› 2l3p

Solution NMR

Structure of the prolyl cis isomer of the Crk Protein

Released:
DOI: 10.2210/pdb2l3p/pdb
PDB entry 2l3p coloured by chain, ensemble of 20 models, front view.
PDB entry 2l3p coloured by chain, ensemble of 20 models, side view.
PDB entry 2l3p coloured by chain, ensemble of 20 models, top view.
Source organism: Gallus gallus
Primary publication:
Structural basis for regulation of the Crk signaling protein by a proline switch.
Sarkar P, Saleh T, Tzeng SR, Birge RB, Kalodimos CG
OpenAccess logo Nat Chem Biol 7 51-7 (2011)
PMID: 21131971

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-170093 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adapter molecule crk Chain: A
Molecule details ›
Chain: A
Length: 78 amino acids
Theoretical weight: 8.73 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q04929 (Residues: 220-297; Coverage: 26%)
Gene name: CRK
Sequence domains: Variant SH3 domain
Structure domains: SH3 Domains

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

13 review citations

The alphabet of intrinsic disorder: I. Act like a Pro: On the abundance and roles of proline residues in intrinsically disordered proteins.
Theillet et al. (2013)
12 more

2 mentions without citation

Structural basis for regulation of the Crk signaling protein by a proline switch.
Sarkar et al. (2011)
1 more