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; PubMed: 18218712; DOI: 10.1110/PS.073271408

Experimental method

X-RAY DIFFRACTION (1.9 Å)