31RR
Mycobacterium abscessus Phophopantheteinyl transferase PptAb in complex with 4-(tert-butyl)-2-((3,4-dihydro-2H-pyrrol-5-yl)amino)phenol (compound 2d)
This is a non-PDB format compatible entry.
Summary for 31RR
| Entry DOI | 10.2210/pdb31rr/pdb |
| Descriptor | Possible 4'-phosphopantetheinyl transferase, COENZYME A, 4-~{tert}-butyl-2-(3,4-dihydro-2~{H}-pyrrol-5-ylamino)phenol, ... (5 entities in total) |
| Functional Keywords | phosphopantheteinyl transferase mycobacterium abscessus, transferase |
| Biological source | Mycobacteroides abscessus ATCC 19977 |
| Total number of polymer chains | 1 |
| Total formula weight | 26541.79 |
| Authors | Publicola, G.,El Faudel, D.,Genisson, Y.,Mourey, L.,Nahoum, V.,Maveyraud, L. (deposition date: 2026-06-18, release date: 2026-09-23) |
| Primary citation | El Faudel, D.,Publicola, G.,Carayon, C.,Robert, F.,Toppan, C.,Alric, J.,Carivenc, C.,Mourey, L.,Nahoum, V.,Ballereau, S.,Maveyraud, L.,Genisson, Y. From serendipitous reaction discovery to antimycobacterial opportunities: general access to scarcely reported 2-((pyrrolin-5-yl)amino)phenols. Org.Biomol.Chem., 2026 Cited by PubMed Abstract: The rearrangement reaction of 3-(benzoxazol-2-yl)propan-1-amines into 2-((pyrrolin-5-yl)amino)phenols was revealed during an X-ray crystallography fragment screening against PptAb, a phosphopantetheinyl transferase from . Mechanistic and methodological studies offered access to a scarcely exemplified scaffold and prompted revision of the commercial fragment structure. The relevance of this series for the design of PptAb inhibitors was confirmed by the co-crystallization of synthetic samples within the enzyme active site. PubMed: 42704347DOI: 10.1039/d6ob01100d PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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