7OIQ: AP2 Mu2

Crystal structure of AP2 Mu2 in complex with FCHO2 WxxPhi motif (C2 crystal form). Determined by X-ray diffraction at 1.85 Å resolution. Released 1 Jun 2022.

Method
X-ray diffraction
Resolution
1.85 Å
Organisms
Rattus norvegicus, Homo sapiens
Chains
4
Atoms
4,604
Mol. weight
67.98 kDa
Released
1 Jun 2022

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

Secondary structure: helices and β-sheets

7OIQ contains 10 α-helices and 39 β-strands across 4 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 AAA: 4 helices, 17 β-strands

ElementResiduesLengthSheet
β-strand172-185141
β-strand191-205151
β-strand211-21662
β-strand244-24851
β-strand25312
β-strand262-26542
α-helix267-2682
β-strand270-279101
β-strand287-296103
β-strand300-309103
β-strand316-325101
β-strand330-33783
β-strand341-34551
α-helix346-3483
β-strand350-359101
β-strand363-372103
α-helix384-3852
β-strand386-39271
β-strand401-40772
α-helix415-4173
β-strand419-433151
Chain BBB: 4 helices, 20 β-strands
ElementResiduesLengthSheet
β-strand172-185144
β-strand191-205154
β-strand211-21665
β-strand21816
β-strand24116
β-strand245-24844
β-strand253-25425
β-strand263-26535
α-helix267-2682
β-strand270-279104
β-strand287-296107
β-strand300-309107
β-strand316-325104
β-strand330-33787
β-strand341-34554
α-helix346-3483
β-strand350-359104
β-strand363-372107
α-helix384-3852
β-strand386-39274
β-strand401-40885
β-strand413-41425
α-helix415-4173
β-strand419-433154
Chains CCC and DDD: 1 helix, 1 β-strand
ElementResiduesLengthSheet
α-helix108-1103
β-strand112-11324

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
AP-2 complex subunit muAAA, BBBprotein285Rattus norvegicusP84092 (AlphaFold model)
F-BAR domain only protein 2CCC, DDDprotein11Homo sapiensQ0JRZ9 (AlphaFold model)
Sequence of entity 1 (AAA, BBB), FASTA
>7OIQ_1 AP-2 complex subunit mu (chains AAA, BBB)
MHHHHHHQIGWRREGIKYRRNELFLDVLESVNLLMSPQGQVLSAHVSGRVVMKSYLSGMP
ECKFGMNDKIVIEKQGKGTADETSKSGKQSIAIDDCTFHQCVRLSKFDSERSISFIPPDG
EFELMRYRTTKDIILPFRVIPLVREVGRTKLEVKVVIKSNFKPSLLAQKIEVRIPTPLNT
SGVQVICMKGKAKYKASENAIVWKIKRMAGMKESQISAEIELLPTNDKKKWARPPISMNF
EVPFAPSGLKVRYLKVFEPKLNYSDHDVIKWVRYIGRSGIYETRC
Sequence of entity 2 (CCC, DDD), FASTA
>7OIQ_2 F-BAR domain only protein 2 (chains CCC, DDD)
SDLLAWDPLFG

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:

Browse structure collections

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