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2Z7L

Unphosphorylated Mitogen Activated Protein Kinase ERK2 in Complex with (4-{[5-Carbamoyl-4-(3-Methylanilino)Pyrimidin 2-Yl]Amino}Phenyl)Acetic Acid

Summary for 2Z7L
Entry DOI10.2210/pdb2z7l/pdb
DescriptorMitogen-activated protein kinase 1, SULFATE ION, [4-({5-(AMINOCARBONYL)-4-[(3-METHYLPHENYL)AMINO]PYRIMIDIN-2-YL}AMINO)PHENYL]ACETIC ACID, ... (5 entities in total)
Functional Keywordstransferase, serine/threonine-protein kinase, atp-binding, cell cycle, phosphorylation, acetylation, nucleotide-binding
Biological sourceRattus norvegicus (Rat)
Total number of polymer chains1
Total formula weight43069.56
Authors
Katayama, N.,Kurihara, H. (deposition date: 2007-08-27, release date: 2008-08-12, Last modification date: 2023-11-01)
Primary citationKatayama, N.,Orita, M.,Yamaguchi, T.,Hisamichi, H.,Kuromitsu, S.,Kurihara, H.,Sakashita, H.,Matsumoto, Y.,Fujita, S.,Niimi, T.
Identification of a key element for hydrogen-bonding patterns between protein kinases and their inhibitors
Proteins, 73:795-801, 2008
Cited by
PubMed Abstract: In this article, we report crystal structures for inhibitor-kinase complexes in which the inhibitor has different binding orientations and hydrogen-bonding patterns with extracellular-signal regulated kinase 2 and insulin receptor tyrosine kinase. Our crystallographic studies, and sequence and structural analyses of 532 coordinates of kinases held in the Protein Data Bank, suggest that the length of the "specificity linker" described here is a key structural element of the hydrogen-bonding patterns between protein kinases and their inhibitors.
PubMed: 18767165
DOI: 10.1002/prot.22207
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.41 Å)
Structure validation

226707

數據於2024-10-30公開中

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