› 2z7l

X-ray diffraction
2.41Å resolution

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

Released:
DOI: 10.2210/pdb2z7l/pdb
PDB entry 2z7l coloured by chain, front view.
PDB entry 2z7l coloured by chain, side view.
PDB entry 2z7l coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Identification of a key element for hydrogen-bonding patterns between protein kinases and their inhibitors.
Katayama N, Orita M, Yamaguchi T, Hisamichi H, Kuromitsu S, Kurihara H, Sakashita H, Matsumoto Y, Fujita S, Niimi T
Proteins 73 795-801 (2008)
PMID: 18767165

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158941 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mitogen-activated protein kinase 1 Chain: A
Molecule details ›
Chain: A
Length: 366 amino acids
Theoretical weight: 42.36 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P63086 (Residues: 1-358; Coverage: 100%)
Gene names: Erk2, Mapk, Mapk1, Prkm1
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand SO4 1 x SO4
Ligand S91 1 x S91
Ligand BME 3 x BME
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 48.873Å b: 69.962Å c: 60.775Å
α: 90° β: 109.58° γ: 90°
R-values:
R R work R free
0.223 0.223 0.276
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Development of extracellular signal-regulated kinase inhibitors.
Burkhard et al. (2009)
3 other articles

2 mentions without citation

Identification of gefitinib off-targets using a structure-based systems biology approach; their validation with reverse docking and retrospective data mining.
Verma et al. (2016)
1 more