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 DOI | 10.2210/pdb2z7l/pdb |
Descriptor | Mitogen-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 Keywords | transferase, serine/threonine-protein kinase, atp-binding, cell cycle, phosphorylation, acetylation, nucleotide-binding |
Biological source | Rattus norvegicus (Rat) |
Total number of polymer chains | 1 |
Total formula weight | 43069.56 |
Authors | Katayama, N.,Kurihara, H. (deposition date: 2007-08-27, release date: 2008-08-12, Last modification date: 2023-11-01) |
Primary citation | Katayama, 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: 18767165DOI: 10.1002/prot.22207 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.41 Å) |
Structure validation
Download full validation report