SitesBLAST
Comparing GFF1561 FitnessBrowser__Marino:GFF1561 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)
P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 from Pseudomonas fluorescens (see 2 papers)
70% identity, 100% coverage: 1:479/480 of query aligns to 1:478/478 of P14218
- M1 (= M1) modified: Initiator methionine, Removed
- 34:49 (vs. 34:50, 47% identical) binding
- C49 (= C50) modified: Disulfide link with 54, Redox-active
- C54 (= C55) modified: Disulfide link with 49, Redox-active
- K58 (= K59) binding
- G122 (= G123) binding
- D319 (= D320) binding
- A327 (= A328) binding
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
70% identity, 99% coverage: 1:476/480 of query aligns to 3:477/477 of 5u8uD
- active site: P16 (= P14), L47 (= L46), C51 (= C50), C56 (= C55), S59 (= S58), G85 (≠ D84), V86 (= V85), V193 (= V192), E197 (= E196), S333 (= S332), F451 (= F450), H453 (= H452), E458 (= E457), N476 (= N475), R477 (= R476)
- binding flavin-adenine dinucleotide: I12 (= I10), G15 (= G13), P16 (= P14), G17 (= G15), E36 (= E34), K37 (≠ S35), G49 (= G48), T50 (= T49), C51 (= C50), G55 (= G54), C56 (= C55), K60 (= K59), H123 (= H122), G124 (= G123), A152 (= A151), S153 (≠ T152), G154 (= G153), I194 (= I193), R281 (= R280), G320 (= G319), D321 (= D320), M327 (= M326), L328 (= L327), A329 (= A328), H330 (= H329), H453 (= H452), P454 (= P453)
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
70% identity, 99% coverage: 2:475/480 of query aligns to 1:473/473 of 5u8wA
- active site: P13 (= P14), L44 (= L46), C48 (= C50), C53 (= C55), S56 (= S58), G82 (≠ D84), V83 (= V85), V190 (= V192), E194 (= E196), S330 (= S332), F448 (= F450), H450 (= H452), E455 (= E457), N473 (= N475)
- binding flavin-adenine dinucleotide: I9 (= I10), G12 (= G13), P13 (= P14), G14 (= G15), E33 (= E34), K34 (≠ S35), G46 (= G48), T47 (= T49), C48 (= C50), G52 (= G54), C53 (= C55), K57 (= K59), H120 (= H122), G121 (= G123), A149 (= A151), S150 (≠ T152), G151 (= G153), S170 (= S172), G317 (= G319), D318 (= D320), M324 (= M326), L325 (= L327), A326 (= A328), H327 (= H329), Y357 (= Y359), H450 (= H452), P451 (= P453)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (= I188), G189 (= G191), V190 (= V192), I191 (= I193), E194 (= E196), E210 (= E212), A211 (= A213), L212 (≠ Q214), A275 (= A277), V276 (= V278), G277 (= G279), R278 (= R280), M324 (= M326), L325 (= L327), V355 (= V357), Y357 (= Y359)
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
70% identity, 98% coverage: 4:475/480 of query aligns to 2:472/472 of 5u8vA
- active site: P12 (= P14), L43 (= L46), C47 (= C50), C52 (= C55), S55 (= S58), G81 (≠ D84), V82 (= V85), V189 (= V192), E193 (= E196), S329 (= S332), F447 (= F450), H449 (= H452), E454 (= E457), N472 (= N475)
- binding flavin-adenine dinucleotide: I8 (= I10), G11 (= G13), P12 (= P14), G13 (= G15), E32 (= E34), G45 (= G48), T46 (= T49), C47 (= C50), G51 (= G54), C52 (= C55), K56 (= K59), H119 (= H122), G120 (= G123), A148 (= A151), S149 (≠ T152), G150 (= G153), S169 (= S172), I190 (= I193), R277 (= R280), G316 (= G319), D317 (= D320), M323 (= M326), L324 (= L327), A325 (= A328), H326 (= H329), H449 (= H452), P450 (= P453)
- binding nicotinamide-adenine-dinucleotide: I185 (= I188), G186 (= G189), G188 (= G191), V189 (= V192), I190 (= I193), L208 (= L211), E209 (= E212), A210 (= A213), V243 (≠ M246), V275 (= V278), G276 (= G279)
6awaA 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from pseudomonas putida in complex with fad and adenosine-5'-monophosphate.
70% identity, 99% coverage: 1:476/480 of query aligns to 1:475/475 of 6awaA
- active site: L45 (= L46), C49 (= C50), C54 (= C55), S57 (= S58), V191 (= V192), E195 (= E196), F449 (= F450), H451 (= H452), E456 (= E457), N474 (= N475), R475 (= R476)
- binding adenosine monophosphate: I187 (= I188), E211 (= E212), A212 (= A213), L213 (≠ Q214), V245 (≠ M246), V277 (= V278)
- binding flavin-adenine dinucleotide: I10 (= I10), G13 (= G13), P14 (= P14), G15 (= G15), E34 (= E34), K35 (≠ S35), T48 (= T49), C49 (= C50), G53 (= G54), C54 (= C55), K58 (= K59), H121 (= H122), G122 (= G123), S151 (≠ T152), G152 (= G153), I192 (= I193), R279 (= R280), G318 (= G319), D319 (= D320), M325 (= M326), L326 (= L327), A327 (= A328), Y358 (= Y359)
P18925 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Azotobacter vinelandii (see 2 papers)
68% identity, 100% coverage: 1:478/480 of query aligns to 1:477/477 of P18925
- 34:49 (vs. 34:50, 47% identical) binding
- C49 (= C50) modified: Disulfide link with 54, Redox-active
- C54 (= C55) modified: Disulfide link with 49, Redox-active
- K58 (= K59) binding
- D319 (= D320) binding
- A327 (= A328) 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)
67% identity, 99% coverage: 2:474/480 of query aligns to 1:472/472 of 3ladA
- active site: L44 (= L46), C48 (= C50), C53 (= C55), S56 (= S58), V190 (= V192), E194 (= E196), F448 (= F450), H450 (= H452), E455 (= E457)
- binding flavin-adenine dinucleotide: I9 (= I10), G10 (= G11), G12 (= G13), P13 (= P14), E33 (= E34), K34 (≠ S35), G46 (= G48), T47 (= T49), C48 (= C50), G52 (= G54), C53 (= C55), H120 (= H122), G121 (= G123), A149 (= A151), S150 (≠ T152), G151 (= G153), I191 (= I193), R278 (= R280), D318 (= D320), L325 (= L327), A326 (= A328)
6bz0A 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from acinetobacter baumannii in complex with fad.
58% identity, 98% coverage: 4:472/480 of query aligns to 1:467/469 of 6bz0A
- active site: C45 (= C50), C50 (= C55), S53 (= S58), V187 (= V192), E191 (= E196), H447 (= H452), E452 (= E457)
- binding flavin-adenine dinucleotide: I7 (= I10), G10 (= G13), P11 (= P14), G12 (= G15), E31 (= E34), K32 (≠ S35), R33 (≠ W36), G43 (= G48), T44 (= T49), C45 (= C50), G49 (= G54), C50 (= C55), K54 (= K59), T117 (≠ H122), G118 (= G123), S147 (≠ T152), G148 (= G153), S167 (= S172), I188 (= I193), R275 (= R280), Y278 (= Y283), D315 (= D320), M321 (= M326), L322 (= L327), A323 (= A328), A326 (= A331), Y354 (= Y359)
6aonA 1.72 angstrom resolution crystal structure of 2-oxoglutarate dehydrogenase complex subunit dihydrolipoamide dehydrogenase from bordetella pertussis in complex with fad
54% identity, 96% coverage: 4:466/480 of query aligns to 2:466/473 of 6aonA
- active site: P43 (≠ L46), C47 (= C50), C52 (= C55), S55 (= S58), V191 (= V192), E195 (= E196), H450 (≠ F450), H452 (= H452), E457 (= E457)
- binding calcium ion: A218 (≠ P219), A220 (≠ V221), Q222 (= Q223)
- binding flavin-adenine dinucleotide: I8 (= I10), G11 (= G13), P12 (= P14), G13 (= G15), D32 (≠ E34), A33 (≠ S35), W34 (= W36), G45 (= G48), T46 (= T49), C47 (= C50), G51 (= G54), C52 (= C55), K56 (= K59), K119 (≠ H122), G120 (= G123), T151 (= T152), G152 (= G153), N171 (≠ S172), I192 (= I193), R280 (= R280), Y283 (= Y283), G319 (= G319), D320 (= D320), M326 (= M326), L327 (= L327), A328 (= A328), H329 (= H329)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
49% identity, 98% coverage: 3:473/480 of query aligns to 5:470/470 of 6uziC
- active site: C45 (= C50), C50 (= C55), S53 (= S58), V187 (= V192), E191 (= E196), H448 (= H452), E453 (= E457)
- binding flavin-adenine dinucleotide: I12 (= I10), G13 (= G11), G15 (= G13), P16 (= P14), G17 (= G15), E36 (= E34), K37 (≠ S35), G43 (= G48), T44 (= T49), C45 (= C50), G49 (= G54), C50 (= C55), S53 (= S58), K54 (= K59), V117 (≠ H122), G118 (= G123), T147 (= T152), G148 (= G153), I188 (= I193), R276 (= R280), D316 (= D320), M322 (= M326), L323 (= L327), A324 (= A328)
- binding zinc ion: H448 (= H452), E453 (= E457)
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, 97% coverage: 6:469/480 of query aligns to 43:504/509 of P09622
- 71:80 (vs. 34:50, 41% identical) binding
- K72 (= K42) to E: in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX; dbSNP:rs121964987
- K89 (= K59) binding ; mutation to E: Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- K104 (≠ H73) to T: in dbSNP:rs1130477
- G154 (= G123) binding
- TGS 183:185 (= TGS 152:154) binding
- 220:227 (vs. 189:196, 88% identical) binding
- E243 (= E212) binding
- V278 (≠ M246) binding
- G314 (= G279) binding
- D355 (= D320) binding
- MLAH 361:364 (= MLAH 326:329) binding
- E375 (= E340) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (≠ Q348) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (= D413) 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 (≠ Q431) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ F438) 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 (= D444) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (≠ L447) 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 (≠ F450) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
- P488 (= P453) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
- S491 (= S456) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
- E492 (= E457) mutation to Q: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- R495 (≠ H460) 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.
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
50% identity, 98% coverage: 5:472/480 of query aligns to 1:465/465 of 3urhB
- active site: Y35 (≠ L46), C39 (= C50), C44 (= C55), S47 (= S58), V183 (= V192), E187 (= E196), H443 (≠ F450), H445 (= H452), E450 (= E457)
- binding flavin-adenine dinucleotide: I6 (= I10), G7 (= G11), G9 (= G13), P10 (= P14), G11 (= G15), E30 (= E34), K31 (= K42), G37 (= G48), T38 (= T49), C39 (= C50), G43 (= G54), C44 (= C55), K48 (= K59), T111 (≠ H122), G112 (= G123), A140 (= A151), T141 (= T152), G142 (= G153), I184 (= I193), R273 (= R280), G312 (= G319), D313 (= D320), M319 (= M326), L320 (= L327), A321 (= A328), H322 (= H329)
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
50% identity, 97% coverage: 6:469/480 of query aligns to 6:467/472 of 1zmdA
- active site: L39 (= L46), C43 (= C50), C48 (= C55), S51 (= S58), V186 (= V192), E190 (= E196), H448 (≠ F450), H450 (= H452), E455 (= E457)
- binding flavin-adenine dinucleotide: I10 (= I10), G11 (= G11), G13 (= G13), P14 (= P14), G15 (= G15), E34 (= E34), K35 (= K42), N36 (≠ A43), G41 (= G48), T42 (= T49), C43 (= C50), G47 (= G54), C48 (= C55), K52 (= K59), Y116 (≠ H122), G117 (= G123), T146 (= T152), G147 (= G153), S166 (= S172), R278 (= R280), F281 (≠ Y283), G317 (= G319), D318 (= D320), M324 (= M326), L325 (= L327), A326 (= A328), H327 (= H329)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (= I188), G183 (= G189), G185 (= G191), V186 (= V192), I187 (= I193), E190 (= E196), E206 (= E212), F207 (= F217), L208 (= L218), I276 (≠ V278), G277 (= G279), R278 (= R280), M324 (= M326), L325 (= L327), V355 (= V357), Y357 (= Y359)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
50% identity, 97% coverage: 6:469/480 of query aligns to 6:467/472 of 1zmcA
- active site: L39 (= L46), C43 (= C50), C48 (= C55), S51 (= S58), V186 (= V192), E190 (= E196), H448 (≠ F450), H450 (= H452), E455 (= E457)
- binding flavin-adenine dinucleotide: I10 (= I10), G11 (= G11), G13 (= G13), P14 (= P14), G15 (= G15), E34 (= E34), K35 (= K42), N36 (≠ A43), G41 (= G48), T42 (= T49), C43 (= C50), G47 (= G54), C48 (= C55), K52 (= K59), Y116 (≠ H122), G117 (= G123), T146 (= T152), G147 (= G153), S166 (= S172), I187 (= I193), F281 (≠ Y283), G317 (= G319), D318 (= D320), M324 (= M326), L325 (= L327), A326 (= A328), H327 (= H329)
- binding nicotinamide-adenine-dinucleotide: G183 (= G189), G185 (= G191), V205 (≠ L211), E206 (= E212), F207 (= F217), L208 (= L218), K240 (≠ R245), V241 (≠ M246), I276 (≠ V278), G277 (= G279), R278 (= R280), R297 (= R299), M324 (= M326)
6hg8B Crystal structure of the r460g disease-causing mutant of the human dihydrolipoamide dehydrogenase.
50% identity, 96% coverage: 6:465/480 of query aligns to 16:473/482 of 6hg8B
- active site: C53 (= C50), C58 (= C55), S61 (= S58), V196 (= V192), E200 (= E196), H460 (= H452), E465 (= E457)
- binding flavin-adenine dinucleotide: I20 (= I10), G23 (= G13), P24 (= P14), G25 (= G15), E44 (= E34), K45 (= K42), N46 (≠ A43), G51 (= G48), T52 (= T49), C53 (= C50), G57 (= G54), C58 (= C55), K62 (= K59), Y126 (≠ H122), G127 (= G123), T156 (= T152), G157 (= G153), I197 (= I193), R288 (= R280), F291 (≠ Y283), G327 (= G319), D328 (= D320), M334 (= M326), L335 (= L327), A336 (= A328), H337 (= H329)
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)
47% identity, 98% coverage: 2:473/480 of query aligns to 35:501/501 of P31023
- 67:76 (vs. 34:50, 41% identical) binding
- C76 (= C50) modified: Disulfide link with 81, Redox-active
- C81 (= C55) modified: Disulfide link with 76, Redox-active
- G149 (= G123) binding
- D348 (= D320) binding
- MLAH 354:357 (= MLAH 326:329) binding
Sites not aligning to the query:
- 1:31 modified: transit peptide, Mitochondrion
1dxlA Dihydrolipoamide dehydrogenase of glycine decarboxylase from pisum sativum (see paper)
47% identity, 98% coverage: 2:473/480 of query aligns to 1:467/467 of 1dxlA
- active site: L38 (= L46), C42 (= C50), C47 (= C55), S50 (= S58), Y184 (≠ V192), E188 (= E196), H444 (≠ F450), H446 (= H452), E451 (= E457)
- binding flavin-adenine dinucleotide: I9 (= I10), P13 (= P14), G14 (= G15), E33 (= E34), K34 (= K42), R35 (≠ A43), G40 (= G48), T41 (= T49), C42 (= C50), G46 (= G54), C47 (= C55), K51 (= K59), Y114 (≠ H122), G115 (= G123), T144 (= T152), G145 (= G153), Y184 (≠ V192), I185 (= I193), R274 (= R280), D314 (= D320), M320 (= M326), L321 (= L327), A322 (= A328), H323 (= H329)
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
49% identity, 98% coverage: 5:473/480 of query aligns to 2:455/455 of 2yquB
- active site: P11 (= P14), L36 (= L46), C40 (= C50), C45 (= C55), S48 (= S58), G72 (≠ D84), V73 (= V85), V177 (= V192), E181 (= E196), S314 (= S332), H432 (≠ F450), H434 (= H452), E439 (= E457)
- binding carbonate ion: A310 (= A328), S314 (= S332), S423 (= S441), D426 (= D444)
- binding flavin-adenine dinucleotide: G8 (= G11), G10 (= G13), P11 (= P14), G12 (= G15), E31 (= E34), K32 (= K42), G38 (= G48), T39 (= T49), C40 (= C50), R42 (≠ N52), G44 (= G54), C45 (= C55), K49 (= K59), T110 (≠ H122), A111 (≠ G123), T137 (= T152), G138 (= G153), I178 (= I193), Y265 (= Y283), G301 (= G319), D302 (= D320), M308 (= M326), L309 (= L327), A310 (= A328), H311 (= H329)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
49% identity, 98% coverage: 5:473/480 of query aligns to 2:455/455 of 2yquA
- active site: P11 (= P14), L36 (= L46), C40 (= C50), C45 (= C55), S48 (= S58), G72 (≠ D84), V73 (= V85), V177 (= V192), E181 (= E196), S314 (= S332), H432 (≠ F450), H434 (= H452), E439 (= E457)
- binding flavin-adenine dinucleotide: G8 (= G11), G10 (= G13), P11 (= P14), G12 (= G15), E31 (= E34), K32 (= K42), G38 (= G48), T39 (= T49), C40 (= C50), R42 (≠ N52), G44 (= G54), C45 (= C55), K49 (= K59), T110 (≠ H122), A111 (≠ G123), T137 (= T152), G138 (= G153), S157 (= S172), I178 (= I193), Y265 (= Y283), G301 (= G319), D302 (= D320), M308 (= M326), L309 (= L327), A310 (= A328)
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
49% identity, 96% coverage: 5:465/480 of query aligns to 2:447/452 of 2eq7A
- active site: P11 (= P14), L36 (= L46), C40 (= C50), C45 (= C55), S48 (= S58), G72 (≠ D84), V73 (= V85), V177 (= V192), E181 (= E196), S314 (= S332), H432 (≠ F450), H434 (= H452), E439 (= E457)
- binding flavin-adenine dinucleotide: G10 (= G13), P11 (= P14), G12 (= G15), E31 (= E34), K32 (= K42), G38 (= G48), T39 (= T49), C40 (= C50), R42 (≠ N52), G44 (= G54), C45 (= C55), K49 (= K59), T110 (≠ H122), A111 (≠ G123), T137 (= T152), G138 (= G153), S157 (= S172), I178 (= I193), R262 (= R280), Y265 (= Y283), D302 (= D320), M308 (= M326), L309 (= L327), A310 (= A328), H311 (= H329), Y341 (= Y359)
- binding nicotinamide-adenine-dinucleotide: W146 (≠ P161), G174 (= G189), G176 (= G191), V177 (= V192), I178 (= I193), E197 (= E212), Y198 (≠ A213), V231 (≠ M246), V260 (= V278), G261 (= G279), R262 (= R280), M308 (= M326), L309 (= L327), V339 (= V357)
Query Sequence
>GFF1561 FitnessBrowser__Marino:GFF1561
MSDKYDVIVIGAGPGGYVAAIKAAQLGLKTACVESWTSEDGKAQVLGGTCLNVGCIPSKA
LLEISHKFEESSHDFEMQGIIAKDVKMDIGKMMERKSGIVKQLTGGIAGLFKSNGVTSIH
GHGKLLANRKVEVTDKDGKSKTYEAENIILATGSKPIQIPPAPFDGEYIVDSEGALEFTE
VPKRLGVIGAGVIGLELGSVWARLGAEVTVLEAQDTFLPAVDQQVAKDALKQFQKQGLNI
VMGARMTGAEVKRKLVNVNYEDSKGKHEAKFDKLIVAVGRRPYTDNLLSEDSGVQMDERG
FIFVDDNCKTEAPGVWAIGDVVRGPMLAHKASEEGIMVAERIAGHKPQVNYDCIPNVVYT
FPEVAWVGKTEEQMKAEGEEYNVGTFPFAANGRAMAANSASGLVKIIADAKTDRIVGFHV
VGPQASEIVAQGVIAMEFGSSAEDLALTCFAHPTLSESVHEAALAVGGGAIHIANRRKKK
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