SitesBLAST
Comparing GFF2444 FitnessBrowser__psRCH2:GFF2444 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)
P18925 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of pyruvate complex; EC 1.8.1.4 from Azotobacter vinelandii (see 2 papers)
86% identity, 100% coverage: 1:477/478 of query aligns to 1:477/477 of P18925
- 34:49 (vs. 34:49, 88% identical) binding
- C49 (= C49) modified: Disulfide link with 54, Redox-active
- C54 (= C54) modified: Disulfide link with 49, Redox-active
- K58 (= K58) binding
- D319 (= D319) binding
- A327 (= A327) binding
P14218 Dihydrolipoyl dehydrogenase; Dihydrolipoamide dehydrogenase; E3 component of 2-oxoglutarate dehydrogenase complex; EC 1.8.1.4 from Pseudomonas fluorescens (see 2 papers)
86% identity, 100% coverage: 1:478/478 of query aligns to 1:478/478 of P14218
- M1 (= M1) modified: Initiator methionine, Removed
- 34:49 (vs. 34:49, 81% 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 (= D319) binding
- A327 (= A327) 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)
86% identity, 99% coverage: 2:473/478 of query aligns to 1:472/472 of 3ladA
- active site: L44 (= L45), C48 (= C49), C53 (= C54), S56 (= S57), V190 (= V191), E194 (= E195), F448 (= F449), H450 (= H451), E455 (= E456)
- 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 (= A150), S150 (= S151), G151 (= G152), I191 (= I192), R278 (= R279), D318 (= D319), L325 (= L326), A326 (= A327)
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
86% identity, 99% coverage: 1:475/478 of query aligns to 3:477/477 of 5u8uD
- active site: P16 (= P14), L47 (= L45), C51 (= C49), C56 (= C54), S59 (= S57), G85 (≠ E83), V86 (= V84), V193 (= V191), E197 (= E195), S333 (= S331), F451 (= F449), H453 (= H451), E458 (= E456), N476 (= N474), R477 (= R475)
- 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 (= A150), S153 (= S151), G154 (= G152), I194 (= I192), R281 (= R279), G320 (= G318), D321 (= D319), M327 (= M325), L328 (= L326), A329 (= A327), H330 (= H328), H453 (= H451), P454 (= P452)
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
86% identity, 99% coverage: 2:474/478 of query aligns to 1:473/473 of 5u8wA
- active site: P13 (= P14), L44 (= L45), C48 (= C49), C53 (= C54), S56 (= S57), G82 (≠ E83), V83 (= V84), V190 (= V191), E194 (= E195), S330 (= S331), F448 (= F449), H450 (= H451), E455 (= E456), N473 (= N474)
- 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 (= A150), S150 (= S151), G151 (= G152), S170 (= S171), G317 (= G318), D318 (= D319), M324 (= M325), L325 (= L326), A326 (= A327), H327 (= H328), Y357 (= Y358), H450 (= H451), P451 (= P452)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (= I187), G189 (= G190), V190 (= V191), I191 (= I192), E194 (= E195), E210 (= E211), A211 (= A212), L212 (≠ M213), A275 (= A276), V276 (= V277), G277 (= G278), R278 (= R279), M324 (= M325), L325 (= L326), V355 (= V356), Y357 (= Y358)
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
86% identity, 99% coverage: 3:474/478 of query aligns to 1:472/472 of 5u8vA
- active site: P12 (= P14), L43 (= L45), C47 (= C49), C52 (= C54), S55 (= S57), G81 (≠ E83), V82 (= V84), V189 (= V191), E193 (= E195), S329 (= S331), F447 (= F449), H449 (= H451), E454 (= E456), N472 (= N474)
- 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 (= A150), S149 (= S151), G150 (= G152), S169 (= S171), I190 (= I192), R277 (= R279), G316 (= G318), D317 (= D319), M323 (= M325), L324 (= L326), A325 (= A327), H326 (= H328), H449 (= H451), P450 (= P452)
- binding nicotinamide-adenine-dinucleotide: I185 (= I187), G186 (= G188), G188 (= G190), V189 (= V191), I190 (= I192), L208 (≠ I210), E209 (= E211), A210 (= A212), V243 (≠ L245), V275 (= V277), G276 (= G278)
6awaA 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from pseudomonas putida in complex with fad and adenosine-5'-monophosphate.
82% identity, 99% coverage: 1:475/478 of query aligns to 1:475/475 of 6awaA
- active site: L45 (= L45), C49 (= C49), C54 (= C54), S57 (= S57), V191 (= V191), E195 (= E195), F449 (= F449), H451 (= H451), E456 (= E456), N474 (= N474), R475 (= R475)
- binding adenosine monophosphate: I187 (= I187), E211 (= E211), A212 (= A212), L213 (≠ M213), V245 (≠ L245), V277 (= V277)
- 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 (= S151), G152 (= G152), I192 (= I192), R279 (= R279), G318 (= G318), D319 (= D319), M325 (= M325), L326 (= L326), A327 (= A327), Y358 (= Y358)
6bz0A 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from acinetobacter baumannii in complex with fad.
63% identity, 98% coverage: 4:471/478 of query aligns to 1:467/469 of 6bz0A
- active site: C45 (= C49), C50 (= C54), S53 (= S57), V187 (= V191), E191 (= E195), H447 (= H451), E452 (= E456)
- binding flavin-adenine dinucleotide: I7 (= I10), G10 (= G13), P11 (= P14), G12 (= G15), E31 (= E34), K32 (= K35), R33 (≠ Q37), G43 (= G47), T44 (= T48), C45 (= C49), G49 (= G53), C50 (= C54), K54 (= K58), T117 (≠ H121), G118 (= G122), S147 (= S151), G148 (= G152), S167 (= S171), I188 (= I192), R275 (= R279), Y278 (≠ V282), D315 (= D319), M321 (= M325), L322 (= L326), A323 (= A327), A326 (= A330), Y354 (= Y358)
6aonA 1.72 angstrom resolution crystal structure of 2-oxoglutarate dehydrogenase complex subunit dihydrolipoamide dehydrogenase from bordetella pertussis in complex with fad
53% identity, 98% coverage: 3:472/478 of query aligns to 1:473/473 of 6aonA
- active site: P43 (≠ L45), C47 (= C49), C52 (= C54), S55 (= S57), V191 (= V191), E195 (= E195), H450 (≠ F449), H452 (= H451), E457 (= E456)
- binding calcium ion: A218 (≠ P218), A220 (= A220), Q222 (≠ E222)
- binding flavin-adenine dinucleotide: I8 (= I10), G11 (= G13), P12 (= P14), G13 (= G15), D32 (≠ E34), A33 (≠ K35), W34 (≠ Y36), G45 (= G47), T46 (= T48), C47 (= C49), G51 (= G53), C52 (= C54), K56 (= K58), K119 (≠ H121), G120 (= G122), T151 (≠ S151), G152 (= G152), N171 (≠ S171), I192 (= I192), R280 (= R279), Y283 (≠ V282), G319 (= G318), D320 (= D319), M326 (= M325), L327 (= L326), A328 (= A327), H329 (= H328)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
50% identity, 98% coverage: 3:472/478 of query aligns to 5:470/470 of 6uziC
- active site: C45 (= C49), C50 (= C54), S53 (= S57), V187 (= V191), E191 (= E195), H448 (= H451), E453 (= E456)
- 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 (≠ S151), G148 (= G152), I188 (= I192), R276 (= R279), D316 (= D319), M322 (= M325), L323 (= L326), A324 (= A327)
- binding zinc ion: H448 (= H451), E453 (= E456)
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
50% identity, 98% coverage: 5:471/478 of query aligns to 1:465/465 of 3urhB
- active site: Y35 (≠ L45), C39 (= C49), C44 (= C54), S47 (= S57), V183 (= V191), E187 (= E195), H443 (≠ F449), H445 (= H451), E450 (= E456)
- 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 (= A150), T141 (≠ S151), G142 (= G152), I184 (= I192), R273 (= R279), G312 (= G318), D313 (= D319), M319 (= M325), L320 (= L326), A321 (= A327), H322 (= H328)
P09622 Dihydrolipoyl dehydrogenase, mitochondrial; Dihydrolipoamide dehydrogenase; Glycine cleavage system L protein; EC 1.8.1.4 from Homo sapiens (Human) (see 14 papers)
49% identity, 96% coverage: 6:464/478 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 (≠ E72) to T: in dbSNP:rs1130477
- G154 (= G122) binding
- TGS 183:185 (≠ SGS 151:153) binding
- 220:227 (vs. 188:195, 88% identical) binding
- E243 (= E211) binding
- V278 (≠ L245) binding
- G314 (= G278) binding
- D355 (= D319) binding
- MLAH 361:364 (= MLAH 325:328) binding
- E375 (= E339) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (≠ Q347) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (= D412) 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 (≠ Q430) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ F437) 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 (= D443) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (≠ M446) 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 (≠ F449) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
- P488 (= P452) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
- S491 (= S455) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
- E492 (= E456) mutation to Q: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- R495 (≠ H459) 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)
49% identity, 96% coverage: 6:464/478 of query aligns to 6:463/472 of 1zmdA
- active site: L39 (= L45), C43 (= C49), C48 (= C54), S51 (= S57), V186 (= V191), E190 (= E195), H448 (≠ F449), H450 (= H451), E455 (= E456)
- binding flavin-adenine dinucleotide: I10 (= I10), G11 (= G11), G13 (= G13), P14 (= P14), G15 (= G15), E34 (= E34), K35 (= K35), N36 (≠ Y36), G41 (= G47), T42 (= T48), C43 (= C49), G47 (= G53), C48 (= C54), K52 (= K58), Y116 (≠ H121), G117 (= G122), T146 (≠ S151), G147 (= G152), S166 (= S171), R278 (= R279), F281 (≠ V282), G317 (= G318), D318 (= D319), M324 (= M325), L325 (= L326), A326 (= A327), H327 (= H328)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (= I187), G183 (= G188), G185 (= G190), V186 (= V191), I187 (= I192), E190 (= E195), E206 (= E211), F207 (≠ A212), L208 (≠ M213), I276 (≠ V277), G277 (= G278), R278 (= R279), M324 (= M325), L325 (= L326), V355 (= V356), Y357 (= Y358)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
49% identity, 96% coverage: 6:464/478 of query aligns to 6:463/472 of 1zmcA
- active site: L39 (= L45), C43 (= C49), C48 (= C54), S51 (= S57), V186 (= V191), E190 (= E195), H448 (≠ F449), H450 (= H451), E455 (= E456)
- binding flavin-adenine dinucleotide: I10 (= I10), G11 (= G11), G13 (= G13), P14 (= P14), G15 (= G15), E34 (= E34), K35 (= K35), N36 (≠ Y36), G41 (= G47), T42 (= T48), C43 (= C49), G47 (= G53), C48 (= C54), K52 (= K58), Y116 (≠ H121), G117 (= G122), T146 (≠ S151), G147 (= G152), S166 (= S171), I187 (= I192), F281 (≠ V282), G317 (= G318), D318 (= D319), M324 (= M325), L325 (= L326), A326 (= A327), H327 (= H328)
- binding nicotinamide-adenine-dinucleotide: G183 (= G188), G185 (= G190), V205 (≠ I210), E206 (= E211), F207 (≠ A212), L208 (≠ M213), K240 (≠ R244), V241 (≠ L245), I276 (≠ V277), G277 (= G278), R278 (= R279), R297 (= R298), M324 (= M325)
6hg8B Crystal structure of the r460g disease-causing mutant of the human dihydrolipoamide dehydrogenase.
49% identity, 96% coverage: 6:464/478 of query aligns to 16:473/482 of 6hg8B
- active site: C53 (= C49), C58 (= C54), S61 (= S57), V196 (= V191), E200 (= E195), H460 (= H451), E465 (= E456)
- binding flavin-adenine dinucleotide: I20 (= I10), G23 (= G13), P24 (= P14), G25 (= G15), E44 (= E34), K45 (= K35), N46 (≠ Y36), G51 (= G47), T52 (= T48), C53 (= C49), G57 (= G53), C58 (= C54), K62 (= K58), Y126 (≠ H121), G127 (= G122), T156 (≠ S151), G157 (= G152), I197 (= I192), R288 (= R279), F291 (≠ V282), G327 (= G318), D328 (= D319), M334 (= M325), L335 (= L326), A336 (= A327), H337 (= H328)
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)
48% identity, 99% coverage: 2:472/478 of query aligns to 35:501/501 of P31023
- 67:76 (vs. 34:49, 50% identical) binding
- C76 (= C49) modified: Disulfide link with 81, Redox-active
- C81 (= C54) modified: Disulfide link with 76, Redox-active
- G149 (= G122) binding
- D348 (= D319) binding
- MLAH 354:357 (= MLAH 325:328) binding
Sites not aligning to the query:
- 1:31 modified: transit peptide, Mitochondrion
1dxlA Dihydrolipoamide dehydrogenase of glycine decarboxylase from pisum sativum (see paper)
48% identity, 99% coverage: 2:472/478 of query aligns to 1:467/467 of 1dxlA
- active site: L38 (= L45), C42 (= C49), C47 (= C54), S50 (= S57), Y184 (≠ V191), E188 (= E195), H444 (≠ F449), H446 (= H451), E451 (= E456)
- binding flavin-adenine dinucleotide: I9 (= I10), P13 (= P14), G14 (= G15), E33 (= E34), K34 (= K35), R35 (≠ K42), G40 (= G47), T41 (= T48), C42 (= C49), G46 (= G53), C47 (= C54), K51 (= K58), Y114 (≠ H121), G115 (= G122), T144 (≠ S151), G145 (= G152), Y184 (≠ V191), I185 (= I192), R274 (= R279), D314 (= D319), M320 (= M325), L321 (= L326), A322 (= A327), H323 (= H328)
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
48% identity, 98% coverage: 5:472/478 of query aligns to 2:455/455 of 2yquB
- active site: P11 (= P14), L36 (= L45), C40 (= C49), C45 (= C54), S48 (= S57), G72 (= G78), V73 (≠ I79), V177 (= V191), E181 (= E195), S314 (= S331), H432 (≠ F449), H434 (= H451), E439 (= E456)
- binding carbonate ion: A310 (= A327), S314 (= S331), S423 (= S440), D426 (= D443)
- 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 (≠ S151), G138 (= G152), I178 (= I192), Y265 (≠ V282), G301 (= G318), D302 (= D319), M308 (= M325), L309 (= L326), A310 (= A327), H311 (= H328)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
48% identity, 98% coverage: 5:472/478 of query aligns to 2:455/455 of 2yquA
- active site: P11 (= P14), L36 (= L45), C40 (= C49), C45 (= C54), S48 (= S57), G72 (= G78), V73 (≠ I79), V177 (= V191), E181 (= E195), S314 (= S331), H432 (≠ F449), H434 (= H451), E439 (= E456)
- 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 (≠ S151), G138 (= G152), S157 (= S171), I178 (= I192), Y265 (≠ V282), G301 (= G318), D302 (= D319), M308 (= M325), L309 (= L326), A310 (= A327)
2eq7A Crystal structure of lipoamide dehydrogenase from thermus thermophilus hb8 with psbdo
49% identity, 96% coverage: 5:464/478 of query aligns to 2:447/452 of 2eq7A
- active site: P11 (= P14), L36 (= L45), C40 (= C49), C45 (= C54), S48 (= S57), G72 (= G78), V73 (≠ I79), V177 (= V191), E181 (= E195), S314 (= S331), H432 (≠ F449), H434 (= H451), E439 (= E456)
- 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 (≠ S151), G138 (= G152), S157 (= S171), I178 (= I192), R262 (= R279), Y265 (≠ V282), D302 (= D319), M308 (= M325), L309 (= L326), A310 (= A327), H311 (= H328), Y341 (= Y358)
- binding nicotinamide-adenine-dinucleotide: W146 (≠ P160), G174 (= G188), G176 (= G190), V177 (= V191), I178 (= I192), E197 (= E211), Y198 (≠ A212), V231 (≠ L245), V260 (= V277), G261 (= G278), R262 (= R279), M308 (= M325), L309 (= L326), V339 (= V356)
Query Sequence
>GFF2444 FitnessBrowser__psRCH2:GFF2444
MSQKFDVVVIGAGPGGYVAAIRAAQLGLKTACIEKYQGKDGKTALGGTCLNVGCIPSKAL
LDSSYKFHEAHESFKVHGISTGEVAMDVPTMVARKDQIVKNLTGGVSALLKANGVTVFEG
HGKLLAGKQVEVTGLDGNVQTLAAENVILASGSTPVNIPPAPVDQKVIVDSTGALDFQGV
PGKLGVIGAGVIGLELGSVWARLGAEVTVIEAMDKFLPAADEQISKEAFKILSKQGLKIL
LGARLTGSEVKGDQVTVSFTSAEGEQQMTFDKLIVAVGRRPVTSELLAADTGVDMDERGF
IFVDDYCATSVPGVYAIGDVVRGAMLAHKASEEGVMVAERIAGHKTQMNYDLIPSVIYTH
PEIAWVGKSEQVLKAEGVEVNVGTFPFAASGRAMAANDTAGLVKVIADAKTDRVLGVHVM
GPSAAELVQQGAIGMEFGTSAEDLGMMVFSHPTMSEALHEAALAVNGHAIHIANRKKR
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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