3J9J
Structure of the capsaicin receptor, TRPV1, determined by single particle electron cryo-microscopy
Summary for 3J9J
Entry DOI | 10.2210/pdb3j9j/pdb |
Related | 3J5P |
EMDB information | 5778 |
Descriptor | Transient receptor potential cation channel subfamily V member 1 (1 entity in total) |
Functional Keywords | alpha helical, membrane protein |
Biological source | Rattus norvegicus (rat) |
Cellular location | Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein: O35433 |
Total number of polymer chains | 4 |
Total formula weight | 268939.81 |
Authors | Wang, R.Y.-R.,Barad, B.A.,Fraser, J.S.,DiMaio, F. (deposition date: 2015-02-02, release date: 2015-09-02, Last modification date: 2024-02-21) |
Primary citation | Barad, B.A.,Echols, N.,Wang, R.Y.,Cheng, Y.,DiMaio, F.,Adams, P.D.,Fraser, J.S. EMRinger: side chain-directed model and map validation for 3D cryo-electron microscopy. Nat.Methods, 12:943-946, 2015 Cited by PubMed Abstract: Advances in high-resolution cryo-electron microscopy (cryo-EM) require the development of validation metrics to independently assess map quality and model geometry. We report EMRinger, a tool that assesses the precise fitting of an atomic model into the map during refinement and shows how radiation damage alters scattering from negatively charged amino acids. EMRinger (https://github.com/fraser-lab/EMRinger) will be useful for monitoring progress in resolving and modeling high-resolution features in cryo-EM. PubMed: 26280328DOI: 10.1038/nmeth.3541 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.275 Å) |
Structure validation
Download full validation report
