4iz5

X-ray diffraction
3.19Å resolution

Structure of the complex between ERK2 phosphomimetic mutant and PEA-15

Released:

Function and Biology Details

Reaction catalysed:
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 356 amino acids
Theoretical weight: 41.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P28482 (Residues: 8-360; Coverage: 98%)
Gene names: ERK2, MAPK1, PRKM1, PRKM2
Sequence domains: Protein kinase domain
Structure domains:
Astrocytic phosphoprotein PEA-15 Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 133 amino acids
Theoretical weight: 15.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q15121 (Residues: 1-130; Coverage: 100%)
Gene name: PEA15
Sequence domains: Death effector domain
Structure domains: Death Domain, Fas

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P21
Unit cell:
a: 80.801Å b: 149.129Å c: 98.869Å
α: 90° β: 90.41° γ: 90°
R-values:
R R work R free
0.245 0.243 0.292
Expression system: Escherichia coli BL21(DE3)