SitesBLAST
Comparing SMc03895 FitnessBrowser__Smeli:SMc03895 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)
3tw6B Structure of rhizobium etli pyruvate carboxylase t882a with the allosteric activator, acetyl coenzyme-a (see paper)
86% identity, 99% coverage: 3:1147/1152 of query aligns to 3:1129/1129 of 3tw6B
- active site: K124 (= K124), K162 (= K166), H212 (= H216), R238 (= R242), T277 (= T281), E279 (= E283), E293 (= E297), N295 (= N299), R297 (= R301), E301 (= E305), R349 (= R353), D544 (= D548), D650 (= D654), K713 (= K717), H742 (= H746), H744 (= H748), A877 (≠ T881)
- binding adenosine-5'-diphosphate: K124 (= K124), K162 (= K166), G167 (= G171), G169 (= G173), M172 (= M176), E204 (= E208), L206 (= L210), V207 (= V211), H212 (= H216), Q236 (= Q240), N239 (= N243), L281 (= L285), E293 (= E297), T450 (= T454)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: R349 (= R353), D395 (= D399), K1102 (= K1117)
- binding magnesium ion: E279 (= E283), E293 (= E297), M529 (≠ V533), R530 (≠ K534), E532 (≠ Q536), D763 (= D767)
- binding zinc ion: D544 (= D548), K713 (= K717), H742 (= H746), H744 (= H748)
2qf7A Crystal structure of a complete multifunctional pyruvate carboxylase from rhizobium etli (see paper)
82% identity, 100% coverage: 3:1150/1152 of query aligns to 3:1076/1076 of 2qf7A
- active site: K124 (= K124), H147 (= H216), R173 (= R242), T212 (= T281), E214 (= E283), E228 (= E297), N230 (= N299), R232 (= R301), E236 (= E305), R284 (= R353), D479 (= D548), D585 (= D654), K648 (= K717), H677 (= H746), H679 (= H748), T812 (= T881)
- binding phosphothiophosphoric acid-adenylate ester: H147 (= H216), Q171 (= Q240), E214 (= E283), L216 (= L285), E228 (= E297), T385 (= T454)
- binding coenzyme a: R400 (= R469), Q401 (= Q470), D402 (= D471), R403 (= R472), A404 (= A473), I956 (= I1025), K960 (= K1029), L962 (= L1031), N985 (= N1054)
- binding magnesium ion: E214 (= E283), E228 (= E297), M464 (≠ V533), R465 (≠ K534), E467 (≠ Q536), D698 (= D767)
- binding zinc ion: D479 (= D548), K648 (= K717), H677 (= H746), H679 (= H748)
3tw6C Structure of rhizobium etli pyruvate carboxylase t882a with the allosteric activator, acetyl coenzyme-a (see paper)
86% identity, 92% coverage: 3:1064/1152 of query aligns to 3:1044/1044 of 3tw6C
- active site: K124 (= K124), K166 (= K166), H200 (= H216), R226 (= R242), T265 (= T281), E267 (= E283), E281 (= E297), N283 (= N299), R285 (= R301), E289 (= E305), R337 (= R353), D528 (= D548), D634 (= D654), K697 (= K717), H726 (= H746), H728 (= H748), A861 (≠ T881)
- binding adenosine-5'-diphosphate: K166 (= K166), M169 (= M176), V195 (= V211), H200 (= H216), Q224 (= Q240), E281 (= E297), T438 (= T454)
- binding coenzyme a: R411 (= R427), R413 (= R429), R453 (= R469), Q454 (= Q470), D455 (= D471), R456 (= R472), L1011 (= L1031)
- binding magnesium ion: E267 (= E283), E281 (= E297)
- binding phosphonoacetic acid: K229 (= K245), R285 (= R301), Q287 (= Q303), V288 (= V304), E289 (= E305)
- binding zinc ion: D528 (= D548), K697 (= K717), H726 (= H746), H728 (= H748)
2qf7B Crystal structure of a complete multifunctional pyruvate carboxylase from rhizobium etli (see paper)
85% identity, 92% coverage: 3:1065/1152 of query aligns to 3:1015/1017 of 2qf7B
- active site: K123 (= K124), K150 (= K166), H169 (= H216), R195 (= R242), T234 (= T281), E236 (= E283), E250 (= E297), N252 (= N299), R254 (= R301), E258 (= E305), R306 (= R353), D498 (= D548), D604 (= D654), K667 (= K717), H696 (= H746), H698 (= H748), T831 (= T881)
- binding phosphothiophosphoric acid-adenylate ester: M148 (= M164), K150 (= K166), M153 (= M176), E161 (= E208), V164 (= V211), H169 (= H216), Q193 (= Q240), E236 (= E283), L238 (= L285), I249 (= I296), E250 (= E297), T407 (= T454)
- binding magnesium ion: E236 (= E283), E250 (= E297), M483 (≠ V533), R484 (≠ K534), E486 (≠ Q536), D717 (= D767)
- binding zinc ion: D498 (= D548), K667 (= K717), H696 (= H746), H698 (= H748)
3tw6A Structure of rhizobium etli pyruvate carboxylase t882a with the allosteric activator, acetyl coenzyme-a (see paper)
82% identity, 93% coverage: 3:1070/1152 of query aligns to 3:1007/1007 of 3tw6A
- active site: K124 (= K124), H152 (= H216), R178 (= R242), T217 (= T281), E219 (= E283), E233 (= E297), N235 (= N299), R237 (= R301), E241 (= E305), R289 (= R353), D485 (= D548), D591 (= D654), K654 (= K717), H683 (= H746), H685 (= H748), A818 (≠ T881)
- binding adenosine-5'-diphosphate: L146 (= L210), V147 (= V211), H152 (= H216), Q176 (= Q240), N179 (= N243), L221 (= L285)
- binding coenzyme a: R365 (= R429), R405 (= R469), Q406 (= Q470), D407 (= D471), R408 (= R472), T967 (= T1030), L968 (= L1031)
- binding magnesium ion: E219 (= E283), E233 (= E297), M470 (≠ V533), R471 (≠ K534), E473 (≠ Q536), D704 (= D767)
- binding zinc ion: D485 (= D548), K654 (= K717), H683 (= H746), H685 (= H748)
A0A0H3JRU9 Pyruvate carboxylase; EC 6.4.1.1 from Staphylococcus aureus (strain Mu50 / ATCC 700699) (see 2 papers)
52% identity, 99% coverage: 3:1148/1152 of query aligns to 4:1143/1150 of A0A0H3JRU9
- R21 (= R20) mutation to A: Complete loss of catalytic activity.
- K119 (= K124) binding ATP
- K161 (= K166) binding ATP
- H211 (= H216) binding ATP
- E278 (= E283) binding ATP
- K411 (≠ R418) mutation to A: Complete loss of catalytic activity.
- RDAHQ 541:545 (≠ RDGHQ 547:551) binding substrate
- D542 (= D548) binding Mn(2+)
- 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 (= K717) binding Mn(2+)
- H741 (= H746) binding Mn(2+)
- H743 (= H748) binding Mn(2+)
- Q838 (= Q843) mutation to A: About 2.5-fold loss of catalytic activity.
- T876 (= T881) mutation to A: Complete loss of catalytic activity.
- S879 (= S884) mutation to A: About 2-fold loss of catalytic activity.
- K880 (= K885) mutation to T: Complete loss of catalytic activity.
3bg5A Crystal structure of staphylococcus aureus pyruvate carboxylase (see paper)
51% identity, 99% coverage: 3:1148/1152 of query aligns to 2:1134/1137 of 3bg5A
- active site: K117 (= K124), K159 (= K166), S189 (≠ D203), H202 (= H216), R228 (= R242), T267 (= T281), E269 (= E283), E281 (= E297), N283 (= N299), R285 (= R301), E289 (= E305), R337 (= R353), D533 (= D548), D639 (= D654), K703 (= K717), H732 (= H746), H734 (= H748), I755 (≠ V769), S761 (≠ A775), M762 (≠ L776), T801 (≠ A815), T867 (= T881), S869 (= S883), V881 (= V895), N883 (≠ Q897), Q888 (≠ A902)
- binding adenosine-5'-triphosphate: K117 (= K124), M157 (= M164), K159 (= K166), Y196 (≠ L210), I197 (≠ V211), H202 (= H216), Q226 (= Q240), H229 (≠ N243), E269 (= E283), L271 (= L285), E281 (= E297), N283 (= N299)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: Y463 (= Y479), G471 (= G487), F472 (≠ H488), P473 (= P489), F579 (= F594)
- binding manganese (ii) ion: D533 (= D548), H732 (= H746), H734 (= H748)
- binding pyruvic acid: L603 (= L618), K703 (= K717)
3hb9A Crystal structure of s. Aureus pyruvate carboxylase a610t mutant (see paper)
51% identity, 99% coverage: 3:1148/1152 of query aligns to 2:1130/1133 of 3hb9A
- active site: K117 (= K124), K159 (= K166), H198 (= H216), R224 (= R242), T263 (= T281), E265 (= E283), E277 (= E297), N279 (= N299), R281 (= R301), E285 (= E305), R333 (= R353), D529 (= D548), D635 (= D654), K699 (= K717), H728 (= H746), H730 (= H748), I751 (≠ V769), S757 (≠ A775), M758 (≠ L776), T797 (≠ A815), T863 (= T881), S865 (= S883), V877 (= V895), N879 (≠ Q897), Q884 (≠ A902)
- binding adenosine-5'-diphosphate: K117 (= K124), M157 (= M164), Y192 (≠ L210), I193 (≠ V211), H198 (= H216), Q222 (= Q240), H225 (≠ N243), L267 (= L285), I276 (= I296), E277 (= E297)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: Y459 (= Y479), N462 (≠ D482), G467 (= G487), F468 (≠ H488), F575 (= F594), K577 (≠ T596)
- binding manganese (ii) ion: D529 (= D548), H728 (= H746), H730 (= H748)
7zz3A Cryo-em structure of "bc react" conformation of lactococcus lactis pyruvate carboxylase with acetyl-coa (see paper)
50% identity, 99% coverage: 3:1148/1152 of query aligns to 2:1135/1138 of 7zz3A
- binding acetyl coenzyme *a: N22 (= N23), F43 (= F44), K44 (= K45), A45 (= A46), D46 (= D47), S48 (= S49), R363 (= R374), H413 (≠ R424), E414 (= E425), R416 (= R427), R418 (= R429), R459 (≠ Q470), R461 (= R472), K1016 (= K1029), T1017 (= T1030), L1018 (= L1031), R1045 (= R1058)
- binding adenosine-5'-triphosphate: K117 (= K124), M156 (= M164), K158 (= K166), G163 (= G171), G164 (= G172), G165 (= G173), M168 (= M176), E200 (= E208), Y202 (≠ L210), I203 (≠ V211), H208 (= H216), Q232 (= Q240), N235 (= N243), L277 (= L285), E287 (= E297), N289 (= N299), T443 (= T454)
- binding bicarbonate ion: K237 (= K245), R291 (= R301), Q293 (= Q303), E295 (= E305)
- binding biotin: G84 (= G91), V294 (= V304), R342 (= R353), K1104 (= K1117)
- binding magnesium ion: E275 (= E283), E287 (= E297), V520 (= V533), T523 (≠ Q536), D754 (= D767)
- binding manganese (ii) ion: D535 (= D548), K704 (= K717), H733 (= H746), H735 (= H748)
- binding pyruvic acid: R534 (= R547), Q538 (= Q551), L605 (= L618), K704 (= K717), T868 (= T881)
5vyzA Crystal structure of lactococcus lactis pyruvate carboxylase in complex with cyclic-di-amp (see paper)
50% identity, 99% coverage: 3:1148/1152 of query aligns to 8:1141/1144 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 (≠ A726), Y722 (≠ R729), S752 (≠ L759), G753 (≠ A760), Q756 (≠ E763)
- binding adenosine-5'-diphosphate: K123 (= K124), M162 (= M164), K164 (= K166), G168 (= G170), G170 (= G172), G171 (= G173), M174 (= M176), Y208 (≠ L210), I209 (≠ V211), H214 (= H216), Q238 (= Q240), N241 (= N243), L283 (= L285), E293 (= E297), T449 (= T454)
- binding magnesium ion: E281 (= E283), E293 (= E297)
- binding manganese (ii) ion: D541 (= D548), K710 (= K717), H739 (= H746), H741 (= H748)
4mfeA Structure of the carboxyl transferase domain from rhizobium etli pyruvate carboxylase with 3-hydroxypyruvate (see paper)
87% identity, 52% coverage: 471:1065/1152 of query aligns to 1:596/597 of 4mfeA
- active site: D79 (= D548), D185 (= D654), K248 (= K717), H277 (= H746), H279 (= H748), T412 (= T881)
- binding 3-hydroxypyruvic acid: R78 (= R547), Q82 (= Q551), G116 (= G585), L149 (= L618), R151 (= R620), V411 (= V880), T412 (= T881)
- binding biotin: Y9 (= Y479), P19 (= P489), R596 (= R1065)
- binding magnesium ion: M64 (≠ V533), R65 (≠ K534), E67 (≠ Q536), D298 (= D767)
- binding zinc ion: D79 (= D548), K248 (= K717), H277 (= H746), H279 (= H748)
4mfdA Structure of the carboxyl transferase domain from rhizobium etli pyruvate carboxylase with oxalate (see paper)
87% identity, 52% coverage: 471:1065/1152 of query aligns to 1:596/597 of 4mfdA
- active site: D79 (= D548), D185 (= D654), K248 (= K717), H277 (= H746), H279 (= H748), T412 (= T881)
- binding magnesium ion: M64 (≠ V533), R65 (≠ K534), E67 (≠ Q536), D298 (= D767)
- binding oxalate ion: Q82 (= Q551), G116 (= G585), L149 (= L618), R151 (= R620), T412 (= T881)
- binding zinc ion: D79 (= D548), K248 (= K717), H277 (= H746), H279 (= H748)
4m6vA Structure of the carboxyl transferase domain from rhizobium etli pyruvate carboxylase with pyruvate and biocytin (see paper)
87% identity, 52% coverage: 471:1065/1152 of query aligns to 1:596/597 of 4m6vA
- active site: D79 (= D548), D185 (= D654), K248 (= K717), H277 (= H746), H279 (= H748), T412 (= T881)
- binding Biocytin: Y9 (= Y479), D12 (= D482), G17 (= G487), H18 (= H488), P19 (= P489), E20 (= E490), R24 (= R494), R124 (= R593), F354 (= F823), T376 (= T845), Y531 (= Y1000), R596 (= R1065)
- binding magnesium ion: M64 (≠ V533), R65 (≠ K534), E67 (≠ Q536), D298 (= D767)
- binding pyruvic acid: Q82 (= Q551), L149 (= L618), R151 (= R620), K248 (= K717), T412 (= T881)
- binding zinc ion: D79 (= D548), K248 (= K717), H277 (= H746), H279 (= H748)
4jx5A Structure of the carboxyl transferase domain from rhizobium etli pyruvate carboxylase with pyruvate (see paper)
87% identity, 52% coverage: 471:1065/1152 of query aligns to 1:596/597 of 4jx5A
- active site: D79 (= D548), D185 (= D654), K248 (= K717), H277 (= H746), H279 (= H748), T412 (= T881)
- binding magnesium ion: M64 (≠ V533), R65 (≠ K534), E67 (≠ Q536), D298 (= D767)
- binding pyruvic acid: Q82 (= Q551), L149 (= L618), R151 (= R620), K248 (= K717), T412 (= T881)
- binding zinc ion: D79 (= D548), K248 (= K717), H277 (= H746), H279 (= H748)
4mimA Structure of the carboxyl transferase domain from rhizobium etli pyruvate carboxylase with 3-bromopyruvate (see paper)
86% identity, 52% coverage: 471:1065/1152 of query aligns to 1:594/595 of 4mimA
- active site: D79 (= D548), D185 (= D654), K248 (= K717), H277 (= H746), H279 (= H748), T412 (= T881)
- binding Bromopyruvate: R78 (= R547), D79 (= D548), Q82 (= Q551), L149 (= L618), R151 (= R620), K248 (= K717), H279 (= H748), T412 (= T881)
- binding magnesium ion: M64 (≠ V533), R65 (≠ K534), E67 (≠ Q536), D298 (= D767)
- binding zinc ion: D79 (= D548), K248 (= K717), H277 (= H746), H279 (= H748)
4locA Structure of the carboxyl transferase domain from rhizobium etli pyruvate carboxylase with oxamate and biotin (see paper)
86% identity, 52% coverage: 471:1065/1152 of query aligns to 1:594/595 of 4locA
- active site: D79 (= D548), D185 (= D654), K248 (= K717), H277 (= H746), H279 (= H748), T412 (= T881)
- binding biotin: Y9 (= Y479), D12 (= D482), P19 (= P489), F125 (= F594), R594 (= R1065)
- binding magnesium ion: M64 (≠ V533), R65 (≠ K534), E67 (≠ Q536), D298 (= D767)
- binding zinc ion: D79 (= D548), K248 (= K717), H277 (= H746), H279 (= H748)
7zyyA Cryo-em structure of lactococcus lactis pyruvate carboxylase with acetyl-coa (see paper)
51% identity, 92% coverage: 3:1066/1152 of query aligns to 2:1053/1056 of 7zyyA
- binding acetyl coenzyme *a: R19 (= R20), N22 (= N23), F43 (= F44), K44 (= K45), A45 (= A46), R363 (= R374), E414 (= E425), R416 (= R427), R418 (= R429), R459 (≠ Q470), D460 (= D471), R461 (= R472), K1016 (= K1029), T1017 (= T1030), L1018 (= L1031), N1041 (= N1054), R1045 (= R1058)
- binding adenosine-5'-diphosphate: K158 (= K166), G163 (= G171), G164 (= G172), M168 (= M176), E200 (= E208), K201 (= K209), Y202 (≠ L210), I203 (≠ V211), H208 (= H216), Q232 (= Q240), N235 (= N243), E275 (= E283), L277 (= L285), E287 (= E297), T443 (= T454)
- binding bicarbonate ion: R291 (= R301), Q293 (= Q303), V294 (= V304), E295 (= E305)
- binding magnesium ion: E275 (= E283), E287 (= E297), V520 (= V533), T523 (≠ Q536), D754 (= D767)
- binding manganese (ii) ion: D535 (= D548), K704 (= K717), H733 (= H746), H735 (= H748)
- binding pyruvic acid: Q538 (= Q551), G572 (= G585), L605 (= L618), R607 (= R620), K704 (= K717), T868 (= T881)
8gk8A R21a staphylococcus aureus pyruvate carboxylase (see paper)
51% identity, 92% coverage: 3:1064/1152 of query aligns to 2:1036/1041 of 8gk8A
- binding acetyl coenzyme *a: E400 (= E425), R402 (= R427), R404 (= R429), L445 (≠ Q470), R447 (= R472), N1026 (= N1054), R1030 (= R1058)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: N457 (≠ D482), G462 (= G487), F463 (≠ H488), P464 (= P489), F570 (= F594), K572 (≠ T596)
- binding coenzyme a: R42 (= R43), Y43 (≠ F44), A45 (= A46), D46 (= D47), E47 (= E48), S48 (= S49)
- binding manganese (ii) ion: D524 (= D548), K694 (= K717), H723 (= H746), H725 (= H748)
7wtbB Cryo-em structure of human pyruvate carboxylase with acetyl-coa (see paper)
48% identity, 99% coverage: 3:1148/1152 of query aligns to 6:1144/1147 of 7wtbB
- binding acetyl coenzyme *a: F22 (= F19), T26 (≠ N23), R46 (= R43), Q47 (≠ F44), K48 (= K45), A49 (= A46), D50 (= D47), R367 (= R374), R414 (= R421), E418 (= E425), R420 (= R427), R422 (= R429), A462 (≠ R469), Q463 (= Q470), R465 (= R472), K1025 (= K1029)
- binding phosphoaminophosphonic acid-adenylate ester: K163 (= K166), G168 (= G171), G169 (= G172), M173 (= M176), F207 (≠ L210), I208 (≠ V211), P211 (≠ A214), H240 (≠ N243)
- binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: D582 (= D589), Q839 (= Q843), T877 (= T881), S880 (= S884), K881 (= K885)
7wtdC Cryo-em structure of human pyruvate carboxylase with acetyl-coa in the intermediate state 1 (see paper)
48% identity, 99% coverage: 3:1148/1152 of query aligns to 5:1143/1146 of 7wtdC
- binding adenosine-5'-triphosphate: K162 (= K166), G167 (= G171), G168 (= G172), F206 (≠ L210), Q236 (= Q240), H239 (≠ N243), E292 (= E297)
- binding coenzyme a: F21 (= F19), R22 (= R20), T25 (≠ N23), R45 (= R43), Q46 (≠ F44), K47 (= K45), A48 (= A46), D49 (= D47), E50 (= E48), R366 (= R374), R413 (= R421), A416 (≠ R424), R419 (= R427), Q462 (= Q470), R464 (= R472), A465 (= A473), Q466 (≠ T474), K1024 (= K1029), R1053 (= R1058)
Query Sequence
>SMc03895 FitnessBrowser__Smeli:SMc03895
MSISKILVANRSEIAIRVFRAANELGLKTVAIWAEEDKLALHRFKADESYQVGRGPHLPR
DLGPIMSYLSIDEVIRVAKLSGADAIHPGYGLLSESPEFAEACAANGITFIGPKPETMRQ
LGNKVAARNLAISIGVPVVPATEPLPDDPEEIKRLAEEIGYPVMLKASWGGGGRGMRAIR
DPKDLIREVTEAKREAKAAFGKDEVYLEKLVERARHVESQILGDTHGNVVHLFERDCSIQ
RRNQKVVERAPAPYLNDAQRQELADYSLKIARATNYIGAGTVEYLMDSDTGKFYFIEVNP
RIQVEHTVTEVVTGIDIVKAQIHILDGFAIGAPESGVPRQEDIRLNGHALQCRITTEDPE
QNFIPDYGRITAYRGATGFGIRLDGGTAYSGAVITRYYDPLLEKVTAWAPNPGEAIQRMI
RALREFRIRGVATNLTFLEAIISHPKFHDNSYTTRFIDTTPELFQQVKRQDRATKLLTYL
ADVTVNGHPEVKGRPKPSDDIAAPVVPFTGGDVKPGTKQRLDQLGPKKFAEWVKAQPEVL
ITDTTMRDGHQSLLATRMRTYDIARIAGTYARALPNLFSLECWGGATFDVSMRFLTEDPW
ERLAMVREGAPNLLLQMLLRGANGVGYKNYPDNVVKYFVRQAAKGGIDVFRVFDCLNWVE
NMRVAMDAVAEEDRICEAAICYTGDILNSARPKYDLKYYTALAAELEKAGAHMIAVKDMA
GLLKPAAARVLFKALKEATGLPIHFHTHDTSGIAAATVLAAVESGVDVVDAAMDALSGNT
SQPCLGSIVEALSGSERDPGLDPEWIRRISFYWEAVRHQYAAFESDLKGPASEVYLHEMP
GGQFTNLKEQARSLGLETRWHEVAQAYADANRMFGDIVKVTPSSKVVGDMALMMVSQDLT
VADVENPGKDIAFPESVVSMLKGDLGQPPGGWPEALQKKALKGEEPYDARPGSLLEDADL
DAERKGIEEKLGREVTDFEFASYLMYPKVFTDYAVACETYGPVSVLPTPAYFYGMAPGEE
LFADIEKGKTLVILNQAQGEIDEKGMVKMFFEMNGQPRSIKVPDRNRGASAAVRRKAEAG
NAAHLGAPMPGVISTVAVASGQSVKAGDVLLSIEAMKMETALHAEKDGVISEVLVRAGDQ
IDAKDLLVVFGG
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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