NMR Solution structure of ARAP3-SAM. Determined by solution NMR. Released 17 Nov 2009.
Explore 2KG5 in 3D Show helices and sheets RCSB PDB PDBe
2KG5 contains 7 α-helices and 2 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 28 | 1 | 1 |
| α-helix | 29-33 | 5 | |
| α-helix | 34-36 | 3 | |
| α-helix | 39-41 | 3 | |
| α-helix | 42-47 | 6 | |
| β-strand | 52 | 1 | 1 |
| α-helix | 53-56 | 4 | |
| α-helix | 61-67 | 7 | |
| α-helix | 72-82 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Arf-GAP, Rho-GAP domain, ANK repeat and PH domain-containing protein 3 | A | protein | 100 | Homo sapiens | Q8WWN8 (AlphaFold model) |
>2KG5_1 Arf-GAP, Rho-GAP domain, ANK repeat and PH domain-containing protein 3 (chains A) MGSSHHHHHHSSGLVPRGSHMAAPQDLDIAVWLATVHLEQYADTFRRHGLATAGAARGLG HEELKQLGISATGHRKRILRLLQTGTEEGSLDPKSDSAME
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. BMC Struct Biol (2009) 9:59-59. DOI 10.1186/1472-6807-9-59 · PubMed
Other PDB entries of the same protein (UniProt Q8WWN8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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