1KY7: The ap-2 clathrin adaptor alpha-appendage

The ap-2 clathrin adaptor alpha-appendage in complex with amphiphysin fxdxf. Determined by X-ray diffraction at 2.15 Å resolution. Released 12 Jun 2002.

Method
X-ray diffraction
Resolution
2.15 Å
Organism
Mus musculus
Chains
2
Atoms
2,196
Mol. weight
29.06 kDa
Released
12 Jun 2002

Explore 1KY7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1KY7 contains 7 α-helices and 16 β-strands across 1 chain. 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 A: 7 helices, 16 β-strands

ElementResiduesLengthSheet
α-helix705-7084
β-strand714-71851
β-strand722-731101
β-strand734-743101
β-strand74912
β-strand750-75783
α-helix760-7656
β-strand766-77051
β-strand77712
β-strand782-791101
β-strand800-80783
β-strand810-81783
α-helix822-8254
β-strand826-82834
α-helix833-8408
α-helix846-8483
β-strand849-85574
α-helix862-87211
β-strand875-87734
β-strand887-89484
β-strand899-909114
β-strand914-92184
α-helix924-93512

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Alpha-adaptin CAprotein247Mus musculusP17427 (AlphaFold model)
AmphiphysinPprotein10P49418 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1KY7_1 ALPHA-ADAPTIN C (chains A)
GSPGIRLGSSEDNFARFVCKNNGVLFENQLLQIGLKSEFRQNLGRMFIFYGNKTSTQFLN
FTPTLICADDLQTNLNLQTKPVDPTVDGGAQVQQVVNIECISDFTEAPVLNIQFRYGGTF
QNVSVKLPITLNKFFQPTEMASQDFFQRWKQLSNPQQEVQNIFKAKHPMDTEITKAKIIG
FGSALLEEVDPNPANFVGAGIIHTKTTQIGCLLRLEPNLQAQMYRLTLRTSKDTVSQRLC
ELLSEQF
Sequence of entity 2 (P), FASTA
>1KY7_2 AMPHIPHYSIN (chains P)
SFFEDNFVPE

Primary citation

Accessory protein recruitment motifs in clathrin-mediated endocytosis. Brett, T.J., Traub, L.M., Fremont, D.H. Structure (2002) 10:797-809. DOI 10.1016/S0969-2126(02)00784-0 · PubMed

Other PDB entries of the same protein (UniProt P17427 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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