Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2F4O

The Mouse PNGase-HR23 Complex Reveals a Complete Remodulation of the Protein-Protein Interface Compared to its Yeast Orthologs

Summary for 2F4O
Entry DOI10.2210/pdb2f4o/pdb
Related2F4M
Related PRD IDPRD_000338
Descriptorpeptide N-glycanase, XP-C repair complementing complex 58 kDa protein, PHQ-VAL-ALA-ASP-CF0, ... (6 entities in total)
Functional Keywordsglycoproteins, ubiquitin-dependent protein degradation, nucleotide excision repair, peptide:n-glycanase, transglutaminase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological sourceMus musculus (house mouse)
More
Cellular locationNucleus : P54728
Total number of polymer chains3
Total formula weight42690.07
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 citationZhao, 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: 16500903
DOI: 10.1074/jbc.M600137200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.26 Å)
Structure validation

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon