› 3eac

X-ray diffraction
1.37Å resolution

Crystal structure of SH2 domain of Human Csk (carboxyl-terminal src kinase), Oxidized form.

Released:
DOI: 10.2210/pdb3eac/pdb
PDB entry 3eac coloured by chain, front view.
PDB entry 3eac coloured by chain, side view.
PDB entry 3eac coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Combining biophysical methods to analyze the disulfide bond in SH2 domain of C-terminal Src kinase.
Liu D, Cowburn D
Biophys Rep 2 33-43 (2016)
PMID: 27819029

Function and Biology Details

Reaction catalysed: 
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
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-154353 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein kinase CSK Chain: A
Molecule details ›
Chain: A
Length: 106 amino acids
Theoretical weight: 12.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P41240 (Residues: 73-178; Coverage: 24%)
Gene name: CSK
Sequence domains: SH2 domain
Structure domains: SH2 domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4C
Spacegroup: P212121
Unit cell:
a: 37.114Å b: 48.025Å c: 49.866Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.209 0.217
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Cysteines and Disulfide Bonds as Structure-Forming Units: Insights From Different Domains of Life and the Potential for Characterization by NMR.
Wiedemann et al. (2020)
3 more

4 mentions without citation

Combining biophysical methods to analyze the disulfide bond in SH2 domain of C-terminal Src kinase.
Liu et al. (2016)
3 more