Quick Links
Recent Citations
A small-molecule SARS-CoV-2 inhibitor targeting the membrane protein. Van Damme E, Abeywickrema P et al. Nature. 2025 Apr 10;640(8058):506–513.
The conserved HIV-1 spacer peptide 2 triggers matrix lattice maturation. Stacey JCV, Hrebík D et al. Nature. 2025 Apr 3;640(8057):258–264.
Structural insights into lipid chain-length selectivity and allosteric regulation of FFA2. Kugawa M, Kawakami K et al. Nat Commun. 2025 Mar 26;16(1):2809.
Molecular architectures of centrosomes in C. elegans embryos visualized by cryo-electron tomography. Tollervey F, Rios MU et al. Dev Cell. 2025 Mar 24;60(6):885-900.e5.
Balanced plant helper NLR activation by a modified host protein complex. Huang S, Wang J et al. Nature. 2025 Mar 13;639(8054):447–455.
Previously featured citations...Chimera Search
Google™ SearchNews
March 6, 2025
Chimera production release 1.19 is now available, fixing the ability to fetch structures from the PDB (details...).
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).
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 TRPA1 ion channel (wasabi receptor) determined by electron cryo-microscopy, Protein Data Bank entry 3j9p. The four subunits of the tetramer are shown as ribbons in different colors over a dark-to-light gradient background. (More samples...)
About RBVI | Projects | People | Publications | Resources | Visit Us
Copyright 2018 Regents of the University of California. All rights reserved.