3HS8: Intersectin 1-peptide-AP2 alpha ear complex

Intersectin 1-peptide-AP2 alpha ear complex. Determined by X-ray diffraction at 1.9 Å resolution. Released 23 Feb 2010.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Mus musculus
Chains: 2
Atoms: 2,171
Mol. weight: 32.17 kDa
Released: 23 Feb 2010

Explore 3HS8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3HS8 contains 7 α-helices and 18 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, 18 β-strands

Element	Residues	Length	Sheet
β-strand	702-703	2	1
α-helix	705-708	4
β-strand	714-718	5	1
β-strand	722-731	10	1
β-strand	734-743	10	1
β-strand	749	1	2
β-strand	750	1	3
β-strand	755-757	3	3
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	3
β-strand	810-817	8	3
α-helix	822-825	4
β-strand	826-828	3	4
α-helix	833-842	10
α-helix	846-848	3
β-strand	849-855	7	4
α-helix	862-872	11
β-strand	875-876	2	4
β-strand	887-894	8	4
β-strand	899-909	11	4
β-strand	914-921	8	4
α-helix	924-935	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Adaptor protein complex AP-2, alpha 2 subunit	A	protein	273	Mus musculus	P17427 (AlphaFold model)
peptide from Intersectin-1, residues 840-851	P	protein	12		Q9Z0R4 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3HS8_1 Adaptor protein complex AP-2, alpha 2 subunit (chains A)
MGSSHHHHHHSSGLVPRGSHMASMTGGQQMGRGSEFEDNFARFVCKNNGVLFENQLLQIG
LKSEFRQNLGRMFIFYGNKTSTQFLNFTPTLICADDLQTNLNLQTKPVDPTVDGGAQVQQ
VVNIECISDFTEAPVLNIQFRYGGTFQNVSVKLPITLNKFFQPTEMASQDFFQRWKQLSN
PQQEVQNIFKAKHPMDTEITKAKIIGFGSALLEEVDPNPANFVGAGIIHTKTTQIGCLLR
LEPNLQAQMYRLTLRTSKDTVSQRLCELLSEQF

Sequence of entity 2 (P), FASTA

>3HS8_2 peptide from Intersectin-1, residues 840-851 (chains P)
PNNWADFSSTWP

Primary citation

Regulation of synaptic vesicle recycling by complex formation between intersectin 1 and the clathrin adaptor complex AP2. Pechstein, A., Bacetic, J., Vahedi-Faridi, A. et al. Proc Natl Acad Sci U S A (2010) 107:4206-4211. DOI 10.1073/pnas.0911073107 · 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,…
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
9PPP 2.1 Å, Structure of Alpha Appendage of AP2 bound to the extended FxDxF motif derived of CCDC32

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