3HS9: Intersectin 1-peptide-AP2 beta ear complex

Intersectin 1-peptide-AP2 beta ear complex. Determined by X-ray diffraction at 2.15 Å resolution. Released 23 Feb 2010.

Method: X-ray diffraction
Resolution: 2.15 Å
Organism: Rattus norvegicus
Chains: 2
Atoms: 2,085
Mol. weight: 30.67 kDa
Released: 23 Feb 2010

Explore 3HS9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3HS9 contains 9 α-helices and 15 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: 9 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	709-711	3
β-strand	712-715	4	1
α-helix	717-719	3
β-strand	723-731	9	1
β-strand	736-744	9	1
β-strand	750	1	2
β-strand	754-757	4	3
α-helix	758-759	2
β-strand	765-766	2	1
β-strand	776	1	2
β-strand	781-789	9	1
β-strand	802-808	7	3
β-strand	813-819	7	3
α-helix	820-821	2
α-helix	822-825	4
α-helix	834-843	10
α-helix	846-848	3
β-strand	849-854	6	4
α-helix	861-870	10
β-strand	874-880	7	4
β-strand	885-892	8	4
β-strand	898-905	8	4
β-strand	912-918	7	4
α-helix	924-934	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
AP-2 complex subunit beta-1	A	protein	260	Rattus norvegicus	P62944 (AlphaFold model)
peptide from Intersectin-1, residues 841-851	P	protein	12		Q9WVE9 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3HS9_1 AP-2 complex subunit beta-1 (chains A)
MGSSHHHHHHSSGLVPRGSHMASGMAPGGYVAPKAVWLPAVKAKGLEISGTFTHRQGHIY
MEMNFTNKALQHMTDFAIQFNKNSFGVIPSTPLAIHTPLMPNQSIDVSLPLNTLGPVMKM
EPLNNLQVAVKNNIDVFYFSCLIPLNVLFVEDGKMERQVFLATWKDIPNENELQFQIKEC
HLNADTVSSKLQNNNVYTIAKRNVEGQDMLYQSLKLTNGIWILAELRIQPGNPNYTLSLK
CRAPEVSQYIYQVYDSILKN

Sequence of entity 2 (P), FASTA

>3HS9_2 peptide from Intersectin-1, residues 841-851 (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 P62944 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3H1Z 1.83 Å, Molecular basis for the association of PIPKIgamma -p90 with the clathrin adaptor AP-2
6OWT 3.8 Å, Structure of SIVsmm Nef and SMM tetherin bound to the clathrin adaptor AP-2 complex

Browse structure collections

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