5AGC
Crystallographic forms of the Vps75 tetramer
Summary for 5AGC
Entry DOI | 10.2210/pdb5agc/pdb |
Descriptor | VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 75 (1 entity in total) |
Functional Keywords | transport protein, vps75, vacuolar protein sorting 75, histone chaperone, nap1, chromatin |
Biological source | SACCHAROMYCES CEREVISIAE (BAKER'S YEAST) |
Cellular location | Nucleus : P53853 |
Total number of polymer chains | 4 |
Total formula weight | 122624.34 |
Authors | Hammond, C.M.,Sundaramoorthy, R.,Owen-Hughes, T. (deposition date: 2015-01-29, release date: 2016-03-02, Last modification date: 2024-01-10) |
Primary citation | Hammond, C.M.,Sundaramoorthy, R.,Larance, M.,Lamond, A.,Stevens, M.A.,El-Mkami, H.,Norman, D.G.,Owen-Hughes, T. The Histone Chaperone Vps75 Forms Multiple Oligomeric Assemblies Capable of Mediating Exchange between Histone H3-H4 Tetramers and Asf1-H3-H4 Complexes. Nucleic Acids Res., 44:6157-, 2016 Cited by PubMed: 27036862DOI: 10.1093/NAR/GKW209 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (4 Å) |
Structure validation
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