4XV6
CcP gateless cavity
Summary for 4XV6
| Entry DOI | 10.2210/pdb4xv6/pdb |
| Related | 4XV4 4XV5 4XV7 4XV8 4XVA |
| Descriptor | Cytochrome c peroxidase, mitochondrial, PROTOPORPHYRIN IX CONTAINING FE, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (4 entities in total) |
| Functional Keywords | model system, flexibility, thermodynamics, cryptic site, transient protein sites, ligand binding, oxidoreductase |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 33740.31 |
| Authors | Fischer, M.,Fraser, J.S. (deposition date: 2015-01-26, release date: 2015-02-18, Last modification date: 2024-02-28) |
| Primary citation | Fischer, M.,Shoichet, B.K.,Fraser, J.S. One Crystal, Two Temperatures: Cryocooling Penalties Alter Ligand Binding to Transient Protein Sites. Chembiochem, 16:1560-1564, 2015 Cited by PubMed Abstract: Interrogating fragment libraries by X-ray crystallography is a powerful strategy for discovering allosteric ligands for protein targets. Cryocooling of crystals should theoretically increase the fraction of occupied binding sites and decrease radiation damage. However, it might also perturb protein conformations that can be accessed at room temperature. Using data from crystals measured consecutively at room temperature and at cryogenic temperature, we found that transient binding sites could be abolished at the cryogenic temperatures employed by standard approaches. Changing the temperature at which the crystallographic data was collected could provide a deliberate perturbation to the equilibrium of protein conformations and help to visualize hidden sites with great potential to allosterically modulate protein function. PubMed: 26032594DOI: 10.1002/cbic.201500196 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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