9F6S: PDZ domain

PDZ domain in complex with the peptide from AP2-associated protein kinase 1. Determined by X-ray diffraction at 1.0 Å resolution. Released 14 May 2025.

Method
X-ray diffraction
Resolution
1.0 Å
Organism
Homo sapiens
Chains
2
Atoms
806
Mol. weight
10.07 kDa
Released
14 May 2025

Explore 9F6S in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9F6S contains 5 α-helices and 6 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: 5 helices, 6 β-strands

ElementResiduesLengthSheet
β-strand3-861
α-helix131
β-strand16-2161
α-helix22-243
β-strand26-3381
α-helix38-414
α-helix481
β-strand49-5351
β-strand56-5721
α-helix63-719
β-strand77-8261

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
PDZ and LIM domain protein 5Aprotein90Homo sapiensQ96HC4 (AlphaFold model)
AP2-associated protein kinase 1Bprotein6Homo sapiensQ2M2I8 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9F6S_1 PDZ and LIM domain protein 5 (chains A)
GPLGSMSNYSVSLVGPAPWGFRLQGGKDFNMPLTISSLKDGGKAAQANVRIGDVVLSIDG
INAQGMTHLEAQNKIKGCTGSLNMTLQRAS
Sequence of entity 2 (B), FASTA
>9F6S_2 AP2-associated protein kinase 1 (chains B)
DQLIDL

Primary citation

AAK1-mediated phosphorylation of PDLIM5 and Talin1 promotes focal adhesion disassembly to accelerate cell migration. Krocianova, D., Dagg, A.D., Clayton, R.A. et al. Nat Commun (2026). DOI 10.1038/s41467-026-72501-w · PubMed

Other PDB entries of the same protein (UniProt Q96HC4 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 9F6S directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.