SitesBLAST
Comparing RR42_RS12930 FitnessBrowser__Cup4G11:RR42_RS12930 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
61% identity, 100% coverage: 3:478/478 of query aligns to 1:473/473 of 6aonA
- active site: P43 (≠ L47), C47 (= C51), C52 (= C56), S55 (= S59), V191 (= V196), E195 (= E200), H450 (= H455), H452 (= H457), E457 (= E462)
- binding calcium ion: A218 (≠ G223), A220 (= A225), Q222 (≠ E227)
- binding flavin-adenine dinucleotide: I8 (= I10), G11 (= G13), P12 (= P14), G13 (= G15), D32 (≠ N36), A33 (= A37), W34 (≠ Y38), G45 (= G49), T46 (= T50), C47 (= C51), G51 (= G55), C52 (= C56), K56 (= K60), K119 (≠ Y123), G120 (= G124), T151 (= T156), G152 (= G157), N171 (= N176), I192 (= I197), R280 (= R285), Y283 (≠ N288), G319 (= G324), D320 (= D325), M326 (= M331), L327 (= L332), A328 (= A333), H329 (= H334)
6awaA 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from pseudomonas putida in complex with fad and adenosine-5'-monophosphate.
55% identity, 99% coverage: 1:472/478 of query aligns to 1:466/475 of 6awaA
- active site: L45 (= L47), C49 (= C51), C54 (= C56), S57 (= S59), V191 (= V196), E195 (= E200), F449 (≠ H455), H451 (= H457), E456 (= E462)
- binding adenosine monophosphate: I187 (= I192), E211 (= E216), A212 (= A217), L213 (= L218), V245 (= V250), V277 (= V283)
- binding flavin-adenine dinucleotide: I10 (= I10), G13 (= G13), P14 (= P14), G15 (= G15), E34 (= E34), K35 (≠ A37), T48 (= T50), C49 (= C51), G53 (= G55), C54 (= C56), K58 (= K60), H121 (≠ Y123), G122 (= G124), S151 (≠ T156), G152 (= G157), I192 (= I197), R279 (= R285), G318 (= G324), D319 (= D325), M325 (= M331), L326 (= L332), A327 (= A333), Y358 (= Y364)
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)
55% identity, 100% coverage: 1:478/478 of query aligns to 1:472/478 of P14218
- M1 (= M1) modified: Initiator methionine, Removed
- 34:49 (vs. 34:51, 39% identical) binding
- C49 (= C51) modified: Disulfide link with 54, Redox-active
- C54 (= C56) modified: Disulfide link with 49, Redox-active
- K58 (= K60) binding
- G122 (= G124) binding
- D319 (= D325) binding
- A327 (= A333) binding
5u8uD Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa (see paper)
55% identity, 100% coverage: 1:478/478 of query aligns to 3:474/477 of 5u8uD
- active site: P16 (= P14), L47 (= L47), C51 (= C51), C56 (= C56), S59 (= S59), G85 (≠ D85), V86 (= V86), V193 (= V196), E197 (= E200), S333 (≠ E337), F451 (≠ H455), H453 (= H457), E458 (= E462)
- binding flavin-adenine dinucleotide: I12 (= I10), G15 (= G13), P16 (= P14), G17 (= G15), E36 (= E34), K37 (≠ A37), G49 (= G49), T50 (= T50), C51 (= C51), G55 (= G55), C56 (= C56), K60 (= K60), H123 (≠ Y123), G124 (= G124), A152 (= A155), S153 (≠ T156), G154 (= G157), I194 (= I197), R281 (= R285), G320 (= G324), D321 (= D325), M327 (= M331), L328 (= L332), A329 (= A333), H330 (= H334), H453 (= H457), P454 (= P458)
Sites not aligning to the query:
5u8wA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to nadh (see paper)
55% identity, 100% coverage: 2:478/478 of query aligns to 1:471/473 of 5u8wA
- active site: P13 (= P14), L44 (= L47), C48 (= C51), C53 (= C56), S56 (= S59), G82 (≠ D85), V83 (= V86), V190 (= V196), E194 (= E200), S330 (≠ E337), F448 (≠ H455), H450 (= H457), E455 (= E462)
- binding flavin-adenine dinucleotide: I9 (= I10), G12 (= G13), P13 (= P14), G14 (= G15), E33 (= E34), K34 (≠ A37), G46 (= G49), T47 (= T50), C48 (= C51), G52 (= G55), C53 (= C56), K57 (= K60), H120 (≠ Y123), G121 (= G124), A149 (= A155), S150 (≠ T156), G151 (= G157), S170 (≠ N176), G317 (= G324), D318 (= D325), M324 (= M331), L325 (= L332), A326 (= A333), H327 (= H334), Y357 (= Y364), H450 (= H457), P451 (= P458)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I186 (= I192), G189 (= G195), V190 (= V196), I191 (= I197), E194 (= E200), E210 (= E216), A211 (= A217), L212 (= L218), A275 (≠ S282), V276 (= V283), G277 (= G284), R278 (= R285), M324 (= M331), L325 (= L332), V355 (= V362), Y357 (= Y364)
Sites not aligning to the query:
5u8vA Dihydrolipoamide dehydrogenase (lpdg) from pseudomonas aeruginosa bound to NAD+ (see paper)
55% identity, 100% coverage: 3:478/478 of query aligns to 1:470/472 of 5u8vA
- active site: P12 (= P14), L43 (= L47), C47 (= C51), C52 (= C56), S55 (= S59), G81 (≠ D85), V82 (= V86), V189 (= V196), E193 (= E200), S329 (≠ E337), F447 (≠ H455), H449 (= H457), E454 (= E462)
- binding flavin-adenine dinucleotide: I8 (= I10), G11 (= G13), P12 (= P14), G13 (= G15), E32 (= E34), G45 (= G49), T46 (= T50), C47 (= C51), G51 (= G55), C52 (= C56), K56 (= K60), H119 (≠ Y123), G120 (= G124), A148 (= A155), S149 (≠ T156), G150 (= G157), S169 (≠ N176), I190 (= I197), R277 (= R285), G316 (= G324), D317 (= D325), M323 (= M331), L324 (= L332), A325 (= A333), H326 (= H334), H449 (= H457), P450 (= P458)
- binding nicotinamide-adenine-dinucleotide: I185 (= I192), G186 (= G193), G188 (= G195), V189 (= V196), I190 (= I197), L208 (= L215), E209 (= E216), A210 (= A217), V243 (= V250), V275 (= V283), G276 (= G284)
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: 1:478/478 of query aligns to 1:472/477 of P18925
- 34:49 (vs. 34:51, 39% identical) binding
- C49 (= C51) modified: Disulfide link with 54, Redox-active
- C54 (= C56) modified: Disulfide link with 49, Redox-active
- K58 (= K60) binding
- D319 (= D325) binding
- A327 (= A333) 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: 2:478/478 of query aligns to 1:471/472 of 3ladA
- active site: L44 (= L47), C48 (= C51), C53 (= C56), S56 (= S59), V190 (= V196), E194 (= E200), F448 (≠ H455), H450 (= H457), E455 (= E462)
- binding flavin-adenine dinucleotide: I9 (= I10), G10 (= G11), G12 (= G13), P13 (= P14), E33 (= E34), K34 (≠ A37), G46 (= G49), T47 (= T50), C48 (= C51), G52 (= G55), C53 (= C56), H120 (≠ Y123), G121 (= G124), A149 (= A155), S150 (≠ T156), G151 (= G157), I191 (= I197), R278 (= R285), D318 (= D325), L325 (= L332), A326 (= A333)
6uziC Crystal structure of dihydrolipoyl dehydrogenase from elizabethkingia anophelis nuhp1
53% identity, 99% coverage: 4:478/478 of query aligns to 6:470/470 of 6uziC
- active site: C45 (= C51), C50 (= C56), S53 (= S59), V187 (= V196), E191 (= E200), H448 (= H457), E453 (= E462)
- binding flavin-adenine dinucleotide: I12 (= I10), G13 (= G11), G15 (= G13), P16 (= P14), G17 (= G15), E36 (= E34), K37 (≠ G35), G43 (= G49), T44 (= T50), C45 (= C51), G49 (= G55), C50 (= C56), S53 (= S59), K54 (= K60), V117 (≠ Y123), G118 (= G124), T147 (= T156), G148 (= G157), I188 (= I197), R276 (= R285), D316 (= D325), M322 (= M331), L323 (= L332), A324 (= A333)
- binding zinc ion: H448 (= H457), E453 (= E462)
6bz0A 1.83 angstrom resolution crystal structure of dihydrolipoyl dehydrogenase from acinetobacter baumannii in complex with fad.
53% identity, 99% coverage: 4:477/478 of query aligns to 1:467/469 of 6bz0A
- active site: C45 (= C51), C50 (= C56), S53 (= S59), V187 (= V196), E191 (= E200), H447 (= H457), E452 (= E462)
- binding flavin-adenine dinucleotide: I7 (= I10), G10 (= G13), P11 (= P14), G12 (= G15), E31 (= E34), K32 (≠ G35), R33 (≠ N36), G43 (= G49), T44 (= T50), C45 (= C51), G49 (= G55), C50 (= C56), K54 (= K60), T117 (≠ Y123), G118 (= G124), S147 (≠ T156), G148 (= G157), S167 (≠ N176), I188 (= I197), R275 (= R285), Y278 (≠ N288), D315 (= D325), M321 (= M331), L322 (= L332), A323 (= A333), A326 (= A336), Y354 (= Y364)
3urhB Crystal structure of a dihydrolipoamide dehydrogenase from sinorhizobium meliloti 1021
51% identity, 97% coverage: 5:470/478 of query aligns to 1:458/465 of 3urhB
- active site: Y35 (≠ L47), C39 (= C51), C44 (= C56), S47 (= S59), V183 (= V196), E187 (= E200), H443 (= H455), H445 (= H457), E450 (= E462)
- binding flavin-adenine dinucleotide: I6 (= I10), G7 (= G11), G9 (= G13), P10 (= P14), G11 (= G15), E30 (= E34), K31 (≠ D43), G37 (= G49), T38 (= T50), C39 (= C51), G43 (= G55), C44 (= C56), K48 (= K60), T111 (≠ Y123), G112 (= G124), A140 (= A155), T141 (= T156), G142 (= G157), I184 (= I197), R273 (= R285), G312 (= G324), D313 (= D325), M319 (= M331), L320 (= L332), A321 (= A333), H322 (= H334)
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: 2:478/478 of query aligns to 35:501/501 of P31023
- 67:76 (vs. 34:51, 33% identical) binding
- C76 (= C51) modified: Disulfide link with 81, Redox-active
- C81 (= C56) modified: Disulfide link with 76, Redox-active
- G149 (= G124) binding
- D348 (= D325) binding
- MLAH 354:357 (= MLAH 331:334) 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: 2:478/478 of query aligns to 1:467/467 of 1dxlA
- active site: L38 (= L47), C42 (= C51), C47 (= C56), S50 (= S59), Y184 (≠ V196), E188 (= E200), H444 (= H455), H446 (= H457), E451 (= E462)
- binding flavin-adenine dinucleotide: I9 (= I10), P13 (= P14), G14 (= G15), E33 (= E34), K34 (≠ G35), R35 (≠ N36), G40 (= G49), T41 (= T50), C42 (= C51), G46 (= G55), C47 (= C56), K51 (= K60), Y114 (= Y123), G115 (= G124), T144 (= T156), G145 (= G157), Y184 (≠ V196), I185 (= I197), R274 (= R285), D314 (= D325), M320 (= M331), L321 (= L332), A322 (= A333), H323 (= H334)
1zmdA Crystal structure of human dihydrolipoamide dehydrogenase complexed to nadh (see paper)
48% identity, 97% coverage: 6:470/478 of query aligns to 6:463/472 of 1zmdA
- active site: L39 (= L47), C43 (= C51), C48 (= C56), S51 (= S59), V186 (= V196), E190 (= E200), H448 (= H455), H450 (= H457), E455 (= E462)
- binding flavin-adenine dinucleotide: I10 (= I10), G11 (= G11), G13 (= G13), P14 (= P14), G15 (= G15), E34 (= E34), K35 (≠ G35), N36 (= N36), G41 (= G49), T42 (= T50), C43 (= C51), G47 (= G55), C48 (= C56), K52 (= K60), Y116 (= Y123), G117 (= G124), T146 (= T156), G147 (= G157), S166 (≠ N176), R278 (= R285), F281 (≠ N288), G317 (= G324), D318 (= D325), M324 (= M331), L325 (= L332), A326 (= A333), H327 (= H334)
- binding 1,4-dihydronicotinamide adenine dinucleotide: I182 (= I192), G183 (= G193), G185 (= G195), V186 (= V196), I187 (= I197), E190 (= E200), E206 (= E216), F207 (≠ A217), L208 (= L218), I276 (≠ V283), G277 (= G284), R278 (= R285), M324 (= M331), L325 (= L332), V355 (= V362), Y357 (= Y364)
1zmcA Crystal structure of human dihydrolipoamide dehydrogenase complexed to NAD+ (see paper)
48% identity, 97% coverage: 6:470/478 of query aligns to 6:463/472 of 1zmcA
- active site: L39 (= L47), C43 (= C51), C48 (= C56), S51 (= S59), V186 (= V196), E190 (= E200), H448 (= H455), H450 (= H457), E455 (= E462)
- binding flavin-adenine dinucleotide: I10 (= I10), G11 (= G11), G13 (= G13), P14 (= P14), G15 (= G15), E34 (= E34), K35 (≠ G35), N36 (= N36), G41 (= G49), T42 (= T50), C43 (= C51), G47 (= G55), C48 (= C56), K52 (= K60), Y116 (= Y123), G117 (= G124), T146 (= T156), G147 (= G157), S166 (≠ N176), I187 (= I197), F281 (≠ N288), G317 (= G324), D318 (= D325), M324 (= M331), L325 (= L332), A326 (= A333), H327 (= H334)
- binding nicotinamide-adenine-dinucleotide: G183 (= G193), G185 (= G195), V205 (≠ L215), E206 (= E216), F207 (≠ A217), L208 (= L218), K240 (= K249), V241 (= V250), I276 (≠ V283), G277 (= G284), R278 (= R285), R297 (= R304), M324 (= M331)
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: 6:470/478 of query aligns to 43:500/509 of P09622
- 71:80 (vs. 34:51, 39% identical) binding
- K72 (≠ G35) to E: in DLDD; reduced dihydrolipoyl dehydrogenase activity; no effect on interaction with PDHX; dbSNP:rs121964987
- K89 (= K60) binding ; mutation to E: Abolishes dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- K104 (≠ H74) to T: in dbSNP:rs1130477
- G154 (= G124) binding
- TGS 183:185 (= TGS 156:158) binding
- 220:227 (vs. 193:200, 88% identical) binding
- E243 (= E216) binding
- V278 (= V250) binding
- G314 (= G284) binding
- D355 (= D325) binding
- MLAH 361:364 (= MLAH 331:334) binding
- E375 (= E345) to K: in DLDD; loss of enzyme activity; abolished interaction with PDHX; dbSNP:rs121964992
- H383 (= H353) mutation to A: Reduces dihydrolipoyl dehydrogenase activity.; mutation to L: Reduces dihydrolipoyl dehydrogenase activity.
- D448 (= D418) 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 (= E436) mutation to A: Decreases dehydrogenase activity. Loss of proteolytic activity.
- Y473 (≠ F443) 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 (= D449) to V: in DLDD; reduced dehydrogenase activity; increased proteolytic activity; dbSNP:rs397514649
- R482 (= R452) 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 (= H455) mutation to A: Loss of dehydrogenase activity. Increases proteolytic activity.
- P488 (= P458) to L: in DLDD; no effect on interaction with PDHX; dbSNP:rs121964988
- S491 (= S461) mutation to A: Loss of proteolytic activity. Does not affect dehydrogenase activity.
- E492 (= E462) mutation to Q: Reduces dihydrolipoyl dehydrogenase activity. Does not affect interaction with PDHX.
- R495 (= R465) 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.
6hg8B Crystal structure of the r460g disease-causing mutant of the human dihydrolipoamide dehydrogenase.
48% identity, 97% coverage: 6:470/478 of query aligns to 16:473/482 of 6hg8B
- active site: C53 (= C51), C58 (= C56), S61 (= S59), V196 (= V196), E200 (= E200), H460 (= H457), E465 (= E462)
- binding flavin-adenine dinucleotide: I20 (= I10), G23 (= G13), P24 (= P14), G25 (= G15), E44 (= E34), K45 (≠ G35), N46 (= N36), G51 (= G49), T52 (= T50), C53 (= C51), G57 (= G55), C58 (= C56), K62 (= K60), Y126 (= Y123), G127 (= G124), T156 (= T156), G157 (= G157), I197 (= I197), R288 (= R285), F291 (≠ N288), G327 (= G324), D328 (= D325), M334 (= M331), L335 (= L332), A336 (= A333), H337 (= H334)
2yquB Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
47% identity, 99% coverage: 5:478/478 of query aligns to 2:455/455 of 2yquB
- active site: P11 (= P14), L36 (= L47), C40 (= C51), C45 (= C56), S48 (= S59), G72 (≠ D85), V73 (= V86), V177 (= V196), E181 (= E200), S314 (≠ E337), H432 (= H455), H434 (= H457), E439 (= E462)
- binding carbonate ion: A310 (= A333), S314 (≠ E337), S423 (≠ A446), D426 (= D449)
- binding flavin-adenine dinucleotide: G8 (= G11), G10 (= G13), P11 (= P14), G12 (= G15), E31 (= E34), K32 (≠ D43), G38 (= G49), T39 (= T50), C40 (= C51), R42 (≠ N53), G44 (= G55), C45 (= C56), K49 (= K60), T110 (≠ Y123), A111 (≠ G124), T137 (= T156), G138 (= G157), I178 (= I197), Y265 (≠ N288), G301 (= G324), D302 (= D325), M308 (= M331), L309 (= L332), A310 (= A333), H311 (= H334)
2yquA Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(e3s) from thermus thermophilus
47% identity, 99% coverage: 5:478/478 of query aligns to 2:455/455 of 2yquA
- active site: P11 (= P14), L36 (= L47), C40 (= C51), C45 (= C56), S48 (= S59), G72 (≠ D85), V73 (= V86), V177 (= V196), E181 (= E200), S314 (≠ E337), H432 (= H455), H434 (= H457), E439 (= E462)
- binding flavin-adenine dinucleotide: G8 (= G11), G10 (= G13), P11 (= P14), G12 (= G15), E31 (= E34), K32 (≠ D43), G38 (= G49), T39 (= T50), C40 (= C51), R42 (≠ N53), G44 (= G55), C45 (= C56), K49 (= K60), T110 (≠ Y123), A111 (≠ G124), T137 (= T156), G138 (= G157), S157 (≠ N176), I178 (= I197), Y265 (≠ N288), G301 (= G324), D302 (= D325), M308 (= M331), L309 (= L332), A310 (= A333)
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)
47% identity, 98% coverage: 1:470/478 of query aligns to 23:491/499 of P09624
- 56:65 (vs. 34:51, 33% identical) binding
- C65 (= C51) modified: Disulfide link with 70, Redox-active
- C70 (= C56) modified: Disulfide link with 65, Redox-active
- K74 (= K60) binding
- G139 (= G124) binding
- D346 (= D325) binding
- MLAH 352:355 (= MLAH 331:334) binding
- H478 (= H457) active site, Proton acceptor
Sites not aligning to the query:
- 1:21 modified: transit peptide, Mitochondrion
Query Sequence
>RR42_RS12930 FitnessBrowser__Cup4G11:RR42_RS12930
MSKQFDVLVIGAGPGGYIAAIRAGQLGLNVACCEGNAYDDPKDEPRLGGTCLNVGCIPSK
ALLASSEEFENVQHHLGDHGITVGDVKVDVAKMLKRKDDIVGKMTKGIEFLFRKNKVTLL
KGYGKFVGKTAEGFQVEIAGKAGTEVVTAKQVIVATGSKARHLPGIAVDNVLVSDNEGAL
KFAGVPKKLGVIGAGVIGLELGSVWRRLGAEVTVLEALPSFLGAADEGVAKEAQKLLTKQ
GLKFSLGVKVNEVKTGKDNVTVSYTDKDGAAQTLEVDRLIVSVGRVPNTDNLGLDAIGLA
ADQRGFIEVDDHCATSVPGLWAIGDVVRGPMLAHKAEDEGVAVAERIAGQKPHIDYNCIP
WVIYTFPEIAWVGKTEQQLKAEGREYKSGQFPFMANGRALGMGHSEGFVKMLADAKTDEI
LGVHVVAANASDLIAEAVVAMEFKAASEDIGRTCHPHPSMSEVMREAALAVDKRQLNM
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