5QLE
Group deposition of library data - Crystal Structure of EcDsbA after initial refinement with no ligand modelled (structure C2_1)
Summary for 5QLE
| Entry DOI | 10.2210/pdb5qle/pdb |
| Group deposition | Crystal Structures of EcDsbA soaked with a library of unpurified reactions after initial automated refinement (G_1002060) |
| Descriptor | Thiol:disulfide interchange protein (2 entities in total) |
| Functional Keywords | disulfide oxidoreductase, redox protein, dsba, oxidoreductase |
| Biological source | Escherichia coli K-12 |
| Total number of polymer chains | 2 |
| Total formula weight | 42310.05 |
| Authors | Ilyichova, O.V.,Bentley, M.R.,Doak, B.C.,Scanlon, M.J. (deposition date: 2019-01-27, release date: 2020-02-05, Last modification date: 2020-07-22) |
| Primary citation | Bentley, M.R.,Ilyichova, O.V.,Wang, G.,Williams, M.L.,Sharma, G.,Alwan, W.S.,Whitehouse, R.L.,Mohanty, B.,Scammells, P.J.,Heras, B.,Martin, J.L.,Totsika, M.,Capuano, B.,Doak, B.C.,Scanlon, M.J. Rapid Elaboration of Fragments into Leads by X-ray Crystallographic Screening of Parallel Chemical Libraries (REFiLX). J.Med.Chem., 63:6863-6875, 2020 Cited by PubMed Abstract: A bottleneck in fragment-based lead development is the lack of systematic approaches to elaborate the initial fragment hits, which usually bind with low affinity to their target. Herein, we describe an analysis using X-ray crystallography of a diverse library of compounds prepared using microscale parallel synthesis. This approach yielded an 8-fold increase in affinity and detailed structural information for the resulting complex, providing an efficient and broadly applicable approach to early fragment development. PubMed: 32529824DOI: 10.1021/acs.jmedchem.0c00111 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.954 Å) |
Structure validation
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