Target Information
| Target General Information | Top | |||||
|---|---|---|---|---|---|---|
| Target ID |
T34337
(Former ID: TTDR01143)
|
|||||
| Target Name |
Bacterial Undecaprenyl pyrophosphate synthetase (Bact ispU)
|
|||||
| Synonyms |
ispU; Undecaprenyl diphosphate synthase; Undecaprenyl diphosphate synthase; UPP synthetase; UPP synthase; UDS; Di-trans-poly-cis-decaprenylcistransferase
Click to Show/Hide
|
|||||
| Gene Name |
Bact ispU
|
|||||
| Target Type |
Literature-reported target
|
[1] | ||||
| Function |
Generates ditrans,octacis-undecaprenyl pyrophosphate (UPP) from isopentenyl pyrophosphate (IPP) and farnesyl diphosphate (FPP). UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide.
Click to Show/Hide
|
|||||
| BioChemical Class |
Alkyl aryl transferase
|
|||||
| UniProt ID | ||||||
| EC Number |
EC 2.5.1.31
|
|||||
| Sequence |
MMLSATQPLSEKLPAHGCRHVAIIMDGNGRWAKKQGKIRAFGHKAGAKSVRRAVSFAANN
GIEALTLYAFSSENWNRPAQEVSALMELFVWALDSEVKSLHRHNVRLRIIGDTSRFNSRL QERIRKSEALTAGNTGLTLNIAANYGGRWDIVQGVRQLAEKVQQGNLQPDQIDEEMLNQH VCMHELAPVDLVIRTGGEHRISNFLLWQIAYAELYFTDVLWPDFDEQDFEGALNAFANRE RRFGGTEPGDETA Click to Show/Hide
|
|||||
| 3D Structure | Click to Show 3D Structure of This Target | PDB | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| Ligand Name: Clomifene | Ligand Info | |||||
| Structure Description | Crystal structure of E. coli undecaprenyl pyrophosphate synthase in complex with clomiphene | PDB:5CQJ | ||||
| Method | X-ray diffraction | Resolution | 2.15 Å | Mutation | No | [3] |
| PDB Sequence |
LPAHGCRHVA
22 IIMDGNGRWA32 KKQGKIRAFG42 HKAGAKSVRR52 AVSFAANNGI62 EALTLYAFEL 88 FVWALDSEVK98 SLHRHNVRLR108 IIGDTSRFNS118 RLQERIRKSE128 ALTAGNTGLT 138 LNIAANYGGR148 WDIVQGVRQL158 AEKVQQGNLQ168 PDQIDEEMLN178 QHVCMHELAP 188 VDLVIRTGGE198 HRISNFLLWQ208 IAYAELYFTD218 VLWPDFDEQD228 FEGALNAFAN 238 RE
|
|||||
|
|
||||||
| Ligand Name: Isopentenyl pyrophosphate | Ligand Info | |||||
| Structure Description | Crystal structure of the D26A mutant UPPs in complex with magnesium and isopentenyl pyrophosphate | PDB:1X09 | ||||
| Method | X-ray diffraction | Resolution | 1.87 Å | Mutation | Yes | [4] |
| PDB Sequence |
LSEKLPAHGC
18 RHVAIIMAGN28 GRWAKKQGKI38 RAFGHKAGAK48 SVRRAVSFAA58 NNGIEALTLY 68 AFSSENWNRP78 AQEVSALMEL88 FVWALDSEVK98 SLHRHNVRLR108 IIGDTSRFNS 118 RLQERIRKSE128 ALTAGNTGLT138 LNIAANYGGR148 WDIVQGVRQL158 AEKVQQGNLQ 168 PDQIDEEMLN178 QHVCMHELAP188 VDLVIRTGGE198 HRISNFLLWQ208 IAYAELYFTD 218 VLWPDFDEQD228 FEGALNAFAN238 R
|
|||||
|
|
||||||
| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Click to View More Binding Site Information of This Target with Different Ligands | ||||||
| Different Human System Profiles of Target | Top |
|---|---|
|
Human Similarity Proteins
of target is determined by comparing the sequence similarity of all human proteins with the target based on BLAST. The similarity proteins for a target are defined as the proteins with E-value < 0.005 and outside the protein families of the target.
A target that has fewer human similarity proteins outside its family is commonly regarded to possess a greater capacity to avoid undesired interactions and thus increase the possibility of finding successful drugs
(Brief Bioinform, 21: 649-662, 2020).
Human Similarity Proteins
|
|
|
There is no similarity protein (E value < 0.005) for this target
|
| References | Top | |||||
|---|---|---|---|---|---|---|
| REF 1 | The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. | |||||
| REF 2 | Synthesis and biological activity of isopentenyl diphosphate analogues. Bioorg Med Chem. 2004 Feb 15;12(4):763-70. | |||||
| REF 3 | Antagonism screen for inhibitors of bacterial cell wall biogenesis uncovers an inhibitor of undecaprenyl diphosphate synthase. Proc Natl Acad Sci U S A. 2015 Sep 1;112(35):11048-53. | |||||
| REF 4 | Crystal structures of undecaprenyl pyrophosphate synthase in complex with magnesium, isopentenyl pyrophosphate, and farnesyl thiopyrophosphate: roles of the metal ion and conserved residues in catalysis. J Biol Chem. 2005 May 27;280(21):20762-74. | |||||
If You Find Any Error in Data or Bug in Web Service, Please Kindly Report It to Dr. Zhou and Dr. Zhang.