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6H2Q

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

Summary for 6H2Q
Entry DOI10.2210/pdb6h2q/pdb
Related5MC5 5mby 5mbz 5mc0 5mc1 5mc2 5mc3 5mc4
DescriptorXaa-Pro dipeptidase, MANGANESE (II) ION, GLYCEROL, ... (6 entities in total)
Functional Keywordsprolidase, peptidase, hydrolysis, pita-bread, metalloenzyme, mutation, hydrolase
Biological sourceHomo sapiens (Human)
Total number of polymer chains2
Total formula weight110160.60
Authors
Wilk, P.,Piwowarczyk, R.,Weiss, M.S. (deposition date: 2018-07-14, release date: 2018-08-15, Last modification date: 2020-04-22)
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 (1.78 Å)
Structure validation

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