› 2b86

Solution NMR

Solution structure of the first Src homology 3 domain of Nck2

Released:
DOI: 10.2210/pdb2b86/pdb
PDB entry 2b86 coloured by chain, ensemble of 30 models, front view.
PDB entry 2b86 coloured by chain, ensemble of 30 models, side view.
PDB entry 2b86 coloured by chain, ensemble of 30 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure of the first SRC homology 3 domain of human Nck2.
Park S, Takeuchi K, Wagner G
J Biomol NMR 34 203-8 (2006)
PMID: 16604428

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-129043 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytoplasmic protein NCK2 Chain: A
Molecule details ›
Chain: A
Length: 67 amino acids
Theoretical weight: 8.25 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O43639 (Residues: 1-61; Coverage: 16%)
Gene names: GRB4, NCK2
Sequence domains: SH3 domain
Structure domains: SH3 Domains

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing tortion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

6 citation in other articles

Reciprocal regulation of SH3 and SH2 domain binding via tyrosine phosphorylation of a common site in CD3epsilon.
Kesti et al. (2007)
5 more

7 mentions without citation

Why do proteins aggregate? "Intrinsically insoluble proteins" and "dark mediators" revealed by studies on "insoluble proteins" solubilized in pure water.
Song J. (2013)
6 more