Solution structure of DLC1-SAM. Determined by solution NMR. Released 20 Oct 2009.
Explore 2KAP in 3D Show helices and sheets RCSB PDB PDBe
2KAP contains 4 α-helices and 0 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 |
|---|---|---|---|
| α-helix | 2-10 | 9 | |
| α-helix | 13-20 | 8 | |
| α-helix | 28-34 | 7 | |
| α-helix | 40-57 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Rho GTPase-activating protein 7 | A | protein | 60 | Homo sapiens | Q96QB1 (AlphaFold model) |
>2KAP_1 Rho GTPase-activating protein 7 (chains A) KEACDWLRATGFPQYAQLYEDFLFPIDISLVKREHDFLDRDAIEALCRRLNTLNKCAVMK
Characterization of DLC1-SAM equilibrium unfolding at the amino acid residue level. Yang, S., Noble, C.G., Yang, D. Biochemistry (2009) 48:4040-4049. DOI 10.1021/bi9000936 · PubMed
Other PDB entries of the same protein (UniProt Q96QB1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2KAP directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.