2JS0: Second SH3 domain of adaptor Nck

Solution structure of second SH3 domain of adaptor Nck. Determined by solution NMR. Released 26 Feb 2008.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
490
Mol. weight
6.99 kDa
Released
26 Feb 2008

Explore 2JS0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2JS0 contains 1 α-helix and 8 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: 1 helix, 8 β-strands

ElementResiduesLengthSheet
β-strand5-951
β-strand1312
β-strand2011
β-strand2312
β-strand28-3471
β-strand39-4461
β-strand47-5261
α-helix53-553
β-strand56-5721

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Cytoplasmic protein NCK1Aprotein61Homo sapiensP16333 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2JS0_1 Cytoplasmic protein NCK1 (chains A)
GSLNMPAYVKFNYMAEREDELSLIKGTKVIVMEKCSDGWWRGSYNGQVGWFPSNYVTEEG
D

Primary citation

Specificity determinants of a novel Nck interaction with the juxtamembrane domain of the epidermal growth factor receptor. Hake, M.J., Choowongkomon, K., Kostenko, O. et al. Biochemistry (2008) 47:3096-3108. DOI 10.1021/bi701549a · PubMed

Other PDB entries of the same protein (UniProt P16333 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 2JS0 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.