› 6ots

X-ray diffraction
2.1Å resolution

Rat ERK2 E320K

Released:
DOI: 10.2210/pdb6ots/pdb
PDB entry 6ots coloured by chain, front view.
PDB entry 6ots coloured by chain, side view.
PDB entry 6ots coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Functional divergence caused by mutations in an energetic hotspot in ERK2.
Taylor CA, Cormier KW, Keenan SE, Earnest S, Stippec S, Wichaidit C, Juang YC, Wang J, Shvartsman SY, Goldsmith EJ, Cobb MH
Proc Natl Acad Sci U S A 116 15514-15523 (2019)
PMID: 31296562

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-158941 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mitogen-activated protein kinase 1 Chain: A
Molecule details ›
Chain: A
Length: 358 amino acids
Theoretical weight: 41.33 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P63086 (Residues: 1-358; Coverage: 100%)
Gene names: Erk2, Mapk, Mapk1, Prkm1
Sequence domains: Protein kinase domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2
Unit cell:
a: 182.315Å b: 41.948Å c: 50.344Å
α: 90° β: 105.86° γ: 90°
R-values:
R R work R free
0.233 0.231 0.264
Expression system: Escherichia coli BL21

Quick links

Citations

3 review citations

Mutations That Confer Drug-Resistance, Oncogenicity and Intrinsic Activity on the ERK MAP Kinases-Current State of the Art.
Smorodinsky-Atias et al. (2020)
2 more

1 mention without citation

Functional divergence caused by mutations in an energetic hotspot in ERK2.
Taylor et al. (2019)