Mu2 subunit of the clathrin adaptor complex AP2 in complex with IRS-1 Y658 peptide. Determined by X-ray diffraction at 2.6 Å resolution. Released 6 Dec 2017.
Explore 5WRM in 3D Show helices and sheets RCSB PDB PDBe
5WRM contains 4 α-helices and 21 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 | 172-185 | 14 | 1 |
| β-strand | 191-205 | 15 | 1 |
| β-strand | 211-216 | 6 | 2 |
| β-strand | 218 | 1 | 3 |
| β-strand | 241 | 1 | 3 |
| β-strand | 245-248 | 4 | 1 |
| β-strand | 252 | 1 | 2 |
| α-helix | 254-259 | 6 | |
| β-strand | 263-265 | 3 | 2 |
| α-helix | 267-268 | 2 | |
| β-strand | 270-279 | 10 | 1 |
| β-strand | 287-292 | 6 | 4 |
| β-strand | 295-296 | 2 | 4 |
| β-strand | 300-309 | 10 | 4 |
| β-strand | 316-325 | 10 | 1 |
| β-strand | 330-337 | 8 | 4 |
| β-strand | 341-345 | 5 | 1 |
| β-strand | 350-359 | 10 | 1 |
| β-strand | 363-372 | 10 | 4 |
| α-helix | 384-385 | 2 | |
| β-strand | 386-392 | 7 | 1 |
| β-strand | 401-407 | 7 | 2 |
| α-helix | 415-417 | 3 | |
| β-strand | 419-433 | 15 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-4 | 2 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| AP-2 complex subunit mu | A | protein | 278 | Rattus norvegicus | P84092 (AlphaFold model) |
| Insulin receptor substrate 1 | P | protein | 8 | Rattus norvegicus | P35570 (AlphaFold model) |
>5WRM_1 AP-2 complex subunit mu (chains A) QIGWRREGIKYRRNELFLDVLESVNLLMSPQGQVLSAHVSGRVVMKSYLSGMPECKFGMN DKIVIEKQGKGTADETSKSGKQSIAIDDCTFHQCVRLSKFDSERSISFIPPDGEFELMRY RTTKDIILPFRVIPLVREVGRTKLEVKVVIKSNFKPSLLAQKIEVRIPTPLNTSGVQVIC MKGKAKYKASENAIVWKIKRMAGMKESQISAEIELLPTNDKKKWARPPISMNFEVPFAPS GLKVRYLKVFEPKLNYSDHDVIKWVRYIGRSGIYETRC
>5WRM_2 Insulin receptor substrate 1 (chains P) GYMMMSPS
IRS-1 acts as an endocytic regulator of IGF-I receptor to facilitate sustained IGF signaling. Yoneyama, Y., Lanzerstorfer, P., Niwa, H. et al. Elife (2018) 7. DOI 10.7554/eLife.32893 · PubMed
Other PDB entries of the same protein (UniProt P84092 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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