7OI5: AP2 Mu2 - FCHO2 chimera

Crystal structure of AP2 Mu2 - FCHO2 chimera (GST cleaved). Determined by X-ray diffraction at 2.61 Å resolution. Released 1 Jun 2022.

Method
X-ray diffraction
Resolution
2.61 Å
Organisms
Rattus norvegicus, Homo sapiens
Chains
2
Atoms
4,669
Mol. weight
79.03 kDa
Released
1 Jun 2022

Explore 7OI5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7OI5 contains 10 α-helices and 41 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.

Chain B: 5 helices, 20 β-strands

ElementResiduesLengthSheet
β-strand16711
β-strand172-185142
β-strand191-205152
β-strand211-21663
α-helix221-2233
β-strand245-24842
β-strand25213
α-helix254-2607
β-strand263-26533
α-helix267-2682
β-strand270-279102
β-strand287-296104
β-strand300-309104
β-strand316-325102
β-strand330-33784
β-strand341-34552
β-strand350-359102
β-strand365-37284
α-helix384-3852
β-strand386-39272
β-strand401-40883
β-strand413-41423
α-helix415-4173
β-strand419-433152
β-strand48311
Chain D: 5 helices, 21 β-strands
ElementResiduesLengthSheet
β-strand16715
β-strand172-185146
β-strand191-205156
β-strand212-21547
β-strand245-24846
β-strand25217
α-helix254-2596
β-strand263-26537
α-helix267-2682
β-strand270-279106
β-strand287-296108
β-strand300-309108
β-strand316-325106
β-strand330-33788
β-strand341-34556
β-strand350-359106
β-strand363-372108
α-helix384-3852
β-strand386-39276
β-strand403-40537
β-strand407-40829
β-strand413-41429
α-helix415-4173
β-strand419-433156
β-strand48315
α-helix486-4883

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
AP-2 complex subunit mu,F-BAR domain only protein 2B, Dprotein359Rattus norvegicus, Homo sapiensP84092 (AlphaFold model), Q0JRZ9 (AlphaFold model)
Sequence of entity 1 (B, D), FASTA
>7OI5_1 AP-2 complex subunit mu,F-BAR domain only protein 2 (chains B, D)
PGIHMQIGWRREGIKYRRNELFLDVLESVNLLMSPQGQVLSAHVSGRVVMKSYLSGMPEC
KFGMNDKIVIEKQGKGTADETSKSGKQSIAIDDCTFHQCVRLSKFDSERSISFIPPDGEF
ELMRYRTTKDIILPFRVIPLVREVGRTKLEVKVVIKSNFKPSLLAQKIEVRIPTPLNTSG
VQVICMKGKAKYKASENAIVWKIKRMAGMKESQISAEIELLPTNDKKKWARPPISMNFEV
PFAPSGLKVRYLKVFEPKLNYSDHDVIKWVRYIGRSGIYETRCGASGSAGSAGPSGAGSA
GSAGPSAGSAGSAGSGSAGSAPGPDVDEEGYSIKPETNQNDTKENHFYSSSDSDSEDEE

Primary citation

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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