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Literature summary for 2.7.11.22 extracted from

  • Bartova, I.; Otyepka, M.; Kriz, Z.; Koca, J.
    The mechanism of inhibition of the cyclin-dependent kinase-2 as revealed by the molecular dynamics study on the complex CDK2 with the peptide substrate HHASPRK (2005), Protein Sci., 14, 445-451.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.11.22

Crystallization (Commentary)

Crystallization (Comment) Organism
analysis of the crystal structure of the phosphorylated CDK2-cyclin A/substrate peptide complex, PDB-AC 1QMZ Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
additional information CDK2 is inhibited by phosphorylation at Y14 and/or Y15 in the glycine-rich loop causing opening of the substrate binding box and affects binding of ATP Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ coordinated by D145 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein CDK2 is inhibited by phosphorylation at Y14 and/or Y15 in the glycine-rich loop causing opening of the substrate binding box and affects binding of ATP Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + HHASPRK
-
 Homo sapiens ADP + HHAS(P)PRK
-
 ?
additional information determination and analysis of CDK2 consensus sequence X-S/T(P)-P-X-K/R, modeling of substrate binding, structure analysis Homo sapiens ?
-
 ?

Subunits

Subunits Comment Organism
More CDK2 exhibit a classical bi-lobal kinase fold with the C-terminus being alpha-helical and the N-terminus being a flexible hinge Homo sapiens

Synonyms

Synonyms Comment Organism
CDK2
-
 Homo sapiens
cyclin-dependent kinase-2
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP binding at the active site between the C- and N-terminal enzyme domains Homo sapiens
cyclin A
-
 Homo sapiens