Target Information
| Target General Information | Top | |||||
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| Target ID |
T85801
(Former ID: TTDR00746)
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| Target Name |
Pseudomonas Phosphomannomutase/phosphoglucomutase (Pseudo algC)
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| Synonyms |
algC; PMM/PGM; PMM / PGM
Click to Show/Hide
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| Gene Name |
Pseudo algC
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| Target Type |
Literature-reported target
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[1] | ||||
| Function |
Highly reversible phosphoryltransferase. The phosphomannomutase activity produces a precursor for alginate polymerization, the alginate layer causes a mucoid phenotype and provides a protective barrier against host immune defenses and antibiotics. Also involved in core lipopolysaccaride (LPS) biosynthesis due to its phosphoglucomutase activity. Essential for rhamnolipid production, an exoproduct correlated with pathogenicity (PubMed:10481091). Required for biofilm production. The reaction proceeds via 2 processive phosphoryl transferase reactions; first from enzyme-phospho-Ser-108 to the substrate (generatinga bisphosphorylated substrate intermediate and a dephosphorylated enzyme), a 180 degree rotation of the intermediate (probably aided by movement of domain 4), and subsequent transfer of phosphate back to the enzyme (PubMed:11716469, PubMed:16880541, PubMed:16595672, PubMed:22242625).
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| BioChemical Class |
Intramolecular transferases
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| UniProt ID | ||||||
| Sequence |
MSTAKAPTLPASIFRAYDIRGVVGDTLTAETAYWIGRAIGSESLARGEPCVAVGRDGRLS
GPELVKQLIQGLVDCGCQVSDVGMVPTPVLYYAANVLEGKSGVMLTGSHNPPDYNGFKIV VAGETLANEQIQALRERIEKNDLASGVGSVEQVDILPRYFKQIRDDIAMAKPMKVVVDCG NGVAGVIAPQLIEALGCSVIPLYCEVDGNFPNHHPDPGKPENLKDLIAKVKAENADLGLA FDGDGDRVGVVTNTGTIIYPDRLLMLFAKDVVSRNPGADIIFDVKCTRRLIALISGYGGR PVMWKTGHSLIKKKMKETGALLAGEMSGHVFFKERWFGFDDGIYSAARLLEILSQDQRDS EHVFSAFPSDISTPEINITVTEDSKFAIIEALQRDAQWGEGNITTLDGVRVDYPKGWGLV RASNTTPVLVLRFEADTEEELERIKTVFRNQLKAVDSSLPVPF Click to Show/Hide
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| 3D Structure | Click to Show 3D Structure of This Target | PDB | ||||
| Drug Binding Sites of Target | Top | |||||
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| Ligand Name: Alpha-D-Glucose-1-Phosphate | Ligand Info | |||||
| Structure Description | Enzyme-ligand complex of P. aeruginosa PMM/PGM | PDB:1P5D | ||||
| Method | X-ray diffraction | Resolution | 1.60 Å | Mutation | Yes | [2] |
| PDB Sequence |
LPASIFRAYD
18 IRGVVGDTLT28 AETAYWIGRA38 IGSESLARGE48 PCVAVGRDGR58 LSGPELVKQL 68 IQGLVDCGCQ78 VSDVGMVPTP88 VLYYAANVLE98 GKSGVMLTGH109 NPPDYNGFKI 119 VVAGETLANE129 QIQALRERIE139 KNDLASGVGS149 VEQVDILPRY159 FKQIRDDIAM 169 AKPMKVVVDC179 GNGVAGVIAP189 QLIEALGCSV199 IPLYCEVDGN209 FPNHHPDPGK 219 PENLKDLIAK229 VKAENADLGL239 AFDGDGDRVG249 VVTNTGTIIY259 PDRLLMLFAK 269 DVVSRNPGAD279 IIFDVKCTRR289 LIALISGYGG299 RPVMWKTGHS309 LIKKKMKETG 319 ALLAGEMSGH329 VFFKERWFGF339 DDGIYSAARL349 LEILSQDQRD359 SEHVFSAFPS 369 DISTPEINIT379 VTEDSKFAII389 EALQRDAQWG399 EGNITTLDGV409 RVDYPKGWGL 419 VRASNTTPVL429 VLRFEADTEE439 ELERIKTVFR449 NQLKAVDSSL459 PVPF |
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Ligand Name: L-serine-O-phosphate | Ligand Info | |||||
| Structure Description | Enzyme-ligand complex of P. aeruginosa PMM/PGM | PDB:1P5D | ||||
| Method | X-ray diffraction | Resolution | 1.60 Å | Mutation | Yes | [2] |
| PDB Sequence |
LPASIFRAYD
18 IRGVVGDTLT28 AETAYWIGRA38 IGSESLARGE48 PCVAVGRDGR58 LSGPELVKQL 68 IQGLVDCGCQ78 VSDVGMVPTP88 VLYYAANVLE98 GKSGVMLTGH109 NPPDYNGFKI 119 VVAGETLANE129 QIQALRERIE139 KNDLASGVGS149 VEQVDILPRY159 FKQIRDDIAM 169 AKPMKVVVDC179 GNGVAGVIAP189 QLIEALGCSV199 IPLYCEVDGN209 FPNHHPDPGK 219 PENLKDLIAK229 VKAENADLGL239 AFDGDGDRVG249 VVTNTGTIIY259 PDRLLMLFAK 269 DVVSRNPGAD279 IIFDVKCTRR289 LIALISGYGG299 RPVMWKTGHS309 LIKKKMKETG 319 ALLAGEMSGH329 VFFKERWFGF339 DDGIYSAARL349 LEILSQDQRD359 SEHVFSAFPS 369 DISTPEINIT379 VTEDSKFAII389 EALQRDAQWG399 EGNITTLDGV409 RVDYPKGWGL 419 VRASNTTPVL429 VLRFEADTEE439 ELERIKTVFR449 NQLKAVDSSL459 PVPF |
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| 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 |
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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
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There is no similarity protein (E value < 0.005) for this target
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| Drug Property Profile of Target | Top | |
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| (1) Molecular Weight (mw) based Drug Clustering | (2) Octanol/Water Partition Coefficient (xlogp) based Drug Clustering | |
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| (3) Hydrogen Bond Donor Count (hbonddonor) based Drug Clustering | (4) Hydrogen Bond Acceptor Count (hbondacc) based Drug Clustering | |
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| (5) Rotatable Bond Count (rotbonds) based Drug Clustering | (6) Topological Polar Surface Area (polararea) based Drug Clustering | |
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| "RO5" indicates the cutoff set by lipinski's rule of five; "D123AB" colored in GREEN denotes the no violation of any cutoff in lipinski's rule of five; "D123AB" colored in PURPLE refers to the violation of only one cutoff in lipinski's rule of five; "D123AB" colored in BLACK represents the violation of more than one cutoffs in lipinski's rule of five | ||
| References | Top | |||||
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| REF 1 | How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6. | |||||
| REF 2 | Structural basis of diverse substrate recognition by the enzyme PMM/PGM from P. aeruginosa. Structure. 2004 Jan;12(1):55-63. | |||||
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