4jqn | pdb_00004jqn

Crystal structure of Cytochrome C Peroxidase W191G-Gateless in complex with 4-Hydroxybenzaldehyde

spinqualitylabelsall models 4jqn, resolution 1.36Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4jqn is a 1 chain structure with sequence from Saccharomyces cerevisiae RM11-1a. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.36Å Ligands: HBA, HEM, MES, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B3LRE1_YEAS1 Publication Abstract from PubMed Predicting absolute protein-ligand binding affinities remains a frontier challenge in ligand discovery and design. This becomes more difficult when ionic interactions are involved because of the large opposing solvation and electrostatic attraction energies. In a blind test, we examined whether alchemical free-energy calculations could predict binding affinities of 14 charged and 5 neutral compounds previously untested as ligands for a cavity binding site in cytochrome c peroxidase. In this simplified site, polar and cationic ligands compete with solvent to interact with a buried aspartate. Predictions were tested by calorimetry, spectroscopy, and crystallography. Of the 15 compounds predicted to bind, 13 were experimentally confirmed, while 4 compounds were false negative predictions. Predictions had a root-mean-square error of 1.95kcal/mol to the experimental affinities, and predicted poses had an average RMSD of 1.7A to the crystallographic poses. This test serves as a benchmark for these thermodynamically rigorous calculations at predicting binding affinities for charged compounds and gives insights into the existing sources of error, which are primarily electrostatic interactions inside proteins. Our experiments also provide a useful set of ionic binding affinities in a simplified system for testing new affinity prediction methods. Blind Prediction of Charged Ligand Binding Affinities in a Model Binding Site.,Rocklin GJ, Boyce SE, Fischer M, Fish I, Mobley DL, Shoichet BK, Dill KA J Mol Biol. 2013 Jul 26. pii: S0022-2836(13)00477-4. doi:, 10.1016/j.jmb.2013.07.030. PMID:23896298 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytochrome c peroxidase 3D structures

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