2FP0
human ADP-ribosylhydrolase 3
Summary for 2FP0
Entry DOI | 10.2210/pdb2fp0/pdb |
Related | 2FOZ |
Descriptor | ADP-ribosylhydrolase like 2, MAGNESIUM ION (3 entities in total) |
Functional Keywords | all alpha-helical, metal binding, adp-ribose binding, hydrolase |
Biological source | Homo sapiens (human) |
Cellular location | Cytoplasm (By similarity): Q9NX46 |
Total number of polymer chains | 2 |
Total formula weight | 75613.77 |
Authors | Mueller-Dieckmann, C.,Weiss, M.S.,Koch-Nolte, F. (deposition date: 2006-01-15, release date: 2006-10-10, Last modification date: 2023-08-30) |
Primary citation | Mueller-Dieckmann, C.,Kernstock, S.,Lisurek, M.,von Kries, J.P.,Haag, F.,Weiss, M.S.,Koch-Nolte, F. The structure of human ADP-ribosylhydrolase 3 (ARH3) provides insights into the reversibility of protein ADP-ribosylation. Proc.Natl.Acad.Sci.Usa, 103:15026-15031, 2006 Cited by PubMed: 17015823DOI: 10.1073/pnas.0606762103 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
Download full validation report