4MUS
Crystal structure of vancomycin resistance D,D-dipeptidase/D,D-pentapeptidase VanXYc D59S mutant in complex with D-Ala-D-Ala phosphinate analog
Summary for 4MUS
Entry DOI | 10.2210/pdb4mus/pdb |
Related | 4F78 4MUQ 4MUR 4MUT 4OAK |
Descriptor | D,D-dipeptidase/D,D-carboxypeptidase, ZINC ION, (2R)-3-[(R)-[(1S)-1-aminoethyl](hydroxy)phosphoryl]-2-methylpropanoic acid, ... (8 entities in total) |
Functional Keywords | center for structural genomics of infectious diseases, csgid, national institute of allergy and infectious diseases, niaid, alpha+beta protein, metallopeptidase, hedgehog/dd-peptidase fold, merops m15b subfamily, zn2+-dependent d, d-dipeptidase, d-pentapeptidase, antibiotic resistance, vancomycin resistance, hydrolase |
Biological source | Enterococcus gallinarum |
Total number of polymer chains | 2 |
Total formula weight | 50666.95 |
Authors | Stogios, P.J.,Evdokimova, E.,Meziane-Cherif, D.,Di Leo, R.,Yim, V.,Courvalin, P.,Savchenko, A.,Anderson, W.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2013-09-23, release date: 2013-10-09, Last modification date: 2023-09-20) |
Primary citation | Meziane-Cherif, D.,Stogios, P.J.,Evdokimova, E.,Savchenko, A.,Courvalin, P. Structural basis for the evolution of vancomycin resistance D,D-peptidases. Proc.Natl.Acad.Sci.USA, 111:5872-5877, 2014 Cited by PubMed: 24711382DOI: 10.1073/pnas.1402259111 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.675 Å) |
Structure validation
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