4AXV
Biochemical and structural characterization of the MpaA amidase as part of a conserved scavenging pathway for peptidoglycan derived peptides in gamma-proteobacteria
Summary for 4AXV
Entry DOI | 10.2210/pdb4axv/pdb |
Descriptor | MPAA, ZINC ION, 1,2-ETHANEDIOL, ... (4 entities in total) |
Functional Keywords | hydrolase |
Biological source | Vibrio campbellii ATCC BAA-1116 |
Total number of polymer chains | 1 |
Total formula weight | 27052.67 |
Authors | Maqbool, A.,Herve, M.,Mengin-Lecreulx, D.,Dodson, E.,Wilkinson, A.J.,Thomas, G.H. (deposition date: 2012-06-14, release date: 2012-09-26, Last modification date: 2020-03-04) |
Primary citation | Maqbool, A.,Herve, M.,Mengin-Lecreulx, D.,Wilkinson, A.J.,Thomas, G.H. Mpaa is a Murein-Tripeptide-Specific Zinc Carboxypeptidase that Functions as Part of a Catabolic Pathway for Peptidoglycan Derived Peptides in Gamma-Proteobacteria. Biochem.J., 448:329-, 2012 Cited by PubMed: 22970852DOI: 10.1042/BJ20121164 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.17 Å) |
Structure validation
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