8DG2
Crystal Structure of EcDsbA in a complex with DMSO
Summary for 8DG2
| Entry DOI | 10.2210/pdb8dg2/pdb |
| Related | 8CXD 8CXE 8CZM 8CZN 8D10 8D11 8D12 8DG0 8DG1 |
| Descriptor | Thiol:disulfide interchange protein DsbA, GLYCEROL, DIMETHYL SULFOXIDE, ... (5 entities in total) |
| Functional Keywords | disulfide oxidoreductase, redox protein, microfrag screening, oxidoreductase |
| Biological source | Escherichia coli K-12 |
| Total number of polymer chains | 2 |
| Total formula weight | 43559.55 |
| Authors | Whitehouse, R.L.,Ilyichova, O.V.,Taylor, A.J. (deposition date: 2022-06-23, release date: 2022-12-07, Last modification date: 2024-11-20) |
| Primary citation | Whitehouse, R.L.,Alwan, W.S.,Ilyichova, O.V.,Taylor, A.J.,Chandrashekaran, I.R.,Mohanty, B.,Doak, B.C.,Scanlon, M.J. Fragment screening libraries for the identification of protein hot spots and their minimal binding pharmacophores. Rsc Med Chem, 14:135-143, 2023 Cited by PubMed Abstract: Fragment-based drug design relies heavily on structural information for the elaboration and optimisation of hits. The ability to identify neighbouring binding hot spots, energetically favourable interactions and conserved binding motifs in protein structures through X-ray crystallography can inform the evolution of fragments into lead-like compounds through structure-based design. The composition of fragment libraries can be designed and curated to fit this purpose and herein, we describe and compare screening libraries containing compounds comprising between 2 and 18 heavy atoms. We evaluate the properties of the compounds in these libraries and assess their ability to probe protein surfaces for binding hot spots. PubMed: 36760747DOI: 10.1039/d2md00253a PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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