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6PMF

Crystal Structure of EcDsbA in complex with aniline 15

Summary for 6PMF
Entry DOI10.2210/pdb6pmf/pdb
DescriptorThiol:disulfide interchange protein DsbA, [6-(phenylamino)-1-benzofuran-3-yl]acetic acid, COPPER (II) ION, ... (4 entities in total)
Functional Keywordsdisulfide oxidoreductase, redox protein, oxidoreductase-inhibitor complex, oxidoreductase, oxidoreductase/inhibitor
Biological sourceEscherichia coli (strain K12)
Total number of polymer chains2
Total formula weight42640.88
Authors
Ilyichova, O.V.,Scanlon, M.J. (deposition date: 2019-07-01, release date: 2019-11-06, Last modification date: 2023-10-11)
Primary citationDuncan, L.F.,Wang, G.,Ilyichova, O.V.,Scanlon, M.J.,Heras, B.,Abbott, B.M.
The Fragment-Based Development of a Benzofuran Hit as a New Class of Escherichia coli DsbA Inhibitors.
Molecules, 24:-, 2019
Cited by
PubMed Abstract: A fragment-based drug discovery approach was taken to target the thiol-disulfide oxidoreductase enzyme DsbA from (DsbA). This enzyme is critical for the correct folding of virulence factors in many pathogenic Gram-negative bacteria, and small molecule inhibitors can potentially be developed as anti-virulence compounds. Biophysical screening of a library of fragments identified several classes of fragments with affinity to DsbA. One hit with high mM affinity, 2-(6-bromobenzofuran-3-yl)acetic acid (), was chemically elaborated at several positions around the scaffold. X-ray crystal structures of the elaborated analogues showed binding in the hydrophobic binding groove adjacent to the catalytic disulfide bond of DsbA. Binding affinity was calculated based on NMR studies and compounds and were identified as the highest affinity binders with dissociation constants () of 326 ± 25 and 341 ± 57 µM respectively. This work suggests the potential to develop benzofuran fragments into a novel class of DsbA inhibitors.
PubMed: 31635355
DOI: 10.3390/molecules24203756
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.95 Å)
Structure validation

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