› 2ojg

X-ray diffraction
2Å resolution

Crystal structure of ERK2 in complex with N,N-dimethyl-4-(4-phenyl-1H-pyrazol-3-yl)-1H-pyrrole-2-carboxamide

Released:
DOI: 10.2210/pdb2ojg/pdb
PDB entry 2ojg coloured by chain, front view.
PDB entry 2ojg coloured by chain, side view.
PDB entry 2ojg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Flipped out: structure-guided design of selective pyrazolylpyrrole ERK inhibitors.
Aronov AM, Baker C, Bemis GW, Cao J, Chen G, Ford PJ, Germann UA, Green J, Hale MR, Jacobs M, Janetka JW, Maltais F, Martinez-Botella G, Namchuk MN, Straub J, Tang Q, Xie X
J Med Chem 50 1280-7 (2007)
PMID: 17300186

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151230 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mitogen-activated protein kinase 1 Chain: A
Molecule details ›
Chain: A
Length: 380 amino acids
Theoretical weight: 43.62 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P28482 (Residues: 2-360; Coverage: 100%)
Gene names: ERK2, MAPK1, PRKM1, PRKM2
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SO4 1 x SO4
Ligand 19A 1 x 19A
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 48.665Å b: 70.776Å c: 60.141Å
α: 90° β: 109.03° γ: 90°
R-values:
R R work R free
0.233 0.216 0.26
Expression system: Escherichia coli

Quick links

Citations

6 review citations

ERK1/2 MAP kinases: structure, function, and regulation.
Roskoski R. (2012)
5 more

19 mentions without citation

Development of small molecule extracellular signal-regulated kinases (ERKs) inhibitors for cancer therapy.
Pan et al. (2022)
18 more