› 4zzm

X-ray diffraction
1.89Å resolution

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: 350 amino acids
Theoretical weight: 40.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P28482 (Residues: 11-360; Coverage: 97%)
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 CQ6 1 x CQ6
1 modified residue:
Ligand CME 1 x CME

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P21
Unit cell:
a: 48.88Å b: 70.31Å c: 60.41Å
α: 90° β: 109.12° γ: 90°
R-values:
R R work R free
0.21 0.207 0.254
Expression system: Escherichia coli

Quick links

Citations

6 review citations

New drug design with covalent modifiers.
Adeniyi et al. (2016)
5 more

3 mentions without citation

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