2VD4
Structure of small-molecule inhibitor of Glmu from Haemophilus influenzae reveals an allosteric binding site
Summary for 2VD4
Entry DOI | 10.2210/pdb2vd4/pdb |
Related | 2V0H 2V0I 2V0J 2V0K 2V0L |
Descriptor | BIFUNCTIONAL PROTEIN GLMU, 4-chloro-N-(3-methoxypropyl)-N-[(3S)-1-(2-phenylethyl)piperidin-3-yl]benzamide, SULFATE ION, ... (7 entities in total) |
Functional Keywords | glmu, inhibitor, magnesium, cell shape, peptidoglycan synthesis, allosteric, transferase, active site, metal-binding, cell wall biogenesis/degradation, multifunctional enzyme, nucleotidyltransferase, acyltransferase, uridyltransferase |
Biological source | HAEMOPHILUS INFLUENZAE |
Cellular location | Cytoplasm (By similarity): P43889 |
Total number of polymer chains | 1 |
Total formula weight | 50924.64 |
Authors | Mochalkin, I.,Lightle, S.,McDowell, L. (deposition date: 2007-09-28, release date: 2008-01-15, Last modification date: 2023-12-13) |
Primary citation | Mochalkin, I.,Lightle, S.,Narasimhan, L.,Bornemeier, D.,Melnick, M.,Vanderroest, S.,Mcdowell, L. Structure of a Small-Molecule Inhibitor Complexed with Glmu from Haemophilus Influenzae Reveals an Allosteric Binding Site. Protein Sci., 17:577-, 2008 Cited by PubMed: 18218712DOI: 10.1110/PS.073271408 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
Download full validation report