Quick Links
Recent Citations
Structure and assembly of the dystrophin glycoprotein complex. Wan L, Ge X et al. Nature. 2025 Jan 30;637(8048):1252–1260.
Structural basis for the conformational protection of nitrogenase from O2. Narehood SM, Cook BD et al. Nature. 2025 Jan 23;637(8047):991–997.
Molecular mechanism of IgE-mediated FcεRI activation. Chen M, Su Q, Shi Y. Nature. 2025 Jan 9;637(8045):453–460.
High-resolution cryo-EM using a common LaB6 120-keV electron microscope equipped with a sub-200-keV direct electron detector. Venugopal H, Mobbs J et al. Sci Adv. 2025 Jan 3;11(1):eadr0438.
Read-write mechanisms of H2A ubiquitination by Polycomb repressive complex 1. López VG, Valencia-Sánchez MI et al. Nature. 2024 Dec 19;636(8043):755–761.
Previously featured citations...Chimera Search
Google SearchNews
December 25, 2024
![]() |
October 14, 2024
Planned downtime: The Chimera and ChimeraX websites, web services (Blast Protein, Modeller, ...) and cgl.ucsf.edu e-mail will be unavailable starting Monday, Oct 14 10 AM PDT, continuing throughout the week and potentially the weekend (Oct 14-20).
August 1, 2024
Planned downtime: The Chimera and ChimeraX websites, web services (Blast Protein, Modeller, ...) and cgl.ucsf.edu e-mail will be unavailable August 1, 3-6 pm PDT.
Previous news...Upcoming Events
UCSF Chimera is a program for the interactive visualization and analysis of molecular structures and related data, including density maps, trajectories, and sequence alignments. It is available free of charge for noncommercial use. Commercial users, please see Chimera commercial licensing.
We encourage Chimera users to try ChimeraX for much better performance with large structures, as well as other major advantages and completely new features in addition to nearly all the capabilities of Chimera (details...).
Chimera is no longer under active development. Chimera development was supported by a grant from the National Institutes of Health (P41-GM103311) that ended in 2018.
Feature Highlight
Structures and their pocket measurements can be fetched directly from the Computed Atlas of Surface Topography of proteins (CASTp) database or read from local files previously returned by the CASTp server. In Chimera, the pockets are shown in a pocket list. Choosing rows in the list performs actions such as zooming in on pockets and selecting the surrounding atoms.
The figure shows the four largest pockets by volume identified by CASTp for PDB entry 1ovh (a cavity mutant of T4 lysozyme), shown in yellow, orange, pink, and magenta in order of decreasing volume. The largest is lysozyme's active site, with two openings. The second largest is the engineered cavity. Mutated positions are shown in red. Green balls are Cl– ions.
(More features...)Gallery Sample
The image shows the structure of the human OX2 orexin receptor bound to the insomnia drug suvorexant, Protein Data Bank entry 4s0v. The drug is shown as spheres colored by element, and the receptor as ribbons with secondary structure elements rainbow-colored from blue at the N-terminus to red at the C-terminus. (More samples...)
About RBVI | Projects | People | Publications | Resources | Visit Us
Copyright 2018 Regents of the University of California. All rights reserved.