5K1X

Catalytic domain of polyspecific pyrrolysyl-tRNA synthetase mutant Y306A/N346A/C348A/Y384F in complex with AMPPNP

Summary for 5K1X

Entry DOI	10.2210/pdb5k1x/pdb
Related	5K1P
Descriptor	Pyrrolysine--tRNA ligase, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MAGNESIUM ION, ... (7 entities in total)
Functional Keywords	protein engineering, aminoacyl-trna synthetase, noncanonical amino acids, ligase
Biological source	Methanosarcina mazei
Total number of polymer chains	1
Total formula weight	32419.76
Authors	Weber, A. (deposition date: 2016-05-18, release date: 2016-10-19, Last modification date: 2024-03-06)
Primary citation	Lee, Y.J.,Schmidt, M.J.,Tharp, J.M.,Weber, A.,Koenig, A.L.,Zheng, H.,Gao, J.,Waters, M.L.,Summerer, D.,Liu, W.R. Genetically encoded fluorophenylalanines enable insights into the recognition of lysine trimethylation by an epigenetic reader. Chem.Commun.(Camb.), 52:12606-12609, 2016 Cited by PubMed Abstract: Fluorophenylalanines bearing 2-5 fluorine atoms at the phenyl ring have been genetically encoded by amber codon. Replacement of F59, a phenylalanine residue that is directly involved in interactions with trimethylated K9 of histone H3, in the Mpp8 chromodomain recombinantly with fluorophenylalanines significantly impairs the binding to a K9-trimethylated H3 peptide. PubMed: 27711380 DOI: 10.1039/c6cc05959g PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.95 Å)

Structure validation