7QTY

X-ray structure of FAD domain of NqrF of Klebsiella pneumoniae

Summary for 7QTY

• Entry DOI: 10.2210/pdb7qty/pdb
• Descriptor: Na(+)-translocating NADH-quinone reductase subunit F, FLAVIN-ADENINE DINUCLEOTIDE, 1-(furan-2-ylmethyl)-3-(2-methylphenyl)thiourea, ... (5 entities in total)
• Functional Keywords: nadh oxidizing, flavoprotein
• Biological source: Klebsiella pneumoniae
• Total number of polymer chains: 1
• Total formula weight: 33204.45

Authors

Stegmann, D.,Steuber, J.,Fritz, G. (deposition date: 2022-01-17, release date: 2022-02-09, Last modification date: 2024-01-31)

Primary citation

Kaminski, J.W.,Vera, L.,Stegmann, D.P.,Vering, J.,Eris, D.,Smith, K.M.L.,Huang, C.Y.,Meier, N.,Steuber, J.,Wang, M.,Fritz, G.,Wojdyla, J.A.,Sharpe, M.E.
Fast fragment- and compound-screening pipeline at the Swiss Light Source.
Acta Crystallogr D Struct Biol, 78:328-336, 2022

PubMed Abstract: Over the last two decades, fragment-based drug discovery (FBDD) has emerged as an effective and efficient method to identify new chemical scaffolds for the development of lead compounds. X-ray crystallography can be used in FBDD as a tool to validate and develop fragments identified as binders by other methods. However, it is also often used with great success as a primary screening technique. In recent years, technological advances at macromolecular crystallography beamlines in terms of instrumentation, beam intensity and robotics have enabled the development of dedicated platforms at synchrotron sources for FBDD using X-ray crystallography. Here, the development of the Fast Fragment and Compound Screening (FFCS) platform, an integrated next-generation pipeline for crystal soaking, handling and data collection which allows crystallography-based screening of protein crystals against hundreds of fragments and compounds, at the Swiss Light Source is reported.

PubMed: 35234147
DOI: 10.1107/S2059798322000705

Experimental method

X-RAY DIFFRACTION (1.69 Å)