› 2kg5

Solution NMR

NMR Solution structure of ARAP3-SAM

Released:
DOI: 10.2210/pdb2kg5/pdb
PDB entry 2kg5 coloured by chain, ensemble of 20 models, front view.
PDB entry 2kg5 coloured by chain, ensemble of 20 models, side view.
PDB entry 2kg5 coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
The Sam domain of the lipid phosphatase Ship2 adopts a common model to interact with Arap3-Sam and EphA2-Sam.
Leone M, Cellitti J, Pellecchia M
OpenAccess logo BMC Struct Biol 9 59 (2009)
PMID: 19765305

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-186757 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 3 Chain: A
Molecule details ›
Chain: A
Length: 100 amino acids
Theoretical weight: 10.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8WWN8 (Residues: 1-80; Coverage: 5%)
Gene names: ARAP3, CENTD3
Sequence domains: SAM domain (Sterile alpha motif)
Structure domains: Transcription Factor, Ets-1

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

6 review citations

Survey of the year 2009: applications of isothermal titration calorimetry.
Falconer et al. (2011)
5 more

3 mentions without citation

The Sam domain of the lipid phosphatase Ship2 adopts a common model to interact with Arap3-Sam and EphA2-Sam.
Leone et al. (2009)
2 more