SitesBLAST
Comparing GFF926 PGA1_c09420 pyruvate carboxylase Pyc 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)
3tw6B Structure of rhizobium etli pyruvate carboxylase t882a with the allosteric activator, acetyl coenzyme-a (see paper)
64% identity, 96% coverage: 46:1184/1188 of query aligns to 3:1129/1129 of 3tw6B
- active site: K124 (= K161), K162 (= K203), H212 (= H253), R238 (= R279), T277 (= T318), E279 (= E320), E293 (= E334), N295 (= N336), R297 (= R338), E301 (= E342), R349 (= R389), D544 (= D585), D650 (= D690), K713 (= K753), H742 (= H782), H744 (= H784), A877 (≠ T917)
- binding adenosine-5'-diphosphate: K124 (= K161), K162 (= K203), G167 (= G208), G169 (= G210), M172 (= M213), E204 (= E245), L206 (≠ M247), V207 (≠ I248), H212 (= H253), Q236 (= Q277), N239 (= N280), L281 (= L322), E293 (= E334), T450 (= T490)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: R349 (= R389), D395 (= D435), K1102 (= K1154)
- binding magnesium ion: E279 (= E320), E293 (= E334), M529 (= M570), R530 (≠ K571), E532 (≠ Q573), D763 (= D803)
- binding zinc ion: D544 (= D585), K713 (= K753), H742 (= H782), H744 (= H784)
3tw6C Structure of rhizobium etli pyruvate carboxylase t882a with the allosteric activator, acetyl coenzyme-a (see paper)
64% identity, 89% coverage: 46:1101/1188 of query aligns to 3:1044/1044 of 3tw6C
- active site: K124 (= K161), K166 (= K203), H200 (= H253), R226 (= R279), T265 (= T318), E267 (= E320), E281 (= E334), N283 (= N336), R285 (= R338), E289 (= E342), R337 (= R389), D528 (= D585), D634 (= D690), K697 (= K753), H726 (= H782), H728 (= H784), A861 (≠ T917)
- binding adenosine-5'-diphosphate: K166 (= K203), M169 (= M213), V195 (≠ I248), H200 (= H253), Q224 (= Q277), E281 (= E334), T438 (= T490)
- binding coenzyme a: R411 (= R463), R413 (= R465), R453 (= R505), Q454 (≠ R506), D455 (= D507), R456 (= R508), L1011 (= L1068)
- binding magnesium ion: E267 (= E320), E281 (= E334)
- binding phosphonoacetic acid: K229 (= K282), R285 (= R338), Q287 (= Q340), V288 (= V341), E289 (= E342)
- binding zinc ion: D528 (= D585), K697 (= K753), H726 (= H782), H728 (= H784)
2qf7A Crystal structure of a complete multifunctional pyruvate carboxylase from rhizobium etli (see paper)
61% identity, 96% coverage: 46:1184/1188 of query aligns to 3:1073/1076 of 2qf7A
- active site: K124 (≠ D185), H147 (= H253), R173 (= R279), T212 (= T318), E214 (= E320), E228 (= E334), N230 (= N336), R232 (= R338), E236 (= E342), R284 (= R389), D479 (= D585), D585 (= D690), K648 (= K753), H677 (= H782), H679 (= H784), T812 (= T917)
- binding phosphothiophosphoric acid-adenylate ester: H147 (= H253), Q171 (= Q277), E214 (= E320), L216 (= L322), E228 (= E334), T385 (= T490)
- binding coenzyme a: R400 (= R505), Q401 (≠ R506), D402 (= D507), R403 (= R508), A404 (≠ G509), I956 (= I1062), K960 (= K1066), L962 (= L1068), N985 (= N1091)
- binding magnesium ion: E214 (= E320), E228 (= E334), M464 (= M570), R465 (≠ K571), E467 (≠ Q573), D698 (= D803)
- binding zinc ion: D479 (= D585), K648 (= K753), H677 (= H782), H679 (= H784)
2qf7B Crystal structure of a complete multifunctional pyruvate carboxylase from rhizobium etli (see paper)
63% identity, 89% coverage: 46:1102/1188 of query aligns to 3:1015/1017 of 2qf7B
- active site: K123 (= K161), K150 (= K203), H169 (= H253), R195 (= R279), T234 (= T318), E236 (= E320), E250 (= E334), N252 (= N336), R254 (= R338), E258 (= E342), R306 (= R389), D498 (= D585), D604 (= D690), K667 (= K753), H696 (= H782), H698 (= H784), T831 (= T917)
- binding phosphothiophosphoric acid-adenylate ester: M148 (= M201), K150 (= K203), M153 (= M213), E161 (= E245), V164 (≠ I248), H169 (= H253), Q193 (= Q277), E236 (= E320), L238 (= L322), I249 (= I333), E250 (= E334), T407 (= T490)
- binding magnesium ion: E236 (= E320), E250 (= E334), M483 (= M570), R484 (≠ K571), E486 (≠ Q573), D717 (= D803)
- binding zinc ion: D498 (= D585), K667 (= K753), H696 (= H782), H698 (= H784)
3tw6A Structure of rhizobium etli pyruvate carboxylase t882a with the allosteric activator, acetyl coenzyme-a (see paper)
61% identity, 89% coverage: 46:1107/1188 of query aligns to 3:1007/1007 of 3tw6A
- active site: K124 (≠ D185), H152 (= H253), R178 (= R279), T217 (= T318), E219 (= E320), E233 (= E334), N235 (= N336), R237 (= R338), E241 (= E342), R289 (= R389), D485 (= D585), D591 (= D690), K654 (= K753), H683 (= H782), H685 (= H784), A818 (≠ T917)
- binding adenosine-5'-diphosphate: L146 (≠ M247), V147 (≠ I248), H152 (= H253), Q176 (= Q277), N179 (= N280), L221 (= L322)
- binding coenzyme a: R365 (= R465), R405 (= R505), Q406 (≠ R506), D407 (= D507), R408 (= R508), T967 (= T1067), L968 (= L1068)
- binding magnesium ion: E219 (= E320), E233 (= E334), M470 (= M570), R471 (≠ K571), E473 (≠ Q573), D704 (= D803)
- binding zinc ion: D485 (= D585), K654 (= K753), H683 (= H782), H685 (= H784)
7zz3A Cryo-em structure of "bc react" conformation of lactococcus lactis pyruvate carboxylase with acetyl-coa (see paper)
53% identity, 96% coverage: 47:1187/1188 of query aligns to 3:1137/1138 of 7zz3A
- binding acetyl coenzyme *a: N22 (= N66), F43 (= F87), K44 (= K88), A45 (= A89), D46 (= D90), S48 (≠ A92), R363 (= R410), H413 (≠ R460), E414 (= E461), R416 (= R463), R418 (= R465), R459 (= R506), R461 (= R508), K1016 (= K1066), T1017 (= T1067), L1018 (= L1068), R1045 (= R1095)
- binding adenosine-5'-triphosphate: K117 (= K161), M156 (= M201), K158 (= K203), G163 (= G208), G164 (= G209), G165 (= G210), M168 (= M213), E200 (= E245), Y202 (≠ M247), I203 (= I248), H208 (= H253), Q232 (= Q277), N235 (= N280), L277 (= L322), E287 (= E334), N289 (= N336), T443 (= T490)
- binding bicarbonate ion: K237 (= K282), R291 (= R338), Q293 (= Q340), E295 (= E342)
- binding biotin: G84 (= G128), V294 (= V341), R342 (= R389), K1104 (= K1154)
- binding magnesium ion: E275 (= E320), E287 (= E334), V520 (≠ M570), T523 (≠ Q573), D754 (= D803)
- binding manganese (ii) ion: D535 (= D585), K704 (= K753), H733 (= H782), H735 (= H784)
- binding pyruvic acid: R534 (= R584), Q538 (= Q588), L605 (= L655), K704 (= K753), T868 (= T917)
5vyzA Crystal structure of lactococcus lactis pyruvate carboxylase in complex with cyclic-di-amp (see paper)
53% identity, 96% coverage: 44:1187/1188 of query aligns to 6:1143/1144 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 (≠ A762), Y722 (≠ R765), S752 (≠ L795), G753 (≠ A796), Q756 (≠ D799)
- binding adenosine-5'-diphosphate: K123 (= K161), M162 (= M201), K164 (= K203), G168 (= G207), G170 (= G209), G171 (= G210), M174 (= M213), Y208 (≠ M247), I209 (= I248), H214 (= H253), Q238 (= Q277), N241 (= N280), L283 (= L322), E293 (= E334), T449 (= T490)
- binding magnesium ion: E281 (= E320), E293 (= E334)
- binding manganese (ii) ion: D541 (= D585), K710 (= K753), H739 (= H782), H741 (= H784)
A0A0H3JRU9 Pyruvate carboxylase; EC 6.4.1.1 from Staphylococcus aureus (strain Mu50 / ATCC 700699) (see 2 papers)
51% identity, 96% coverage: 43:1188/1188 of query aligns to 1:1146/1150 of A0A0H3JRU9
- R21 (= R63) mutation to A: Complete loss of catalytic activity.
- K119 (= K161) binding
- K161 (= K203) binding
- H211 (= H253) binding
- E278 (= E320) binding
- K411 (≠ R454) mutation to A: Complete loss of catalytic activity.
- RDAHQ 541:545 (≠ RDGHQ 584:588) binding
- D542 (= D585) binding
- A580 (= A623) mutation to T: Complete loss of catalytic activity.
- R614 (= R657) mutation to A: Complete loss of catalytic activity.
- Y621 (= Y664) mutation to A: Complete loss of catalytic activity.
- K712 (= K753) binding
- H741 (= H782) binding
- H743 (= H784) binding
- Q838 (= Q879) mutation to A: About 2.5-fold loss of catalytic activity.
- T876 (= T917) mutation to A: Complete loss of catalytic activity.
- S879 (= S920) mutation to A: About 2-fold loss of catalytic activity.
- K880 (= K921) mutation to T: Complete loss of catalytic activity.
3bg5A Crystal structure of staphylococcus aureus pyruvate carboxylase (see paper)
51% identity, 96% coverage: 47:1188/1188 of query aligns to 3:1137/1137 of 3bg5A
- active site: K117 (= K161), K159 (= K203), S189 (≠ G240), H202 (= H253), R228 (= R279), T267 (= T318), E269 (= E320), E281 (= E334), N283 (= N336), R285 (= R338), E289 (= E342), R337 (= R389), D533 (= D585), D639 (= D690), K703 (= K753), H732 (= H782), H734 (= H784), I755 (≠ V805), S761 (≠ A811), M762 (≠ F812), T801 (≠ Q851), T867 (= T917), S869 (= S919), V881 (= V931), N883 (≠ Q933), Q888 (≠ D938)
- binding adenosine-5'-triphosphate: K117 (= K161), M157 (= M201), K159 (= K203), Y196 (≠ M247), I197 (= I248), H202 (= H253), Q226 (= Q277), H229 (≠ N280), E269 (= E320), L271 (= L322), E281 (= E334), N283 (= N336)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: Y463 (= Y515), G471 (= G523), F472 (≠ H524), P473 (= P525), F579 (= F631)
- binding manganese (ii) ion: D533 (= D585), H732 (= H782), H734 (= H784)
- binding pyruvic acid: L603 (= L655), K703 (= K753)
3hb9A Crystal structure of s. Aureus pyruvate carboxylase a610t mutant (see paper)
50% identity, 96% coverage: 47:1188/1188 of query aligns to 3:1133/1133 of 3hb9A
- active site: K117 (= K161), K159 (= K203), H198 (= H253), R224 (= R279), T263 (= T318), E265 (= E320), E277 (= E334), N279 (= N336), R281 (= R338), E285 (= E342), R333 (= R389), D529 (= D585), D635 (= D690), K699 (= K753), H728 (= H782), H730 (= H784), I751 (≠ V805), S757 (≠ A811), M758 (≠ F812), T797 (≠ Q851), T863 (= T917), S865 (= S919), V877 (= V931), N879 (≠ Q933), Q884 (≠ D938)
- binding adenosine-5'-diphosphate: K117 (= K161), M157 (= M201), Y192 (≠ M247), I193 (= I248), H198 (= H253), Q222 (= Q277), H225 (≠ N280), L267 (= L322), I276 (= I333), E277 (= E334)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: Y459 (= Y515), N462 (≠ D518), G467 (= G523), F468 (≠ H524), F575 (= F631), K577 (≠ Q633)
- binding manganese (ii) ion: D529 (= D585), H728 (= H782), H730 (= H784)
7zyyA Cryo-em structure of lactococcus lactis pyruvate carboxylase with acetyl-coa (see paper)
54% identity, 89% coverage: 47:1106/1188 of query aligns to 3:1056/1056 of 7zyyA
- binding acetyl coenzyme *a: R19 (= R63), N22 (= N66), F43 (= F87), K44 (= K88), A45 (= A89), R363 (= R410), E414 (= E461), R416 (= R463), R418 (= R465), R459 (= R506), D460 (= D507), R461 (= R508), K1016 (= K1066), T1017 (= T1067), L1018 (= L1068), N1041 (= N1091), R1045 (= R1095)
- binding adenosine-5'-diphosphate: K158 (= K203), G163 (= G208), G164 (= G209), M168 (= M213), E200 (= E245), K201 (= K246), Y202 (≠ M247), I203 (= I248), H208 (= H253), Q232 (= Q277), N235 (= N280), E275 (= E320), L277 (= L322), E287 (= E334), T443 (= T490)
- binding bicarbonate ion: R291 (= R338), Q293 (= Q340), V294 (= V341), E295 (= E342)
- binding magnesium ion: E275 (= E320), E287 (= E334), V520 (≠ M570), T523 (≠ Q573), D754 (= D803)
- binding manganese (ii) ion: D535 (= D585), K704 (= K753), H733 (= H782), H735 (= H784)
- binding pyruvic acid: Q538 (= Q588), G572 (= G622), L605 (= L655), R607 (= R657), K704 (= K753), T868 (= T917)
5vyzC Crystal structure of lactococcus lactis pyruvate carboxylase in complex with cyclic-di-amp (see paper)
51% identity, 96% coverage: 44:1187/1188 of query aligns to 7:1082/1083 of 5vyzC
- 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: P657 (= P761), Y661 (≠ R765), S691 (≠ L795), Q695 (≠ D799)
- binding adenosine-5'-diphosphate: Y147 (≠ V226), H153 (≠ Y243), Q177 (= Q277), L222 (= L322), E232 (= E334), T388 (= T490)
- binding magnesium ion: E220 (= E320), E232 (= E334)
- binding manganese (ii) ion: D480 (= D585), K649 (= K753), H678 (= H782), H680 (= H784)
7wtdC Cryo-em structure of human pyruvate carboxylase with acetyl-coa in the intermediate state 1 (see paper)
50% identity, 96% coverage: 47:1188/1188 of query aligns to 6:1146/1146 of 7wtdC
- binding adenosine-5'-triphosphate: K162 (= K203), G167 (= G208), G168 (= G209), F206 (≠ M247), Q236 (= Q277), H239 (≠ N280), E292 (= E334)
- binding coenzyme a: F21 (≠ M62), R22 (= R63), T25 (≠ N66), R45 (= R86), Q46 (≠ F87), K47 (= K88), A48 (= A89), D49 (= D90), E50 (= E91), R366 (= R410), R413 (= R457), A416 (≠ R460), R419 (= R463), Q462 (≠ R506), R464 (= R508), A465 (≠ G509), Q466 (≠ T510), K1024 (= K1066), R1053 (= R1095)
7wtbB Cryo-em structure of human pyruvate carboxylase with acetyl-coa (see paper)
50% identity, 96% coverage: 47:1188/1188 of query aligns to 7:1147/1147 of 7wtbB
- binding acetyl coenzyme *a: F22 (≠ M62), T26 (≠ N66), R46 (= R86), Q47 (≠ F87), K48 (= K88), A49 (= A89), D50 (= D90), R367 (= R410), R414 (= R457), E418 (= E461), R420 (= R463), R422 (= R465), A462 (≠ R505), Q463 (≠ R506), R465 (= R508), K1025 (= K1066)
- binding phosphoaminophosphonic acid-adenylate ester: K163 (= K203), G168 (= G208), G169 (= G209), M173 (= M213), F207 (≠ M247), I208 (= I248), P211 (≠ A251), H240 (≠ N280)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: D582 (= D626), Q839 (= Q879), T877 (= T917), S880 (= S920), K881 (= K921)
P11498 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Homo sapiens (Human) (see 6 papers)
50% identity, 96% coverage: 47:1188/1188 of query aligns to 38:1178/1178 of P11498
- V145 (≠ T154) to A: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs28940591
- R156 (= R165) to Q: in PC deficiency; dbSNP:rs119103241
- R270 (= R279) to W: in PC deficiency; dbSNP:rs1258494752
- Y304 (= Y313) to C: in PC deficiency
- R451 (= R463) to C: in PC deficiency; mild; strongly reduced pyruvate carboxylase activity; dbSNP:rs113994143
- D572 (= D585) binding
- R583 (= R596) to L: in PC deficiency; dbSNP:rs119103242
- A610 (= A623) to T: in PC deficiency; mild; dbSNP:rs28940589
- R631 (= R644) to Q: in PC deficiency; dbSNP:rs113994145
- K741 (= K753) binding via carbamate group; modified: N6-carboxylysine
- M743 (= M755) to I: in PC deficiency; mild; dbSNP:rs28940590
- H771 (= H782) binding
- H773 (= H784) binding
- F1077 (= F1087) mutation F->A,E: Loss of tetramerization and enzyme activity, resulting in an inactive homodimer.
- VAK 1131:1133 (≠ VHE 1141:1143) natural variant: Missing (in PC deficiency)
- K1144 (= K1154) modified: N6-biotinyllysine
Q05920 Pyruvate carboxylase, mitochondrial; Pyruvic carboxylase; PCB; EC 6.4.1.1 from Mus musculus (Mouse) (see paper)
50% identity, 96% coverage: 47:1188/1188 of query aligns to 38:1178/1178 of Q05920
- K39 (= K48) modified: N6-acetyllysine
- K79 (= K88) modified: N6-acetyllysine; alternate; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K148 (≠ A157) modified: N6-acetyllysine
- K152 (= K161) modified: N6-acetyllysine; mutation K->Q,R: Reduced pyruvate carboxylase activity.
- K241 (≠ R250) modified: N6-acetyllysine
- K434 (≠ P446) modified: N6-acetyllysine
- K589 (= K602) modified: N6-acetyllysine
- K717 (= K729) modified: N6-acetyllysine
- K748 (= K760) modified: N6-acetyllysine; mutation to Q: Reduced pyruvate carboxylase activity.
- K892 (≠ Q901) modified: N6-acetyllysine
- K969 (= K978) modified: N6-acetyllysine
Sites not aligning to the query:
- 35 modified: N6-acetyllysine
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)
48% identity, 97% coverage: 33:1188/1188 of query aligns to 6:1169/1178 of P11154
- K1135 (= K1154) modified: N6-biotinyllysine
8gk8A R21a staphylococcus aureus pyruvate carboxylase
50% identity, 89% coverage: 47:1103/1188 of query aligns to 3:1038/1041 of 8gk8A
- binding acetyl coenzyme *a: E400 (= E461), R402 (= R463), R404 (= R465), L445 (≠ R506), R447 (= R508), N1026 (= N1091), R1030 (= R1095)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: N457 (≠ D518), G462 (= G523), F463 (≠ H524), P464 (= P525), F570 (= F631), K572 (≠ Q633)
- binding coenzyme a: R42 (= R86), Y43 (≠ F87), A45 (= A89), D46 (= D90), E47 (= E91), S48 (≠ A92)
- binding manganese (ii) ion: D524 (= D585), K694 (= K753), H723 (= H782), H725 (= H784)
4qshC Crystal structure of l. Monocytogenes pyruvate carboxylase in complex with cyclic-di-amp (see paper)
53% identity, 80% coverage: 240:1187/1188 of query aligns to 138:1079/1081 of 4qshC
- active site: K650 (= K753)
- 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: Y662 (≠ R765), Y689 (≠ A792), A693 (= A796), S696 (≠ D799)
- binding manganese (ii) ion: D481 (= D585), H679 (= H782), H681 (= H784)
3bg5B Crystal structure of staphylococcus aureus pyruvate carboxylase (see paper)
51% identity, 79% coverage: 248:1188/1188 of query aligns to 134:1074/1074 of 3bg5B
- active site: H139 (= H253), R165 (= R279), T204 (= T318), E206 (= E320), E218 (= E334), N220 (= N336), R222 (= R338), E226 (= E342), R274 (= R389), D470 (= D585), D576 (= D690), K640 (= K753), H669 (= H782), H671 (= H784), I692 (≠ V805), S698 (≠ A811), M699 (≠ F812), T738 (≠ Q851), T804 (= T917), S806 (= S919), V818 (= V931), N820 (≠ Q933), Q825 (≠ D938)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: N403 (≠ D518), G408 (= G523), F409 (≠ H524), P410 (= P525), F516 (= F631), K518 (≠ Q633)
- binding manganese (ii) ion: D470 (= D585), H669 (= H782), H671 (= H784)
- binding pyruvic acid: Q473 (= Q588), K640 (= K753), T804 (= T917)
Sites not aligning to the query:
Query Sequence
>GFF926 PGA1_c09420 pyruvate carboxylase Pyc
MRILPISGLRSALSRWPYPELRLYRTLICAYHFAKLHDPEDAMTDFKKILIANRGEIAIR
VMRAANEMGKKTVAVYAEEDKLGLHRFKADEAYRIGEGMGPVAAYLSIDEIIRVAKECGA
DAIHPGYGLLSENPDFVDACARNGITFIGPKAETMRALGDKASARRVAIDADVPVIPATE
VLGNDMDAIRKEAAEVGYPLMLKASWGGGGRGMRPIHSEDELEEKVLEGRREAEAAFGNG
EGYLEKMITRARHVEVQILGDKHGEIYHLYERDCSVQRRNQKVVERAPAPYLTEEQRTEI
CDLGRKICQHVNYECAGTVEFLMDMNDGKFYFIEVNPRVQVEHTVTEEVTGIDIVQAQIL
IAEGKTIAEATGKASQDEIQLNGHALQTRVTTEDPLNNFIPDYGRITAYRSATGMGIRLD
GGTAYAGGVITRYYDSLLTKVTAKAPTPEKAIARMDRALREFRVRGVSTNIAFVENLLKH
PTFLSNEYTTKFIDETPELFQFAKRRDRGTKVLTYIADISVNGHPETEGRAAPHTDLKEP
RAPKADAATQPYGTRNLLEQKGAQAVADWMKAQRQLLLTDTTMRDGHQSLLATRMRSHDM
IKVAPAYAQNLSQLFSVECWGGATFDVAYRFLQECPWQRLRDLRERMPNLMTQMLLRASN
GVGYTNYPDNVVQSFVKQAATGVDVFRVFDSLNWVENMRVAMDAVVESGKICEGTICYTG
DILDPNRAKYDLKYYVGMAKELEAAGAHILGLKDMAGLLKPAAARQLVKALKEEVGLPVH
FHTHDTSGVAGATILAAADAGVDAVDAAMDAFSGGTSQPCLGSIVEALRNTDRDTGIDIA
AVREISGYWEQVRAHYVAFESGLAAPASEVYLHEMPGGQFTNLKAQARSLGLEEKWSDVA
QTYADVNQMFGDIVKVTPSSKVVGDMALMMVSQGLTRDDVEDPKSDVAFPDSVVDMMRGN
LGQPPGGFPEAIVSKVLKGDAPNLERPGAHLAPVDLEATRAELSKELEGKDVDDEDLNGY
LMYPKVFLDYMGRHRTYGPVRSLPTRTFFYGMEPGEEITAEIDPGKTLEIRLQAIGDTDD
KGEVKVFFELNGQPRVIRVPNRLVKATTQANPKAEQGNPNHIGAPMPGVVASVAVQVGQP
VHEGDMLLTIEAMKMETGIHAERDAVVKAVHVQPGGQIDAKDLLIELE
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