Crystal structure of AP2 Mu2 - FCHO2 chimera (His6-tagged). Determined by X-ray diffraction at 2.27 Å resolution. Released 1 Jun 2022.
Explore 7OHZ in 3D Show helices and sheets RCSB PDB PDBe
7OHZ contains 14 α-helices and 38 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 |
|---|---|---|---|
| α-helix | 155-156 | 2 | |
| β-strand | 172-185 | 14 | 5 |
| β-strand | 191-205 | 15 | 5 |
| β-strand | 211-216 | 6 | 6 |
| β-strand | 246-248 | 3 | 5 |
| α-helix | 254-260 | 7 | |
| β-strand | 264-265 | 2 | 6 |
| α-helix | 267-268 | 2 | |
| β-strand | 270-279 | 10 | 5 |
| β-strand | 287-296 | 10 | 7 |
| β-strand | 300-309 | 10 | 7 |
| β-strand | 316-325 | 10 | 5 |
| β-strand | 330-337 | 8 | 7 |
| β-strand | 341-345 | 5 | 5 |
| β-strand | 350-359 | 10 | 5 |
| β-strand | 362-372 | 11 | 7 |
| α-helix | 383-385 | 3 | |
| β-strand | 386-392 | 7 | 5 |
| β-strand | 401-408 | 8 | 6 |
| β-strand | 413-414 | 2 | 6 |
| α-helix | 415-417 | 3 | |
| β-strand | 419-433 | 15 | 5 |
| β-strand | 478 | 1 | 8 |
| α-helix | 483 | 1 | |
| β-strand | 484 | 1 | 8 |
| α-helix | 485-487 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 153-156 | 4 | |
| β-strand | 172-185 | 14 | 1 |
| β-strand | 191-205 | 15 | 1 |
| β-strand | 211-216 | 6 | 2 |
| β-strand | 245-248 | 4 | 1 |
| α-helix | 254-259 | 6 | |
| β-strand | 263-265 | 3 | 2 |
| α-helix | 267-268 | 2 | |
| β-strand | 270-279 | 10 | 1 |
| β-strand | 287-296 | 10 | 3 |
| β-strand | 300-309 | 10 | 3 |
| β-strand | 316-325 | 10 | 1 |
| β-strand | 330-337 | 8 | 3 |
| β-strand | 341-345 | 5 | 1 |
| β-strand | 350-359 | 10 | 1 |
| β-strand | 362-372 | 11 | 3 |
| α-helix | 379-381 | 3 | |
| α-helix | 383-385 | 3 | |
| β-strand | 386-392 | 7 | 1 |
| β-strand | 401-408 | 8 | 2 |
| β-strand | 413-414 | 2 | 2 |
| α-helix | 415-417 | 3 | |
| β-strand | 419-433 | 15 | 1 |
| β-strand | 478 | 1 | 4 |
| β-strand | 484 | 1 | 4 |
| α-helix | 485-486 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| AP-2 complex subunit mu,F-BAR domain only protein 2 | A, B | protein | 361 | Rattus norvegicus, Homo sapiens | P84092 (AlphaFold model), Q0JRZ9 (AlphaFold model) |
>7OHZ_1 AP-2 complex subunit mu,F-BAR domain only protein 2 (chains A, B) MHHHHHHQIGWRREGIKYRRNELFLDVLESVNLLMSPQGQVLSAHVSGRVVMKSYLSGMP ECKFGMNDKIVIEKQGKGTADETSKSGKQSIAIDDCTFHQCVRLSKFDSERSISFIPPDG EFELMRYRTTKDIILPFRVIPLVREVGRTKLEVKVVIKSNFKPSLLAQKIEVRIPTPLNT SGVQVICMKGKAKYKASENAIVWKIKRMAGMKESQISAEIELLPTNDKKKWARPPISMNF EVPFAPSGLKVRYLKVFEPKLNYSDHDVIKWVRYIGRSGIYETRCGASGSAGSAGPSGAG SAGSAGPSAGSAGSAGSGSAGSAPGPDVDEEGYSIKPETNQNDTKENHFYSSSDSDSEDE E
FCHO controls AP2's initiating role in endocytosis through a PtdIns(4,5)P 2 -dependent switch. Zaccai, N.R., Kadlecova, Z., Dickson, V.K. et al. Sci Adv (2022) 8:eabn2018-eabn2018. DOI 10.1126/sciadv.abn2018 · 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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