The crystal structure of Arc C-lobe. Determined by X-ray diffraction at 2.0 Å resolution. Released 3 Jun 2015.
Explore 4X3X in 3D Show helices and sheets RCSB PDB PDBe
4X3X contains 6 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 | 279-288 | 10 | |
| α-helix | 298-312 | 15 | |
| α-helix | 318-327 | 10 | |
| α-helix | 331-337 | 7 | |
| α-helix | 341-342 | 2 | |
| α-helix | 345-359 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Activity-regulated cytoskeleton-associated protein | A | protein | 90 | Rattus norvegicus | Q63053 (AlphaFold model) |
>4X3X_1 Activity-regulated cytoskeleton-associated protein (chains A) GPLGSTLSREAIQRELDLPQKQGEPLDQFLWRKRDLYQTLYVDAEEEEIIQYVVGTLQPK FKRFLRHPLPKTLEQLIQRGMEVQDGLEQA
Structural basis of arc binding to synaptic proteins: implications for cognitive disease. Zhang, W., Wu, J., Ward, M.D. et al. Neuron (2015) 86:490-500. DOI 10.1016/j.neuron.2015.03.030 · PubMed
Other PDB entries of the same protein (UniProt Q63053 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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