SitesBLAST
Comparing 207299 MicrobesOnline__882:207299 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)
A0A0H3JRU9 Pyruvate carboxylase; EC 6.4.1.1 from Staphylococcus aureus (strain Mu50 / ATCC 700699) (see 2 papers)
32% identity, 94% coverage: 16:1177/1234 of query aligns to 5:1128/1150 of A0A0H3JRU9
- R21 (= R32) mutation to A: Complete loss of catalytic activity.
- K119 (= K128) binding
- K161 (= K169) binding
- H211 (= H219) binding
- E278 (= E288) binding
- K411 (≠ I415) mutation to A: Complete loss of catalytic activity.
- RDAHQ 541:545 (≠ RDITQ 549:553) binding
- D542 (= D550) binding
- A580 (= A586) mutation to T: Complete loss of catalytic activity.
- R614 (= R620) mutation to A: Complete loss of catalytic activity.
- Y621 (= Y627) mutation to A: Complete loss of catalytic activity.
- K712 (= K724) binding
- H741 (= H754) binding
- H743 (= H756) binding
- Q838 (≠ A853) mutation to A: About 2.5-fold loss of catalytic activity.
- T876 (= T890) mutation to A: Complete loss of catalytic activity.
- S879 (= S893) mutation to A: About 2-fold loss of catalytic activity.
- K880 (≠ Q894) mutation to T: Complete loss of catalytic activity.
3bg5A Crystal structure of staphylococcus aureus pyruvate carboxylase (see paper)
31% identity, 94% coverage: 16:1177/1234 of query aligns to 3:1119/1137 of 3bg5A
- active site: K117 (= K128), K159 (= K169), S189 (≠ P206), H202 (= H219), R228 (≠ N245), T267 (= T286), E269 (= E288), E281 (= E301), N283 (= N303), R285 (= R305), E289 (= E309), R337 (= R351), D533 (= D550), D639 (= D653), K703 (= K724), H732 (= H754), H734 (= H756), I755 (≠ V777), S761 (≠ A783), M762 (≠ S784), T801 (≠ Q824), T867 (= T890), S869 (≠ G892), V881 (= V904), N883 (≠ G906), Q888 (≠ G911)
- binding adenosine-5'-triphosphate: K117 (= K128), M157 (= M167), K159 (= K169), Y196 (= Y213), I197 (≠ L214), H202 (= H219), Q226 (= Q243), H229 (= H246), E269 (= E288), L271 (= L290), E281 (= E301), N283 (= N303)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: Y463 (≠ L476), G471 (= G484), F472 (= F485), P473 (= P487), F579 (≠ A594)
- binding manganese (ii) ion: D533 (= D550), H732 (= H754), H734 (= H756)
- binding pyruvic acid: L603 (= L618), K703 (= K724)
7wtbB Cryo-em structure of human pyruvate carboxylase with acetyl-coa (see paper)
32% identity, 95% coverage: 16:1182/1234 of query aligns to 7:1134/1147 of 7wtbB
- binding acetyl coenzyme *a: F22 (≠ C31), T26 (≠ R35), R46 (≠ P54), Q47 (≠ A55), K48 (≠ A56), A49 (≠ S57), D50 (≠ A58), R367 (≠ V372), R414 (= R418), E418 (= E422), R420 (≠ I424), R422 (≠ G426), A462 (≠ E469), Q463 (≠ G470), R465 (= R472), K1025 (= K1072)
- binding phosphoaminophosphonic acid-adenylate ester: K163 (= K169), G168 (= G174), G169 (= G175), M173 (≠ I179), F207 (≠ Y213), I208 (≠ L214), P211 (≠ V217), H240 (= H246)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: D582 (≠ H589), Q839 (≠ A853), T877 (= T890), S880 (= S893), K881 (≠ Q894)
7wtdC Cryo-em structure of human pyruvate carboxylase with acetyl-coa in the intermediate state 1 (see paper)
32% identity, 95% coverage: 16:1182/1234 of query aligns to 6:1133/1146 of 7wtdC
- binding adenosine-5'-triphosphate: K162 (= K169), G167 (= G174), G168 (= G175), F206 (≠ Y213), Q236 (= Q243), H239 (= H246), E292 (= E301)
- binding coenzyme a: F21 (≠ C31), R22 (= R32), T25 (≠ R35), R45 (≠ P54), Q46 (≠ A55), K47 (≠ A56), A48 (≠ S57), D49 (≠ A58), E50 (≠ A59), R366 (≠ V372), R413 (= R418), A416 (≠ S421), R419 (≠ I424), Q462 (≠ G470), R464 (= R472), A465 (≠ L473), Q466 (≠ A474), K1024 (= K1072), R1053 (≠ M1101)
P11498 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Homo sapiens (Human) (see 6 papers)
32% identity, 95% coverage: 16:1182/1234 of query aligns to 38:1165/1178 of P11498
- V145 (≠ A121) to A: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs28940591
- R156 (= R132) to Q: in PC deficiency; dbSNP:rs119103241
- R270 (≠ N245) to W: in PC deficiency; dbSNP:rs1258494752
- Y304 (= Y281) to C: in PC deficiency
- R451 (≠ I424) to C: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs113994143
- D572 (= D550) binding
- R583 (= R561) to L: in PC deficiency; dbSNP:rs119103242
- A610 (= A586) to T: in PC deficiency; mild; dbSNP:rs28940589
- R631 (≠ N607) to Q: in PC deficiency; dbSNP:rs113994145
- K741 (= K724) binding via carbamate group; modified: N6-carboxylysine
- M743 (= M726) to I: in PC deficiency; mild; dbSNP:rs28940590
- H771 (= H754) binding
- H773 (= H756) binding
- F1077 (≠ R1093) mutation F->A,E: Loss of tetramerization and enzyme activity, resulting in an inactive homodimer.
- VAK 1131:1133 (≠ VKK 1148:1150) natural variant: Missing (in PC deficiency)
- K1144 (= K1161) modified: N6-biotinyllysine
Q05920 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Mus musculus (Mouse) (see paper)
31% identity, 95% coverage: 16:1182/1234 of query aligns to 38:1165/1178 of Q05920
- K39 (≠ A17) modified: N6-acetyllysine
- K79 (≠ A56) modified: N6-acetyllysine; alternate; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K148 (≠ L124) modified: N6-acetyllysine
- K152 (= K128) modified: N6-acetyllysine; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K241 (≠ S216) modified: N6-acetyllysine
- K434 (≠ Q407) modified: N6-acetyllysine
- K589 (≠ L567) modified: N6-acetyllysine
- K717 (≠ G687) modified: N6-acetyllysine
- K748 (≠ P731) modified: N6-acetyllysine; mutation to Q: Reduced pyruvate carboxylase activity.
- K892 (= K875) modified: N6-acetyllysine
- K969 (≠ N980) modified: N6-acetyllysine
Sites not aligning to the query:
- 35 modified: N6-acetyllysine
3hb9A Crystal structure of s. Aureus pyruvate carboxylase a610t mutant (see paper)
31% identity, 94% coverage: 16:1177/1234 of query aligns to 3:1115/1133 of 3hb9A
- active site: K117 (= K128), K159 (= K169), H198 (= H219), R224 (≠ N245), T263 (= T286), E265 (= E288), E277 (= E301), N279 (= N303), R281 (= R305), E285 (= E309), R333 (= R351), D529 (= D550), D635 (= D653), K699 (= K724), H728 (= H754), H730 (= H756), I751 (≠ V777), S757 (≠ A783), M758 (≠ S784), T797 (≠ Q824), T863 (= T890), S865 (≠ G892), V877 (= V904), N879 (≠ G906), Q884 (≠ G911)
- binding adenosine-5'-diphosphate: K117 (= K128), M157 (= M167), Y192 (= Y213), I193 (≠ L214), H198 (= H219), Q222 (= Q243), H225 (= H246), L267 (= L290), I276 (= I300), E277 (= E301)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: Y459 (≠ L476), N462 (≠ E479), G467 (= G484), F468 (= F485), F575 (≠ A594), K577 (≠ M596)
- binding manganese (ii) ion: D529 (= D550), H728 (= H754), H730 (= H756)
7zz3A Cryo-em structure of "bc react" conformation of lactococcus lactis pyruvate carboxylase with acetyl-coa (see paper)
31% identity, 94% coverage: 16:1174/1234 of query aligns to 3:1117/1138 of 7zz3A
- binding acetyl coenzyme *a: N22 (≠ R35), F43 (≠ S57), K44 (≠ A58), A45 (= A59), D46 (≠ Q60), S48 (≠ L62), R363 (≠ V372), H413 (≠ S421), E414 (= E422), R416 (≠ I424), R418 (≠ G426), R459 (≠ A467), R461 (≠ E469), K1016 (= K1072), T1017 (≠ P1073), L1018 (≠ H1074), R1045 (vs. gap)
- binding adenosine-5'-triphosphate: K117 (= K128), M156 (= M167), K158 (= K169), G163 (= G174), G164 (= G175), G165 (= G176), M168 (≠ I179), E200 (= E211), Y202 (= Y213), I203 (≠ L214), H208 (= H219), Q232 (= Q243), N235 (≠ H246), L277 (= L290), E287 (= E301), N289 (= N303), T443 (= T451)
- binding bicarbonate ion: K237 (= K248), R291 (= R305), Q293 (= Q307), E295 (= E309)
- binding biotin: G84 (= G95), V294 (= V308), R342 (= R351), K1104 (= K1161)
- binding magnesium ion: E275 (= E288), E287 (= E301), V520 (≠ L535), T523 (≠ A538), D754 (≠ H775)
- binding manganese (ii) ion: D535 (= D550), K704 (= K724), H733 (= H754), H735 (= H756)
- binding pyruvic acid: R534 (= R549), Q538 (= Q553), L605 (= L618), K704 (= K724), T868 (= T890)
5vyzA Crystal structure of lactococcus lactis pyruvate carboxylase in complex with cyclic-di-amp (see paper)
31% identity, 94% coverage: 16:1174/1234 of query aligns to 9:1123/1144 of 5vyzA
- binding (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide: Q719 (≠ R733), Y722 (≠ T736), S752 (≠ G767), G753 (≠ A768), Q756 (≠ K771)
- binding adenosine-5'-diphosphate: K123 (= K128), M162 (= M167), K164 (= K169), G168 (= G173), G170 (= G175), G171 (= G176), M174 (≠ I179), Y208 (= Y213), I209 (≠ L214), H214 (= H219), Q238 (= Q243), N241 (≠ H246), L283 (= L290), E293 (= E301), T449 (= T451)
- binding magnesium ion: E281 (= E288), E293 (= E301)
- binding manganese (ii) ion: D541 (= D550), K710 (= K724), H739 (= H754), H741 (= H756)
P11154 Pyruvate carboxylase 1; Pyruvic carboxylase 1; PCB 1; EC 6.4.1.1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
30% identity, 96% coverage: 18:1200/1234 of query aligns to 22:1175/1178 of P11154
- K1135 (= K1161) modified: N6-biotinyllysine
7zyyA Cryo-em structure of lactococcus lactis pyruvate carboxylase with acetyl-coa (see paper)
31% identity, 88% coverage: 16:1099/1234 of query aligns to 3:1043/1056 of 7zyyA
- binding acetyl coenzyme *a: R19 (= R32), N22 (≠ R35), F43 (≠ S57), K44 (≠ A58), A45 (= A59), R363 (≠ V372), E414 (= E422), R416 (≠ I424), R418 (≠ G426), R459 (≠ A467), D460 (≠ P468), R461 (≠ E469), K1016 (= K1072), T1017 (≠ P1073), L1018 (≠ H1074), N1041 (≠ D1097)
- binding adenosine-5'-diphosphate: K158 (= K169), G163 (= G174), G164 (= G175), M168 (≠ I179), E200 (= E211), K201 (= K212), Y202 (= Y213), I203 (≠ L214), H208 (= H219), Q232 (= Q243), N235 (≠ H246), E275 (= E288), L277 (= L290), E287 (= E301), T443 (= T451)
- binding bicarbonate ion: R291 (= R305), Q293 (= Q307), V294 (= V308), E295 (= E309)
- binding magnesium ion: E275 (= E288), E287 (= E301), V520 (≠ L535), T523 (≠ A538), D754 (≠ H775)
- binding manganese (ii) ion: D535 (= D550), K704 (= K724), H733 (= H754), H735 (= H756)
- binding pyruvic acid: Q538 (= Q553), G572 (= G585), L605 (= L618), R607 (= R620), K704 (= K724), T868 (= T890)
Sites not aligning to the query:
8gk8A R21a staphylococcus aureus pyruvate carboxylase
31% identity, 88% coverage: 16:1099/1234 of query aligns to 3:1028/1041 of 8gk8A
- binding acetyl coenzyme *a: E400 (= E422), R402 (≠ I424), R404 (≠ G426), L445 (≠ A467), R447 (≠ E469), N1026 (≠ D1097)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: N457 (≠ E479), G462 (= G484), F463 (= F485), P464 (= P487), F570 (≠ A594), K572 (≠ M596)
- binding coenzyme a: R42 (≠ A56), Y43 (≠ S57), A45 (= A59), D46 (≠ Q60), E47 (= E61), S48 (≠ L62)
- binding manganese (ii) ion: D524 (= D550), K694 (= K724), H723 (= H754), H725 (= H756)
Sites not aligning to the query:
3tw6B Structure of rhizobium etli pyruvate carboxylase t882a with the allosteric activator, acetyl coenzyme-a (see paper)
30% identity, 95% coverage: 18:1190/1234 of query aligns to 6:1129/1129 of 3tw6B
- active site: K124 (= K128), K162 (= K169), H212 (= H219), R238 (≠ N245), T277 (= T286), E279 (= E288), E293 (= E301), N295 (= N303), R297 (= R305), E301 (= E309), R349 (= R351), D544 (= D550), D650 (= D653), K713 (= K724), H742 (= H754), H744 (= H756), A877 (≠ T890)
- binding adenosine-5'-diphosphate: K124 (= K128), K162 (= K169), G167 (= G174), G169 (= G176), M172 (≠ I179), E204 (= E211), L206 (≠ Y213), V207 (≠ L214), H212 (= H219), Q236 (= Q243), N239 (≠ H246), L281 (= L290), E293 (= E301), T450 (= T451)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: R349 (= R351), D395 (= D396), K1102 (= K1161)
- binding magnesium ion: E279 (= E288), E293 (= E301), M529 (≠ L535), R530 (= R536), E532 (≠ A538), D763 (≠ H775)
- binding zinc ion: D544 (= D550), K713 (= K724), H742 (= H754), H744 (= H756)
3tw6C Structure of rhizobium etli pyruvate carboxylase t882a with the allosteric activator, acetyl coenzyme-a (see paper)
30% identity, 88% coverage: 18:1099/1234 of query aligns to 6:1036/1044 of 3tw6C
- active site: K124 (= K128), K166 (= K169), H200 (= H219), R226 (≠ N245), T265 (= T286), E267 (= E288), E281 (= E301), N283 (= N303), R285 (= R305), E289 (= E309), R337 (= R351), D528 (= D550), D634 (= D653), K697 (= K724), H726 (= H754), H728 (= H756), A861 (≠ T890)
- binding adenosine-5'-diphosphate: K166 (= K169), M169 (≠ I179), V195 (≠ L214), H200 (= H219), Q224 (= Q243), E281 (= E301), T438 (= T451)
- binding coenzyme a: R411 (≠ I424), R413 (≠ G426), R453 (≠ L466), Q454 (≠ A467), D455 (≠ P468), R456 (≠ E469), L1011 (≠ H1074)
- binding magnesium ion: E267 (= E288), E281 (= E301)
- binding phosphonoacetic acid: K229 (= K248), R285 (= R305), Q287 (= Q307), V288 (= V308), E289 (= E309)
- binding zinc ion: D528 (= D550), K697 (= K724), H726 (= H754), H728 (= H756)
8hz4A The tetrameric structure of biotin carboxylase from chloroflexus aurantiacus in complex with bicarbonate
46% identity, 36% coverage: 16:461/1234 of query aligns to 3:444/456 of 8hz4A
7kctA Crystal structure of the hydrogenobacter thermophilus 2-oxoglutarate carboxylase (ogc) biotin carboxylase (bc) domain dimer in complex with adenosine 5'-diphosphate magnesium salt (mgadp), adenosine 5'- diphosphate (adp, and bicarbonate anion (hydrogen carbonate/hco3-) (see paper)
41% identity, 36% coverage: 16:465/1234 of query aligns to 5:453/453 of 7kctA
- active site: E276 (= E288), E289 (= E301), N291 (= N303), E297 (= E309), R339 (= R351)
- binding adenosine-5'-diphosphate: K117 (= K128), L157 (≠ M167), K159 (= K169), G164 (= G174), G165 (= G175), G166 (= G176), I169 (= I179), E201 (= E211), Y203 (= Y213), I204 (≠ L214), H209 (= H219), Q233 (= Q243), Q237 (= Q247), K238 (= K248), I278 (≠ L290), E289 (= E301), R293 (= R305), Q295 (= Q307), V296 (= V308), E297 (= E309), R339 (= R351)
- binding bicarbonate ion: D116 (≠ N127), R119 (≠ Q130)
- binding magnesium ion: E276 (= E288), E289 (= E301)
4mv4A Crystal structure of biotin carboxylase from haemophilus influenzae in complex with amppcp and mg2 (see paper)
43% identity, 35% coverage: 18:454/1234 of query aligns to 5:437/442 of 4mv4A
- active site: K116 (= K128), K159 (= K169), D193 (≠ P206), H206 (= H219), R232 (≠ N245), T271 (= T286), E273 (= E288), E285 (= E301), N287 (= N303), R289 (= R305), E293 (= E309), R335 (= R351)
- binding phosphomethylphosphonic acid adenylate ester: K159 (= K169), G164 (= G174), M166 (≠ G176), E198 (= E211), Y200 (= Y213), L201 (= L214), H233 (= H246), L275 (= L290), E285 (= E301)
- binding magnesium ion: E273 (= E288), E285 (= E301)
6oi8A Crystal structure of haemophilus influenzae biotin carboxylase complexed with 7-((1r,5s,6s)-6-amino-3-azabicyclo[3.1.0]hexan-3-yl)- 6-(2-chloro-6-(pyridin-3-yl)phenyl)pyrido[2,3-d]pyrimidin-2-amine (see paper)
42% identity, 35% coverage: 18:454/1234 of query aligns to 5:435/440 of 6oi8A
- active site: K116 (= K128), K159 (= K169), D191 (≠ P206), H204 (= H219), R230 (≠ N245), T269 (= T286), E271 (= E288), E283 (= E301), N285 (= N303), R287 (= R305), E291 (= E309), R333 (= R351)
- binding 7-[(1R,5S,6s)-6-amino-3-azabicyclo[3.1.0]hexan-3-yl]-6-[2-chloro-6-(pyridin-3-yl)phenyl]pyrido[2,3-d]pyrimidin-2-amine: I157 (≠ M167), K159 (= K169), M164 (≠ I179), E196 (= E211), Y198 (= Y213), L199 (= L214), H204 (= H219), Q228 (= Q243), E271 (= E288), L273 (= L290), E283 (= E301), I432 (≠ T451)
P43873 Biotin carboxylase; Acetyl-coenzyme A carboxylase biotin carboxylase subunit A; EC 6.3.4.14 from Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) (see paper)
43% identity, 35% coverage: 18:454/1234 of query aligns to 5:440/448 of P43873
- K116 (= K128) binding
- K159 (= K169) binding
- EKYL 201:204 (= EKYL 211:214) binding
- E276 (= E288) binding ; binding
- E288 (= E301) binding ; binding
- N290 (= N303) binding
6ojhA Crystal structure of haemophilus influenzae biotin carboxylase complexed with (r)-7-(3-aminopyrrolidin-1-yl)-6-(naphthalen-1-yl) pyrido[2,3-d]pyrimidin-2-amine
43% identity, 35% coverage: 18:454/1234 of query aligns to 5:440/445 of 6ojhA
- active site: K116 (= K128), K159 (= K169), D196 (≠ P206), H209 (= H219), R235 (≠ N245), T274 (= T286), E276 (= E288), E288 (= E301), N290 (= N303), R292 (= R305), E296 (= E309), R338 (= R351)
- binding calcium ion: E276 (= E288), E288 (= E301), N290 (= N303)
- binding 7-[(3R)-3-aminopyrrolidin-1-yl]-6-(naphthalen-1-yl)pyrido[2,3-d]pyrimidin-2-amine: K159 (= K169), M169 (≠ I179), E201 (= E211), Y203 (= Y213), L204 (= L214), H236 (= H246), L278 (= L290), E288 (= E301), I437 (≠ T451)
Query Sequence
>207299 MicrobesOnline__882:207299
MAIKTFEQVMEEVRGKAILVANRGIPARRICRSIRERFDAVAVMTATDVDKTSPAASAAQ
ELLLLGADPRAYLDIDRIISLAKQRGVVAIHPGWGFASEDDRFPSKCHEAGLTFIGSTAE
AMNLLGNKVQVRKLARKLGVPVVPGSEGAVDIPTARKLIDEIGLPIMLKAEGGGGGRGIF
AIRDESELDDAFFKASTMAQASFGNPRLFVEKYLESVRHIEIQVIADMYGNAFAFDERDC
SIQRNHQKLIEITPSPWPGITPELREKLKEYSKMLVREVGYHSLATVEFLVTASGEAYLI
EVNTRLQVEHGITECRYGIDLVEEQIAVAFGAQLRLTEENTKPVHHAMQVRINCEDPQAG
FSPNSGLVSRYVSPGGPGVRLDSNMCAGYEFPPNYDSAGSLLITYGQGWQKVLGIMERCL
SEYIIGGLKTTIPFYKQVMKHPRFRAGDFDTNFIAETPELMCYTDLAPEGERLARLVAEI
SAKGFNPYVQLGEYRTRETPRMPKFEPVLPHIPGQVRRNPSPYPHGDRGALLDYLRDAGH
VHFTDTTARDITQSNSGNRFRLAEDALMGPYLDNCNFFSLENGGGAHFHVAMMANMTYPF
SEAAEWNKFAPKTLKQILIRSTNVLGYKPQPRNLMRITGEMICEHYQVIRCFDFLNHVEN
MRPFAEVALNRNDVVFEPALSLSWARGFDVAHYVGVTEAILRMVGDVAGFGPEQASRSII
LGLKDMAGVCPPRFMTELVSTLRKRWPSLVLHCHRHYTDGLFVPAVGAAAKAGAHIVDTA
IGASVRWYGQGDVLSMAAYLEDELGLRTNLNKTMIRDCNFVLKQVMPFYDRYCAPYFQGI
DYDVVEHGMPGGATSSSQAGAMKQGYIHLLPYMLKFLAGTRKIVRYHDVTPGSQITWNTA
FLAVTGAHKRGGEDEVRYLLEVLDNVTRHPESDLSEDMKKARLAIYQDCNDAFRDLLLGK
FGRLPLGFPDEWVYRSAFGNEWRKAMASRTEASPLDSLAPVDLALEERGFIDIVRRKPTE
EEFVMYLNHPGDAIKTIQFKARFGNANNLPLDVWFEGLQPGEELNFTDSSGKPHHLVILS
ISRPNDAGYSVIRYVLDSEIMSCEAQVKQSSVADIKGVEMADRANPMHVAAPSNGDLWVM
YVHPGDVVKKGEELFNVSIMKQEKAVLAPMDAMVKRVLKTADYRESKQMVAVREGELVVE
LCPIPKMCPNHACGHPITLDGIDFCPYCGERLDA
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