170), S149 (≠ T171), G150 (= G172), S169 (= S191), I190 (= I212), R277 (= R300), G316 (= G339), D317 (= D340), M323 (= M346), L324 (= L347), A325 (= A348), H326 (= H349), H449 (= H472), P450 (= P473)
- binding nicotinamide-adenine-dinucleotide: I185 (= I207), G186 (= G208), G188 (= G210), V189 (= V211), I190 (= I212), L208 (≠ V230), E209 (= E231), A210 (≠ F232), V243 (= V265), V275 (≠ I298), G276 (= G299)
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)
49% identity, 94% coverage: 31:494/494 of query aligns to 5:472/477 of P18925
- 34:49 (vs. 60:69, 50% identical) binding
- C49 (= C69) modified: Disulfide link with 54, Redox-active
- C54 (= C74) modified: Disulfide link with 49, Redox-active
- K58 (= K78) binding
- D319 (= D340) binding
- A327 (= A348) binding
6hg8B Crystal structure of the r460g disease-causing mutant of the human dihydrolipoamide dehydrogenase.
50% identity, 94% coverage: 32:493/494 of query aligns to 16:481/482 of 6hg8B
- active site: C53 (= C69), C58 (= C74), S61 (= S77), V196 (= V211), E200 (= E215), H460 (= H472), E465 (= E477)
- binding flavin-adenine dinucleotide: I20 (= I36), G23 (= G39), P24 (= P40), G25 (= G41), E44 (= E60), K45 (= K61), N46 (≠ Y62), G51 (= G67), T52 (= T68), C53 (= C69), G57 (= G73), C58 (= C74), K62 (= K78), Y126 (≠ V141), G127 (= G142), T156 (= T171), G157 (= G172), I197 (= I212), R288 (= R300), F291 (≠ Y303), G327 (= G339), D328 (= D340), M334 (= M346), L335 (= L347), A336 (= A348), H337 (= H349)
6awaA 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from pseudomonas putida in complex with fad and adenosine-5'-monophosphate.
48% identity, 94% coverage: 31:494/494 of query aligns to 5:472/475 of 6awaA
- active site: L45 (= L65), C49 (= C69), C54 (= C74), S57 (= S77), V191 (= V211), E195 (= E215), F449 (≠ H470), H451 (= H472), E456 (= E477)
- binding adenosine monophosphate: I187 (= I207), E211 (= E231), A212 (≠ F232), L213 (≠ M233), V245 (= V265), V277 (≠ I298)
- binding flavin-adenine dinucleotide: I10 (= I36), G13 (= G39), P14 (= P40), G15 (= G41), E34 (= E60), K35 (= K61), T48 (= T68), C49 (= C69), G53 (= G73), C54 (= C74), K58 (= K78), H121 (≠ V141), G122 (= G142), S151 (≠ T171), G152 (= G172), I192 (= I212), R279 (= R300), G318 (= G339), D319 (= D340), M325 (= M346), L326 (= L347), A327 (= A348), Y358 (= Y379)
Sites not aligning to the query:
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, 94% coverage: 28:493/494 of query aligns to 24:498/499 of P09624
- 56:65 (vs. 60:69, 70% identical) binding
- C65 (= C69) modified: Disulfide link with 70, Redox-active
- C70 (= C74) modified: Disulfide link with 65, Redox-active
- K74 (= K78) binding
- G139 (= G142) binding
- D346 (= D340) binding
- MLAH 352:355 (= MLAH 346:349) binding
- H478 (= H472) active site, Proton acceptor
Sites not aligning to the query:
- 1:21 modified: transit peptide, Mitochondrion
Query Sequence
>Echvi_0770 Echvi_0770 dihydrolipoamide dehydrogenase
MDLSGALKNNTFFVLGTLYLVLCSKPTNMTYDLIVIGSGPGGYVAAIRGAQLGMKTAIVE
KYPTLGGTCLNVGCIPSKALLDSSEHYHNAAHTFKTHGIDLKDLKVNLKQMISRKDDVVK
QNVDGISYLMKKNKIDVHQGVGSFVDKNTVKVTKDDGKSTEITGENIIIATGSKPASLPF
IEIDKKRVITSTEALKMKEVPKRMIVIGGGVIGMELGSVYARMGAKVSVVEFMDSLIPSM
DKTMGKELQKSLKKLGFEFYLKHKVTAVKSTAKEVTVTAENSKGEEVQVKGDYVLVSIGR
KPYTEGLNPEAAGVKVNDRGQVEVDEHLKTSADNIYAIGDVVKGAMLAHKAEEEGVLVAE
QLAGQKPHINYNLIPGVVYTWPEVAAVGYSEEQLKEKGIKYKTGKFPFMASGRARASMDT
DGLVKVLADAETDEILGVHMIGPRTADMIAEAVVAMEYRASAEDIARMSHAHPTYTEAFK
EACLAATENRALHV
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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