9PPP: Alpha Appendage of AP2

Structure of Alpha Appendage of AP2 bound to the extended FxDxF motif derived of CCDC32. Determined by X-ray diffraction at 2.1 Å resolution. Released 8 Apr 2026.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Mus musculus
Chains: 4
Atoms: 4,858
Mol. weight: 61.65 kDa
Released: 8 Apr 2026

Explore 9PPP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9PPP contains 17 α-helices and 32 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 A: 7 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	702-703	2	1
α-helix	705-707	3
β-strand	714-718	5	1
β-strand	722-731	10	1
β-strand	734-743	10	1
β-strand	749-757	9	2
α-helix	762-765	4
β-strand	766-770	5	1
β-strand	777	1	2
β-strand	782-791	10	1
β-strand	800-807	8	2
β-strand	810-817	8	2
α-helix	822-825	4
β-strand	826-828	3	3
α-helix	833-842	10
α-helix	846-848	3
β-strand	849-855	7	3
α-helix	862-872	11
β-strand	875-877	3	3
β-strand	887-894	8	3
β-strand	899-909	11	3
β-strand	914-921	8	3
α-helix	924-935	12

Chain B: 8 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	702-703	2	4
α-helix	705-707	3
β-strand	714-718	5	4
β-strand	722-731	10	4
β-strand	734-743	10	4
β-strand	749-757	9	5
α-helix	762-765	4
β-strand	766-770	5	4
α-helix	771-774	4
β-strand	777	1	5
β-strand	782-791	10	4
β-strand	800-807	8	5
β-strand	810-817	8	5
α-helix	822-825	4
β-strand	826-828	3	6
α-helix	833-842	10
α-helix	846-848	3
β-strand	849-855	7	6
α-helix	862-872	11
β-strand	875-877	3	6
β-strand	887-894	8	6
β-strand	899-909	11	6
β-strand	914-921	8	6
α-helix	924-935	12

Chains P and Q: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	3-7	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
AP-2 complex subunit alpha-2	A, B	protein	244	Mus musculus	P17427 (AlphaFold model)
Coiled-coil domain-containing protein 32	P, Q	protein	28	Mus musculus	Q8BS39 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>9PPP_1 AP-2 complex subunit alpha-2 (chains A, B)
APLAPGSEDNFARFVCKNNGVLFENQLLQIGLKSEFRQNLGRMFIFYGNKTSTQFLNFTP
TLICADDLQTNLNLQTKPVDPTVDGGAQVQQVVNIECISDFTEAPVLNIQFRYGGTFQNV
SVKLPITLNKFFQPTEMASQDFFQRWKQLSNPQQEVQNIFKAKHPMDTEITKAKIIGFGS
ALLEEVDPNPANFVGAGIIHTKTTQIGCLLRLEPNLQAQMYRLTLRTSKDTVSQRLCELL
SEQF

Sequence of entity 2 (P, Q), FASTA

>9PPP_2 Coiled-coil domain-containing protein 32 (chains P, Q)
DLWAEICSCLPSPAQEDVSDNAFSDSFM

Primary citation

CCDC32 collaborates with the membrane to assemble the AP-2 clathrin adaptor complex. Sloan, D.E., Matthews, A., Yanagisawa, H. et al. bioRxiv (2025). DOI 10.1101/2025.08.05.668722 · PubMed

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

1KYF 1.22 Å, Ap-2 clathrin adaptor alpha-appendage in complex with EPS15 dpf peptide
1QTS 1.4 Å, Crystal structure of the ap-2 clathrin adaptor alpha-appendage
7OHI 1.41 Å, FCHO1-peptide-AP2 alpha ear complex
1QTP 1.6 Å, Crystal structure of the ap-2 clathrin adaptor alpha-appendage
2VJ0 1.6 Å, Crystal structure of the alpha-adaptin appendage domain, from the AP2 adaptor complex,…
1KYU 1.8 Å, Ap-2 clathrin adaptor alpha-appendage in complex with EPS15 dpf peptide
1B9K 1.9 Å, Alpha-adaptin appendage domain, from clathrin adaptor AP2
1W80 1.9 Å, Crystal structure of the alpha-adaptin appendage domain, from the AP2 adaptor complex,…
3HS8 1.9 Å, Intersectin 1-peptide-AP2 alpha ear complex
9PUE 1.91 Å, Structure of Alpha Appendage of AP2 bound to the FxDxF motif derived of CCDC32
1KY6 2.0 Å, Ap-2 clathrin adaptor alpha-appendage in complex with epsin dpw peptide
1KYD 2.0 Å, Ap-2 clathrin adaptor alpha-appendage in complex with epsin dpw peptide

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