PDBe 1yrk

X-ray diffraction
1.7Å resolution

The C2 Domain of PKC is a new Phospho-Tyrosine Binding Domain

Released:
Source organism: Homo sapiens
Primary publication:
C2 can do it, too.
Cell 121 158-60 (2005)
PMID: 15851022

Function and Biology Details

Reactions catalysed:
ATP + a protein = ADP + a phosphoprotein
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protein kinase C delta type regulatory subunit Chain: A
Molecule details ›
Chain: A
Length: 126 amino acids
Theoretical weight: 14.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: NEW Q05655 (Residues: 1-123; Coverage: 18%)
Gene name: PRKCD
Structure domains: C2 domain
13-residue peptide Chain: B
Molecule details ›
Chain: B
Length: 13 amino acids
Theoretical weight: 1.65 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P212121
Unit cell:
a: 37.272Å b: 41.856Å c: 88.463Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.176 0.221
Expression systems:
  • Escherichia coli
  • Not provided