Any feedback?
Literature summary for 2.7.7.3 extracted from
- Umbrella sampling and X-ray crystallographic analysis unveil an Arg-Asp gate facilitating inhibitor binding inside phosphopantetheine adenylyltransferase allosteric cleft (2018), J. Phys. Chem. B, 122, 1551-1559 .
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| structure of apo-PPAT. Residues R90 and D94 residues act like a gate near the binding cavity to accommodate and stabilize the incoming ligand | Pseudomonas aeruginosa |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| R90A/D94A | in silico mutation, ligand acetyl-CoA fails to maintain its position inside the binding cavity | Pseudomonas aeruginosa |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| acetyl-CoA | - |
Pseudomonas aeruginosa |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudomonas aeruginosa | A0A0X1KGP2 | - |
- |
| Pseudomonas aeruginosa 2192 | A0A0X1KGP2 | - |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CoaD | - |
Pseudomonas aeruginosa |
| phosphopantetheine adenylyltransferase | - |
Pseudomonas aeruginosa |
| PPAT | - |
Pseudomonas aeruginosa |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
