› 5o2q

Solution NMR

p130Cas SH3 domain Vinculin peptide chimera

Released:
DOI: 10.2210/pdb5o2q/pdb
PDB entry 5o2q coloured by chain, ensemble of 40 models, front view.
PDB entry 5o2q coloured by chain, ensemble of 40 models, side view.
PDB entry 5o2q coloured by chain, ensemble of 40 models, top view.
Source organism: Homo sapiens
Primary publication:
Structural characterization of CAS SH3 domain selectivity and regulation reveals new CAS interaction partners.
Gemperle J, Hexnerová R, Lepšík M, Tesina P, Dibus M, Novotný M, Brábek J, Veverka V, Rosel D
Sci Rep 7 8057 (2017)
PMID: 28808245

Function and Biology Details

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-148316 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Breast cancer anti-estrogen resistance protein 1; Vinculin Chain: A
Molecule details ›
Chain: A
Length: 99 amino acids
Theoretical weight: 10.62 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P56945 (Residues: 4-73; Coverage: 8%)
  • Canonical: P18206 (Residues: 854-870; Coverage: 2%)
Gene names: BCAR1, CAS, CASS1, CRKAS, VCL
Sequence domains: SH3 domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 93%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

1 review citation

The TFIIS N-terminal domain (TND): a transcription assembly module at the interface of order and disorder.
Cermakova et al. (2023)
6 other articles