2F4O
The Mouse PNGase-HR23 Complex Reveals a Complete Remodulation of the Protein-Protein Interface Compared to its Yeast Orthologs
Summary for 2F4O
Entry DOI | 10.2210/pdb2f4o/pdb |
Related | 2F4M |
Related PRD ID | PRD_000338 |
Descriptor | peptide N-glycanase, XP-C repair complementing complex 58 kDa protein, PHQ-VAL-ALA-ASP-CF0, ... (6 entities in total) |
Functional Keywords | glycoproteins, ubiquitin-dependent protein degradation, nucleotide excision repair, peptide:n-glycanase, transglutaminase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
Biological source | Mus musculus (house mouse) More |
Cellular location | Nucleus : P54728 |
Total number of polymer chains | 3 |
Total formula weight | 42690.07 |
Authors | Zhao, G.,Zhou, X.,Wang, L.,Kisker, C.,Lennarz, W.J.,Schindelin, H. (deposition date: 2005-11-23, release date: 2006-03-07, Last modification date: 2023-08-23) |
Primary citation | Zhao, G.,Zhou, X.,Wang, L.,Li, G.,Kisker, C.,Lennarz, W.J.,Schindelin, H. Structure of the mouse peptide N-glycanase-HR23 complex suggests co-evolution of the endoplasmic reticulum-associated degradation and DNA repair pathways. J.Biol.Chem., 281:13751-13761, 2006 Cited by PubMed: 16500903DOI: 10.1074/jbc.M600137200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.26 Å) |
Structure validation
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