Literature summary for 1.14.11.67 extracted from

Longbotham, J.E.; Kelly, M.J.S.; Fujimori, D.G.
Recognition of histone H3 methylation states by the PHD1 domain of histone demethylase KDM5A (2021), ACS Chem. Biol., FEHLT, 0000 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
solution strucuture of apo and H3-bound domain PHD1. The H3 peptide adopts a helical conformation that allows for extended interactions between the H3 ligand and PHD1 reader domain. H3 residues A1, R2, and K4 are the major determinants of H3 peptide binding, with smaller contributions from H3T3	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P29375	-	-

Synonyms

Synonyms	Comment	Organism
KDM5A	-	Homo sapiens

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Release 2023.1 (January 2023)