3O4H

Structure and Catalysis of Acylaminoacyl Peptidase

Summary for 3O4H

• Entry DOI: 10.2210/pdb3o4h/pdb
• Related: 3O4G 3O4I 3O4J
• Descriptor: Acylamino-acid-releasing enzyme, GLYCEROL, SODIUM ION, ... (4 entities in total)
• Functional Keywords: alpha/beta hydrolase fold, beta propeller, hydrolase, oligopeptidase, size selectivity
• Biological source: Aeropyrum pernix
• Cellular location: Cytoplasm : Q9YBQ2
• Total number of polymer chains: 4
• Total formula weight: 252764.62

Authors

Harmat, V.,Domokos, K.,Menyhard, D.K.,Pallo, A.,Szeltner, Z.,Szamosi, I.,Beke-Somfai, T.,Naray-Szabo, G.,Polgar, L. (deposition date: 2010-07-27, release date: 2010-11-17, Last modification date: 2023-09-06)

• Primary citation: Harmat, V.,Domokos, K.,Menyhard, D.K.,Pallo, A.,Szeltner, Z.,Szamosi, I.,Beke-Somfai, T.,Naray-Szabo, G.,Polgar, L.; Structure and Catalysis of Acylaminoacyl Peptidase: CLOSED AND OPEN SUBUNITS OF A DIMER OLIGOPEPTIDASE.; J.Biol.Chem., 286:1987-1998, 2011; PubMed: 21084296; DOI: 10.1074/jbc.M110.169862

Experimental method

X-RAY DIFFRACTION (1.82 Å)