6H2P
Crystal Structure of Arg184Gln mutant of Human Prolidase with Mn ions and Cacodylate ligand
Summary for 6H2P
Entry DOI | 10.2210/pdb6h2p/pdb |
Related | 5mby 5mbz 5mc0 5mc1 5mc2 5mc3 5mc4 5mc5 |
Descriptor | Xaa-Pro dipeptidase, MANGANESE (II) ION, CACODYLATE ION, ... (5 entities in total) |
Functional Keywords | prolidase, peptidase, hydrolysis, pita-bread, metalloenzyme, mutation, hydrolase |
Biological source | Homo sapiens (Human) |
Total number of polymer chains | 2 |
Total formula weight | 109984.00 |
Authors | Wilk, P.,Piwowarczyk, R.,Weiss, M.S. (deposition date: 2018-07-14, release date: 2018-08-29, Last modification date: 2024-01-17) |
Primary citation | Wilk, P.,Uehlein, M.,Piwowarczyk, R.,Dobbek, H.,Mueller, U.,Weiss, M.S. Structural basis for prolidase deficiency disease mechanisms. FEBS J., 285:3422-3441, 2018 Cited by PubMed: 30066404DOI: 10.1111/febs.14620 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.479 Å) |
Structure validation
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