› 5o2p

Solution NMR

p130Cas SH3 domain PTP-PEST peptide chimera

Released:
DOI: 10.2210/pdb5o2p/pdb
PDB entry 5o2p coloured by chain, ensemble of 40 models, front view.
PDB entry 5o2p coloured by chain, ensemble of 40 models, side view.
PDB entry 5o2p 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

Reaction catalysed: 
Protein tyrosine phosphate + H(2)O = protein 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-157581 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Breast cancer anti-estrogen resistance protein 1; Tyrosine-protein phosphatase non-receptor type 12 Chain: A
Molecule details ›
Chain: A
Length: 100 amino acids
Theoretical weight: 10.85 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P56945 (Residues: 4-73; Coverage: 8%)
  • Canonical: Q05209 (Residues: 328-344; Coverage: 2%)
Gene names: BCAR1, CAS, CASS1, CRKAS, PTPN12
Sequence domains: SH3 domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 92%
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

1 mention without citation

Ins and outs of AlphaFold2 transmembrane protein structure predictions.
Hegedűs et al. (2022)