Crystal structure of the radixin ferm domain. Determined by X-ray diffraction at 2.8 Å resolution. Released 20 Sept 2000.
Explore 1GC7 in 3D Show helices and sheets RCSB PDB PDBe
1GC7 contains 13 α-helices and 17 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 | 2-4 | 3 | |
| β-strand | 5-10 | 6 | 1 |
| β-strand | 15-20 | 6 | 1 |
| β-strand | 25 | 1 | 2 |
| α-helix | 26-37 | 12 | |
| α-helix | 42-44 | 3 | |
| β-strand | 45-50 | 6 | 1 |
| β-strand | 51 | 1 | 3 |
| β-strand | 56-58 | 3 | 1 |
| α-helix | 59-60 | 2 | |
| β-strand | 64 | 1 | 2 |
| α-helix | 65-67 | 3 | |
| β-strand | 70 | 1 | 3 |
| β-strand | 76-82 | 7 | 1 |
| α-helix | 89-92 | 4 | |
| α-helix | 96-111 | 16 | |
| α-helix | 119-134 | 16 | |
| α-helix | 155-158 | 4 | |
| α-helix | 165-178 | 14 | |
| α-helix | 184-195 | 12 | |
| β-strand | 204-210 | 7 | 4 |
| β-strand | 215-220 | 6 | 4 |
| β-strand | 224-229 | 6 | 4 |
| β-strand | 232 | 1 | 4 |
| β-strand | 238-241 | 4 | 4 |
| α-helix | 242-244 | 3 | |
| β-strand | 245-251 | 7 | 4 |
| β-strand | 254-259 | 6 | 4 |
| β-strand | 267-270 | 4 | 4 |
| α-helix | 274-295 | 22 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Radixin | A | protein | 297 | Mus musculus | P26043 (AlphaFold model) |
>1GC7_1 RADIXIN (chains A) MPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTWLK LNKKVTQQDVKKENPLQFKFRAKFFPEDVSEELIQEITQRLFFLQVKEAILNDEIYCPPE TAVLLASYAVQAKYGDYNKEIHKPGYLANDRLLPQRVLEQHKLTKEQWEERIQNWHEEHR GMLREDSMMEYLKIAQDLEMYGVNYFEIKNKKGTELWLGVDALGLNIYEHDDKLTPKIGF PWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKP
Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain. Hamada, K., Shimizu, T., Matsui, T. et al. EMBO J (2000) 19:4449-4462. DOI 10.1093/emboj/19.17.4449 · PubMed
Other PDB entries of the same protein (UniProt P26043 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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