2FRW: Second SH3 domain of human adaptor protein NCK2

Solution structure of the second SH3 domain of human adaptor protein NCK2. Determined by solution NMR. Released 20 Jun 2006.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
464
Mol. weight
6.57 kDa
Released
20 Jun 2006

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

Secondary structure: helices and β-sheets

2FRW contains 3 α-helices and 10 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: 3 helices, 10 β-strands

ElementResiduesLengthSheet
β-strand3-531
β-strand912
β-strand1313
β-strand1613
α-helix181
β-strand1912
α-helix201
β-strand24-2521
β-strand2614
β-strand37-4044
β-strand43-4644
α-helix49-513
β-strand52-5321

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Cytoplasmic protein NCK2Aprotein57Homo sapiensO43639 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2FRW_1 Cytoplasmic protein NCK2 (chains A)
IPAFVKFAYVAEREDELSLVKGSRVTVMEKCSDGWWRGSYNGQIGWFPSNYVLEEVD

Primary citation

Structural Insight into the Binding Diversity between the Human Nck2 SH3 Domains and Proline-Rich Proteins. Liu, J., Li, M., Ran, X. et al. Biochemistry (2006) 45:7171-7184. DOI 10.1021/bi060091y · PubMed

Other PDB entries of the same protein (UniProt O43639 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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