Solution structure of the C-terminal SH3 domain of c-CrkII. Determined by solution NMR. Released 1 Aug 2006.
Explore 2GGR in 3D Show helices and sheets RCSB PDB PDBe
2GGR contains 2 α-helices and 5 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 | 237 | 1 | |
| β-strand | 238-242 | 5 | 1 |
| β-strand | 262-268 | 7 | 1 |
| β-strand | 275-279 | 5 | 1 |
| β-strand | 282-286 | 5 | 1 |
| α-helix | 288-290 | 3 | |
| β-strand | 291-294 | 4 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Proto-oncogene C-crk | A | protein | 76 | Mus musculus | Q64010 (AlphaFold model) |
>2GGR_1 Proto-oncogene C-crk (chains A) GLPNLQNGPIYARVIQKRVPNAYDKTALALEVGELVKVTKINVSGQWEGECNGKRGHFPF THVRLLDQQNPDEDFS
Solution Structure and Folding Characteristics of the C-Terminal SH3 Domain of c-Crk-II. Muralidharan, V., Dutta, K., Cho, J. et al. Biochemistry (2006) 45:8874-8884. DOI 10.1021/bi060590z · PubMed
Other PDB entries of the same protein (UniProt Q64010 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2GGR 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.