2KG5
NMR Solution structure of ARAP3-SAM
Summary for 2KG5
| Entry DOI | 10.2210/pdb2kg5/pdb |
| Descriptor | Arf-GAP, Rho-GAP domain, ANK repeat and PH domain-containing protein 3 (1 entity in total) |
| Functional Keywords | sam domain, helix bundle, cell membrane, cell projection, cytoplasm, cytoskeleton, gtpase activation, membrane, metal-binding, phosphoprotein, polymorphism, zinc, zinc-finger, signaling protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm (By similarity): Q8WWN8 |
| Total number of polymer chains | 1 |
| Total formula weight | 10864.16 |
| Authors | Leone, M.,Pellecchia, M. (deposition date: 2009-03-05, release date: 2009-11-17, Last modification date: 2024-05-22) |
| Primary citation | Leone, M.,Cellitti, J.,Pellecchia, M. The Sam domain of the lipid phosphatase Ship2 adopts a common model to interact with Arap3-Sam and EphA2-Sam. Bmc Struct.Biol., 9:59-59, 2009 Cited by PubMed Abstract: Sterile alpha motif (Sam) domains are small protein modules that can be involved in homotypic or heterotypic associations and exhibit different functions. Previous studies have demonstrated that the Sam domain of the lipid phosphatase Ship2 can hetero-dimerize with the Sam domain of the PI3K effector protein Arap3. PubMed: 19765305DOI: 10.1186/1472-6807-9-59 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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