Target Binding Site Detail
| 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 | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | Thiamin diphosphate | Ligand Info | |||
| Canonical SMILES | CC1=C(SC=[N+]1CC2=CN=C(N=C2N)C)CCOP(=O)(O)OP(=O)(O)O | ||||
| InChI | 1S/C12H18N4O7P2S/c1-8-11(3-4-22-25(20,21)23-24(17,18)19)26-7-16(8)6-10-5-14-9(2)15-12(10)13/h5,7H,3-4,6H2,1-2H3,(H4-,13,14,15,17,18,19,20,21)/p+1 | ||||
| InChIKey | AYEKOFBPNLCAJY-UHFFFAOYSA-O | ||||
| PubChem Compound ID | 1132 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 1L8A E. COLI PYRUVATE DEHYDROGENASE | ||||||
| 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 |
|||||
|
|
||||||
| PDB ID: 2IEA E. coli pyruvate dehydrogenase | ||||||
| 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 |
|||||
|
|
||||||
| PDB ID: 2QTA E. coli Pyruvate dehydrogenase E1 component E401K mutant with thiamin diphosphate | ||||||
| Method | X-ray diffraction | Resolution | 1.85 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
4.482
SER109
2.934
SER112
4.845
GLN140
3.079
HIS142
2.683
VAL192
2.831
SER193
3.936
MET194
3.259
GLY229
3.403
ASP230
2.984
|
|||||
| 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. | ||||
If You Find Any Error in Data or Bug in Web Service, Please Kindly Report It to Dr. Zhou and Dr. Zhang.