Crystal structure of the mouse radxin FERM domain complexed with the mouse CD44 cytoplasmic peptide. Determined by X-ray diffraction at 2.1 Å resolution. Released 26 Aug 2008.
Explore 2ZPY in 3D Show helices and sheets RCSB PDB PDBe
2ZPY contains 12 α-helices and 18 β-strands across 2 chains. 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 |
|---|---|---|---|
| β-strand | 5-10 | 6 | 1 |
| β-strand | 15-20 | 6 | 1 |
| β-strand | 25 | 1 | 2 |
| α-helix | 26-36 | 11 | |
| 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 | 89-91 | 3 | |
| α-helix | 96-111 | 16 | |
| α-helix | 119-134 | 16 | |
| α-helix | 155-160 | 6 | |
| α-helix | 165-178 | 14 | |
| α-helix | 184-195 | 12 | |
| β-strand | 204-210 | 7 | 4 |
| β-strand | 215-221 | 7 | 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 | 274-293 | 20 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 300-304 | 5 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Radixin | A | protein | 312 | Mus musculus | P26043 (AlphaFold model) |
| CD44 antigen | B | protein | 20 | P15379 (AlphaFold model) |
>2ZPY_1 Radixin (chains A) GPMPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTW LKLNKKVTQQDVKKENPLQFKFRAKFFPEDVSEELIQEITQRLFFLQVKEAILNDEIYCP PETAVLLASYAVQAKYGDYNKEIHKPGYLANDRLLPQRVLEQHKLTKEQWEERIQNWHEE HRGMLREDSMMEYLKIAQDLEMYGVNYFEIKNKKGTELWLGVDALGLNIYEHDDKLTPKI GFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPD TIEVQQMKAQAR
>2ZPY_2 CD44 antigen (chains B) SRRRCGQKKKLVINGGNGTV
Structural basis for CD44 recognition by ERM proteins. Mori, T., Kitano, K., Terawaki, S. et al. J Biol Chem (2008) 283:29602-29612. DOI 10.1074/jbc.M803606200 · 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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