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6H2P

Crystal Structure of Arg184Gln mutant of Human Prolidase with Mn ions and Cacodylate ligand

Summary for 6H2P
Entry DOI10.2210/pdb6h2p/pdb
Related5mby 5mbz 5mc0 5mc1 5mc2 5mc3 5mc4 5mc5
DescriptorXaa-Pro dipeptidase, MANGANESE (II) ION, CACODYLATE ION, ... (5 entities in total)
Functional Keywordsprolidase, peptidase, hydrolysis, pita-bread, metalloenzyme, mutation, hydrolase
Biological sourceHomo sapiens (Human)
Total number of polymer chains2
Total formula weight109984.00
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 citationWilk, 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: 30066404
DOI: 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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