4h3q

X-ray diffraction
2.2Å resolution

Crystal structure of human ERK2 complexed with a MAPK docking peptide

Released:
Source organism: Homo sapiens
Primary publication:
Protein-peptide complex crystallization: a case study on the ERK2 mitogen-activated protein kinase.
OpenAccess logo Acta Crystallogr. D Biol. Crystallogr. 69 486-9 (2013)
PMID: 23519423

Function and Biology Details

Reactions catalysed:
ATP + a protein = ADP + a phosphoprotein
ATP + L-seryl/L-threonyl/L-tyrosyl-[protein] = ADP + O-phospho-L-seryl/O-phospho-L-threonyl/O-phospho-L-tyrosyl-[protein]

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Mitogen-activated protein kinase 1 Chain: A
Molecule details ›
Chain: A
Length: 362 amino acids
Theoretical weight: 41.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P28482 (Residues: 1-360; Coverage: 100%)
Gene names: ERK2, MAPK1, PRKM1, PRKM2
Sequence domains: Protein kinase domain
Structure domains:
Dual specificity mitogen-activated protein kinase kinase 2 Chain: B
Molecule details ›
Chain: B
Length: 13 amino acids
Theoretical weight: 1.48 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P36507 (Residues: 4-16; Coverage: 3%)
Gene names: MAP2K2, MEK2, MKK2, PRKMK2

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P212121
Unit cell:
a: 41.75Å b: 58.53Å c: 159.15Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.181 0.232
Expression systems:
  • Escherichia coli
  • Not provided