PDBe 2fys

X-ray diffraction
2.5Å resolution

Crystal structure of Erk2 complex with KIM peptide derived from MKP3

Released:
Source organism: Rattus norvegicus
Primary publication:
Structural basis of docking interactions between ERK2 and MAP kinase phosphatase 3.
Proc. Natl. Acad. Sci. U.S.A. 103 5326-31 (2006)
PMID: 16567630

Function and Biology Details

Reactions catalysed:
ATP + a protein = ADP + a phosphoprotein. 
[a protein]-serine/threonine phosphate + H(2)O = [a protein]- serine/threonine + phosphate. 
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate. 
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Mitogen-activated protein kinase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 364 amino acids
Theoretical weight: 42.16 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P63086 (Residues: 2-358; Coverage: 100%)
Gene names: Erk2, Mapk, Mapk1, Prkm1
Sequence domains: Protein kinase domain
Structure domains:
Dual specificity protein phosphatase 6 Chains: C, D
Molecule details ›
Chains: C, D
Length: 17 amino acids
Theoretical weight: 1.94 KDa
Source organism: Rattus norvegicus
Expression system: Not provided
UniProt:
  • Canonical: Q64346 (Residues: 60-76; Coverage: 5%)
Gene names: Dusp6, Mkp3

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P21
Unit cell:
a: 57.377Å b: 67.478Å c: 86.605Å
α: 90° β: 99.55° γ: 90°
R-values:
R R work R free
0.174 0.174 0.266
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided