Binding Site Information of Target
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T71690 | Target Info | |||
| Target Name | Bacterial Pyruvate decarboxylase (Bact aceE) | ||||
| Synonyms | aceE; Pyruvate decarboxylase E1 component | ||||
| Target Type | Successful Target | ||||
| Gene Name | Bact aceE | ||||
| Biochemical Class | Aldehyde/oxo donor oxidoreductase | ||||
| UniProt ID | |||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| Ligand Name: Thiamin diphosphate | Ligand Info | |||||
| Structure Description | E. COLI PYRUVATE DEHYDROGENASE | PDB:1L8A | ||||
| Method | X-ray diffraction | Resolution | 1.85 Å | Mutation | No | [1] |
| PDB Sequence |
ISNYINTIPV
65 EEQPEYPGNL75 ELERRIRSAI85 RWNAIMTVLR95 ASKKDLELGG105 HMASFQSSAT 115 IYDVCFNHFF125 RARNEQDGGD135 LVYFQGHISP145 GVYARAFLEG155 RLTQEQLDNF 165 RQEVHGNGLS175 SYPHPKLMPE185 FWQFPTVSMG195 LGPIGAIYQA205 KFLKYLEHRG 215 LKDTSKQTVY225 AFLGDGEMDE235 PESKGAITIA245 TREKLDNLVF255 VINCNLQRLD 265 GPVTGNGKII275 NELEGIFEGA285 GWNVIKVMWG295 SRWDELLRKD305 TSGKLIQLMN 315 ETVDGDYQTF325 KSKDGAYVRE335 HFFGKYPETA345 ALVADWTDEQ355 IWALNRGGHD 365 PKKIYAAFKK375 AQETKGKATV385 ILAHTIKGYG395 MGDAAMDGVR418 HIRDRFNVPV 428 SDADIEKLPY438 ITFPEGSEEH448 TYLHAQRQKL458 HGYLPSRQPN468 FTEKLELPSL 478 QDFGALLEEQ488 SKEISTTIAF498 VRALNVMLKN508 KSIKDRLVPI518 IADEARTFGM 528 EGLFRQIGIY538 SPEDEKGQIL565 QEGINELGAG575 CSWLAAATSY585 STNNLPMIPF 595 YIYYSMFGFQ605 RIGDLCWAAG615 DQQARGFLIG625 GTSGRTTLNG635 EGLQHEDGHS 645 HIQSLTIPNC655 ISYDPAYAYE665 VAVIMHDGLE675 RMYGEKQENV685 YYYITTLNEN 695 YHMPAMPEGA705 EEGIRKGIYK715 LETIEGSKGK725 VQLLGSGSIL735 RHVREAAEIL 745 AKDYGVGSDV755 YSVTSFTELA765 RDGQDCERWN775 MLHPLETPRV785 PYIAQVMNDA 795 PAVASTDYMK805 LFAEQVRTYV815 PADDYRVLGT825 DGFGRSDSRE835 NLRHHFEVDA 845 SYVVVAALGE855 LAKRGEIDKK865 VVADAIAKFN875 IDADKVNPRL885 A |
|||||
|
|
||||||
| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Ligand Name: 3-[(4-Amino-2-methylpyrimidin-5-YL)methyl]-2-{(1S)-1-hydroxy-1-[(R)-hydroxy(methoxy)phosphoryl]ethyl}-5-(2-{[(S)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium | Ligand Info | |||||
| Structure Description | E. coli Pyruvate dehydrogenase E1 component E401K mutant with phosphonolactylthiamin diphosphate | PDB:2QTC | ||||
| Method | X-ray diffraction | Resolution | 1.77 Å | Mutation | Yes | [2] |
| PDB Sequence |
ISNYINTIPV
65 EEQPEYPGNL75 ELERRIRSAI85 RWNAIMTVLR95 ASKKDLELGG105 HMASFQSSAT 115 IYDVCFNHFF125 RARNEQDGGD135 LVYFQGHISP145 GVYARAFLEG155 RLTQEQLDNF 165 RQEVHGNGLS175 SYPHPKLMPE185 FWQFPTVSMG195 LGPIGAIYQA205 KFLKYLEHRG 215 LKDTSKQTVY225 AFLGDGEMDE235 PESKGAITIA245 TREKLDNLVF255 VINCNLQRLD 265 GPVTGNGKII275 NELEGIFEGA285 GWNVIKVMWG295 SRWDELLRKD305 TSGKLIQLMN 315 ETVDGDYQTF325 KSKDGAYVRE335 HFFGKYPETA345 ALVADWTDEQ355 IWALNRGGHD 365 PKKIYAAFKK375 AQETKGKATV385 ILAHTIKGYG395 MGDAAMDGVR418 HIRDRFNVPV 428 SDADIEKLPY438 ITFPEGSEEH448 TYLHAQRQKL458 HGYLPSRQPN468 FTEKLELPSL 478 QDFGALLEEQ488 SKEISTTIAF498 VRALNVMLKN508 KSIKDRLVPI518 IADEARTFGM 528 EGLFRQIGIY538 SPEDEKGQIL565 QEGINELGAG575 CSWLAAATSY585 STNNLPMIPF 595 YIYYSMFGFQ605 RIGDLCWAAG615 DQQARGFLIG625 GTSGRTTLNG635 EGLQHEDGHS 645 HIQSLTIPNC655 ISYDPAYAYE665 VAVIMHDGLE675 RMYGEKQENV685 YYYITTLNEN 695 YHMPAMPEGA705 EEGIRKGIYK715 LETIEGSKGK725 VQLLGSGSIL735 RHVREAAEIL 745 AKDYGVGSDV755 YSVTSFTELA765 RDGQDCERWN775 MLHPLETPRV785 PYIAQVMNDA 795 PAVASTDYMK805 LFAEQVRTYV815 PADDYRVLGT825 DGFGRSDSRE835 NLRHHFEVDA 845 SYVVVAALGE855 LAKRGEIDKK865 VVADAIAKFN875 IDADKVNPRL885 A |
|||||
|
|
HIS106
2.564
SER109
3.297
SER112
4.851
GLN140
3.237
HIS142
2.926
TYR177
3.570
VAL192
2.862
SER193
3.799
MET194
2.971
GLY229
3.277
|
|||||
| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Ligand Name: 2-{3-[(4-Amino-2-methylpyrimidin-5-YL)methyl]-4-methyl-2-oxo-2,3-dihydro-1,3-thiazol-5-YL}ethyl trihydrogen diphosphate | Ligand Info | |||||
| Structure Description | E. COLI PYRUVATE DEHYDROGENASE INHIBITOR COMPLEX | PDB:1RP7 | ||||
| Method | X-ray diffraction | Resolution | 2.09 Å | Mutation | No | [3] |
| PDB Sequence |
ISNYINTIPV
65 EEQPEYPGNL75 ELERRIRSAI85 RWNAIMTVLR95 ASKKDLELGG105 HMASFQSSAT 115 IYDVCFNHFF125 RARNEQDGGD135 LVYFQGHISP145 GVYARAFLEG155 RLTQEQLDNF 165 RQEVHGNGLS175 SYPHPKLMPE185 FWQFPTVSMG195 LGPIGAIYQA205 KFLKYLEHRG 215 LKDTSKQTVY225 AFLGDGEMDE235 PESKGAITIA245 TREKLDNLVF255 VINCNLQRLD 265 GPVTGNGKII275 NELEGIFEGA285 GWNVIKVMWG295 SRWDELLRKD305 TSGKLIQLMN 315 ETVDGDYQTF325 KSKDGAYVRE335 HFFGKYPETA345 ALVADWTDEQ355 IWALNRGGHD 365 PKKIYAAFKK375 AQETKGKATV385 ILAHTIKGYG395 MGDAAMDGVR418 HIRDRFNVPV 428 SDADIEKLPY438 ITFPEGSEEH448 TYLHAQRQKL458 HGYLPSRQPN468 FTEKLELPSL 478 QDFGALLEEQ488 SKEISTTIAF498 VRALNVMLKN508 KSIKDRLVPI518 IADEARTFGM 528 EGLFRQIGIY538 SPEDEKGQIL565 QEGINELGAG575 CSWLAAATSY585 STNNLPMIPF 595 YIYYSMFGFQ605 RIGDLCWAAG615 DQQARGFLIG625 GTSGRTTLNG635 EGLQHEDGHS 645 HIQSLTIPNC655 ISYDPAYAYE665 VAVIMHDGLE675 RMYGEKQENV685 YYYITTLNEN 695 YHMPAMPEGA705 EEGIRKGIYK715 LETIEGSKGK725 VQLLGSGSIL735 RHVREAAEIL 745 AKDYGVGSDV755 YSVTSFTELA765 RDGQDCERWN775 MLHPLETPRV785 PYIAQVMNDA 795 PAVASTDYMK805 LFAEQVRTYV815 PADDYRVLGT825 DGFGRSDSRE835 NLRHHFEVDA 845 SYVVVAALGE855 LAKRGEIDKK865 VVADAIAKFN875 IDADKVNPRL885 A |
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .TZD or .TZD2 or .TZD3 or :3TZD;style chemicals stick;color identity;select .A:106 or .A:109 or .A:112 or .A:140 or .A:142 or .A:177 or .A:192 or .A:193 or .A:194 or .A:229 or .A:230 or .A:231 or .A:232 or .A:235 or .A:258 or .A:260 or .A:262 or .A:263 or .A:264 or .A:268 or .A:392; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
HIS106
4.341
SER109
2.736
SER112
4.797
GLN140
3.192
HIS142
2.603
TYR177
4.677
VAL192
2.635
SER193
3.580
MET194
3.147
GLY229
3.343
ASP230
2.955
|
|||||
| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 A resolution. Biochemistry. 2002 Apr 23;41(16):5213-21. | ||||
| REF 2 | A dynamic loop at the active center of the Escherichia coli pyruvate dehydrogenase complex E1 component modulates substrate utilization and chemical communication with the E2 component. J Biol Chem. 2007 Sep 21;282(38):28106-16. | ||||
| REF 3 | Structural determinants of enzyme binding affinity: the E1 component of pyruvate dehydrogenase from Escherichia coli in complex with the inhibitor thiamin thiazolone diphosphate. Biochemistry. 2004 Mar 9;43(9):2405-11. | ||||
If You Find Any Error in Data or Bug in Web Service, Please Kindly Report It to Dr. Zhou and Dr. Zhang.