Literature summary for 2.7.11.1 extracted from

Zakharevich, N.; Osolodkin, D.; Artamonova, I.; Palyulin, V.; Zefirov, N.; Danilenko, V.
Signatures of the ATP-binding pocket as a basis for structural classification of the serine/threonine protein kinases of gram-positive bacteria (2012), Proteins, 80, 1363-1376.

Search for more literature for 2.7.11.1

Application

Application	Comment	Organism
drug development	the eukaryotic-like serine/threonine protein kinases are targets for the treatment of tuberculosis	Firmicutes

Organism

Organism	UniProt	Comment	Textmining
Firmicutes	-	human pathogenic, pro-biotic, and antibiotic-producing	-

Synonyms

Synonyms	Comment	Organism
ESTPK	-	Firmicutes
eukaryotic-like serine/threonine protein kinase	-	Firmicutes

Cofactor

Cofactor	Comment	Organism	Structure
ATP	physicochemical properties of amino acid residues in the ATP-binding site of the enzyme, overview. Nine residues are identified that line the surface of the adenine-binding pocket, and ESTPKs are classified based on these signatures	Firmicutes

General Information

General Information	Comment	Organism
evolution	classification of amino acid residues in the ATP-binding site of the enzyme in diverse Gram-positive bacteria, 20 groups, phylogenetic tree and homology modeling, overview	Firmicutes

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Release 2023.1 (January 2023)