2KKC: P62 PB1 domain

NMR structure of the p62 PB1 domain. Determined by solution NMR. Released 15 Sept 2009.

Method
Solution NMR
Organism
Rattus norvegicus
Chains
1
Atoms
791
Mol. weight
11.43 kDa
Released
15 Sept 2009

Explore 2KKC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2KKC contains 2 α-helices and 5 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: 2 helices, 5 β-strands

ElementResiduesLengthSheet
β-strand3-1191
β-strand17-26101
α-helix41-5212
β-strand61-6661
β-strand72-7541
α-helix78-8710
β-strand92-9981

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Sequestosome-1Aprotein102Rattus norvegicusO08623 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2KKC_1 Sequestosome-1 (chains A)
GPHMSLTVKAYLLGKEEAAREIRRFSFCFSPEPEAEAAAGPGPCERLLSRVAVLFPALRP
GGFQAHYRAERGDLVAFSSDEELTMAMSYVKDDIFRIYIKEK

Primary citation

The NMR structure of the p62 PB1 domain, a key protein in autophagy and NF-kappaB signaling pathway. Saio, T., Yokochi, M., Inagaki, F. J Biomol NMR (2009) 45:335-341. DOI 10.1007/s10858-009-9370-7 · PubMed

Other PDB entries of the same protein (UniProt O08623 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 2KKC 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.