› 5v60

X-ray diffraction
2.18Å resolution

Phospho-ERK2 bound to AMP-PCP

Released:
DOI: 10.2210/pdb5v60/pdb
PDB entry 5v60 coloured by chain, front view.
PDB entry 5v60 coloured by chain, side view.
PDB entry 5v60 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure-Guided Strategy for the Development of Potent Bivalent ERK Inhibitors.
Lechtenberg BC, Mace PD, Sessions EH, Williamson R, Stalder R, Wallez Y, Roth GP, Riedl SJ, Pasquale EB
ACS Med Chem Lett 8 726-731 (2017)
PMID: 28740606

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: 356 amino acids
Theoretical weight: 41.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P28482 (Residues: 8-360; Coverage: 98%)
Gene names: ERK2, MAPK1, PRKM1, PRKM2
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand ACP 1 x ACP
Ligand GOL 6 x GOL
Ligand MG 2 x MG
2 modified residues:
Ligand TPO 1 x TPO
Ligand PTR 1 x PTR

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P212121
Unit cell:
a: 41.757Å b: 78.516Å c: 152.566Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.191 0.226
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Targeting ERK beyond the boundaries of the kinase active site in melanoma.
Sammons et al. (2019)
4 other articles

3 mentions without citation

Activation loop dynamics are controlled by conformation-selective inhibitors of ERK2.
Pegram et al. (2019)
2 more