Target Information
| Target General Information | Top | |||||
|---|---|---|---|---|---|---|
| Target ID |
T94594
(Former ID: TTDR01157)
|
|||||
| Target Name |
Pseudomonas Nicotinate-nucleotide adenylyltransferase (Pseudo nadD)
|
|||||
| Synonyms |
nadD of Pseudomonas aeruginosa; Nicotinic acid mononucleotide adenylyltransferase of Pseudomonas aeruginosa; Nicotinatemononucleotide adenylyltransferase of Pseudomonas aeruginosa; Nicotinate-nucleotide adenylyltransferase of Pseudomonas aeruginosa; NaMN-Atase; NaMN adenylyltransferase of Pseudomonas aeruginosa; NaMN AT of Pseudomonas aeruginosa; Deamido-NAD(+) pyrophosphorylase of Pseudomonas aeruginosa; Deamido-NAD(+) diphosphorylase of Pseudomonas aeruginosa
Click to Show/Hide
|
|||||
| Gene Name |
Pseudo nadD
|
|||||
| Target Type |
Literature-reported target
|
[1] | ||||
| Function |
Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Click to Show/Hide
|
|||||
| BioChemical Class |
Kinase
|
|||||
| UniProt ID | ||||||
| EC Number |
EC 2.7.7.18
|
|||||
| Sequence |
MGKRIGLFGGTFDPVHIGHMRSAVEMAEQFALDELRLLPNARPPHRETPQVSAAQRLAMV
ERAVAGVERLTVDPRELQRDKPSYTIDTLESVRAELAADDQLFMLIGWDAFCGLPTWHRW EALLDHCHIVVLQRPDADSEPPESLRDLLAARSVADPQALKGPGGQITFVWQTPLAVSAT QIRALLGAGRSVRFLVPDAVLNYIEAHHLYRAPH Click to Show/Hide
|
|||||
| 3D Structure | Click to Show 3D Structure of This Target | PDB | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| Ligand Name: Adenosine triphosphate | Ligand Info | |||||
| Structure Description | Crystal Structure of Nicotinic Acid Mononucleotide Adenylyltransferase from Pseudomonas aeruginosa | PDB:1YUN | ||||
| Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | No | [2] |
| PDB Sequence |
GKRIGLFGGT
11 FDPVHIGHMR21 SAVEMAEQFA31 LDELRLLPNA41 RPPHRETPQV51 SAAQRLAMVE 61 RAVAGVERLT71 VDPRELQRDK81 PSYTIDTLES91 VRAELAADDQ101 LFMLIGWDAF 111 CGLPTWHRWE121 ALLDHCHIVV131 LQRPDADSEP141 PESLRDLLAA151 RSVADPQALK 161 GPGGQITFVW171 QTPLAVSATQ181 IRALLGAGRS191 VRFLVPDAVL201 NYIEAHHLYR 211
|
|||||
|
|
||||||
| Ligand Name: Namn | Ligand Info | |||||
| Structure Description | Crystal Structure of Nicotinic Acid Mononucleotide Adenylyltransferase from Pseudomonas aeruginosa | PDB:1YUM | ||||
| Method | X-ray diffraction | Resolution | 1.70 Å | Mutation | No | [2] |
| PDB Sequence |
GKRIGLFGGT
11 FDPVHIGHMR21 SAVEMAEQFA31 LDELRLLPNA41 RPPHRETPQV51 SAAQRLAMVE 61 RAVAGVERLT71 VDPRELQRDK81 PSYTIDTLES91 VRAELAADDQ101 LFMLIGWDAF 111 CGLPTWHRWE121 ALLDHCHIVV131 LQRPDADSEP141 PESLRDLLAA151 RSVADPQALK 161 GPGGQITFVW171 QTPLAVSATQ181 IRALLGAGRS191 VRFLVPDAVL201 NYIEAHHLYR 211 AP
|
|||||
|
|
||||||
| 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
|
| Target Affiliated Biological Pathways | Top | |||||
|---|---|---|---|---|---|---|
| KEGG Pathway | [+] 2 KEGG Pathways | + | ||||
| 1 | Nicotinate and nicotinamide metabolism | |||||
| 2 | Metabolic pathways | |||||
| References | Top | |||||
|---|---|---|---|---|---|---|
| REF 1 | How many drug targets are there Nat Rev Drug Discov. 2006 Dec;5(12):993-6. | |||||
| REF 2 | Crystal structure of nicotinic acid mononucleotide adenylyltransferase from Pseudomonas aeruginosa in its Apo and substrate-complexed forms reveals a fully open conformation. J Mol Biol. 2005 Aug 12;351(2):258-65. | |||||
If You Find Any Error in Data or Bug in Web Service, Please Kindly Report It to Dr. Zhou and Dr. Zhang.