› 2fk9

X-ray diffraction
1.75Å resolution

Human protein kinase C, eta

Released:
DOI: 10.2210/pdb2fk9/pdb
PDB entry 2fk9 coloured by chain, front view.
PDB entry 2fk9 coloured by chain, side view.
PDB entry 2fk9 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of human protein kinase C eta (PKCeta) C2 domain and identification of phosphorylation sites.
Littler DR, Walker JR, She YM, Finerty PJ, Newman EM, Dhe-Paganon S
Biochem Biophys Res Commun 349 1182-9 (2006)
PMID: 16973127

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150275 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein kinase C eta type Chain: A
Molecule details ›
Chain: A
Length: 157 amino acids
Theoretical weight: 17.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P24723 (Residues: 1-138; Coverage: 20%)
Gene names: PKCL, PRKCH, PRKCL
Sequence domains: C2 domain
Structure domains: C2 domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E
Spacegroup: P212121
Unit cell:
a: 45.007Å b: 49.404Å c: 67.508Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.178 0.215
Expression system: Escherichia coli BL21

Quick links

Citations

5 review citations

Protein kinase C: perfectly balanced.
Newton AC. (2018)
4 more

3 mentions without citation

Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination.
Vedadi et al. (2006)
2 more