Solution structure of the capsid domain from the activity-regulated cytoskeleton-associated protein, Arc. Determined by solution NMR. Released 22 May 2019.
Explore 6GSE in 3D Show helices and sheets RCSB PDB PDBe
6GSE contains 12 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 | 211-214 | 4 | |
| α-helix | 218-231 | 14 | |
| α-helix | 235-245 | 11 | |
| α-helix | 249-257 | 9 | |
| α-helix | 264-288 | 25 | |
| α-helix | 290-293 | 4 | |
| α-helix | 298-312 | 15 | |
| α-helix | 318-325 | 8 | |
| α-helix | 326-328 | 3 | |
| α-helix | 331-335 | 5 | |
| α-helix | 340-342 | 3 | |
| α-helix | 345-360 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Activity-regulated cytoskeleton-associated protein | A | protein | 159 | Rattus norvegicus | Q63053 (AlphaFold model) |
>6GSE_1 Activity-regulated cytoskeleton-associated protein (chains A) SPGLDTQIFEDPREFLSHLEEYLRQVGGSEEYWLSQIQNHMNGPAKKWWEFKQGSVKNWV EFKKEFLQYSEGTLSREAIQRELDLPQKQGEPLDQFLWRKRDLYQTLYVDAEEEEIIQYV VGTLQPKFKRFLRHPLPKTLEQLIQRGMEVQDGLEQAAE
The Capsid Domain of Arc Changes Its Oligomerization Propensity through Direct Interaction with the NMDA Receptor. Nielsen, L.D., Pedersen, C.P., Erlendsson, S. et al. Structure (2019) 27:1071-1081.e5. DOI 10.1016/j.str.2019.04.001 · PubMed
Other PDB entries of the same protein (UniProt Q63053 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 6GSE 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.