4AC3
S.pneumoniae GlmU in complex with an antibacterial inhibitor
Summary for 4AC3
| Entry DOI | 10.2210/pdb4ac3/pdb |
| Related | 4AA7 4AAW |
| Descriptor | BIFUNCTIONAL PROTEIN GLMU, N-{2,4-DIMETHOXY-5-[(2-PIPERIDIN-1-YLBENZYL)sulfamoyl]phenyl}acetamide, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | transferase, acetyl transferase, transferase-inhibitor complex |
| Biological source | STREPTOCOCCUS PNEUMONIAE |
| Cellular location | Cytoplasm : Q8DQ18 |
| Total number of polymer chains | 1 |
| Total formula weight | 50025.08 |
| Authors | Otterbein, L.,Breed, J.,Ogg, D.J. (deposition date: 2011-12-12, release date: 2012-02-15, Last modification date: 2023-12-20) |
| Primary citation | Green, O.M.,McKenzie, A.R.,Shapiro, A.B.,Otterbein, L.,Ni, H.,Patten, A.,Stokes, S.,Albert, R.,Kawatkar, S.,Breed, J. Inhibitors of Acetyltransferase Domain of N-Acetylglucosamine-1-Phosphate-Uridyltransferase/ Glucosamine-1-Phosphate-Acetyltransferase (Glmu). Part 1: Hit to Lead Evaluation of a Novel Arylsulfonamide Series. Bioorg.Med.Chem.Lett., 22:1510-, 2012 Cited by PubMed Abstract: A novel arylsulfonamide-containing series of compounds represented by 1, discovered by highthroughput screening, inhibit the acetyltransferase domain of N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU). X-ray structure determination confirmed that inhibitor binds at the site occupied by acetyl-CoA, indicating that series is competitive with this substrate. This letter documents our early hit-to-lead evaluation of the chemical series and some of the findings that led to improvement in in-vitro potency against Gram-negative and Gram-positive bacterial isozymes, exemplified by compound 40. PubMed: 22297115DOI: 10.1016/J.BMCL.2012.01.016 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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