scispace - formally typeset
C

Colin R. Groom

Researcher at University of Cambridge

Publications -  53
Citations -  15467

Colin R. Groom is an academic researcher from University of Cambridge. The author has contributed to research in topics: Crystal structure & Crystal structure prediction. The author has an hindex of 27, co-authored 53 publications receiving 13081 citations. Previous affiliations of Colin R. Groom include Massey University & University of Leeds.

Papers
More filters
Journal ArticleDOI

Identifying Interactions that Determine Fragment Binding at Protein Hotspots.

TL;DR: A method that samples atomic hotspots with simple molecular probes to produce fragment hotspot maps that provide an intuitive visual guide within the binding site, directing medicinal chemists where to grow the molecule and alerting them to suboptimal interactions within the original hit.
Journal ArticleDOI

The good, the bad and the twisted: a survey of ligand geometry in protein crystal structures

TL;DR: An analysis of the geometry of ligands bound to proteins is presented and the role of small molecule crystal structures is highlighted in enabling molecular modellers to critically evaluate a ligand model’s quality and investigate protein-induced strain.
Journal ArticleDOI

IRAK-4 inhibitors. Part II: a structure-based assessment of imidazo[1,2-a]pyridine binding.

TL;DR: A potent IRAK-4 inhibitor was identified through routine project cross screening and the binding mode was inferred using a combination of in silico docking into an IRAK -4 homology model, surrogate crystal structure analysis and chemical analogue SAR.
Journal ArticleDOI

The Cambridge Structural Database in Retrospect and Prospect

TL;DR: The Cambridge Crystallographic Data Centre (CCDC) as discussed by the authors was established in 1965 to record numerical, chemical and bibliographic data relating to published organic and metal-organic crystal structures.
Journal ArticleDOI

The hydrogen bond environments of 1H-tetrazole and tetrazolate rings: the structural basis for tetrazole-carboxylic acid bioisosterism.

TL;DR: Analysis of pairs of PDB structures containing ligands which differ only in having a tetrazole or a carboxyl substituent and which are bound to the same protein indicates that the protein binding site must flex sufficiently to form strong H-bonds to either substituents.