› 5qu7

X-ray diffraction
1.27Å resolution

Crystal Structure of swapped human Nck SH3.1 domain, 1.3A, orthorhombic form III

Released:
DOI: 10.2210/pdb5qu7/pdb
PDB entry 5qu7 coloured by chain, front view.
PDB entry 5qu7 coloured by chain, side view.
PDB entry 5qu7 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Small molecule AX-024 reduces T cell proliferation independently of CD3ϵ/Nck1 interaction, which is governed by a domain swap in the Nck1-SH3.1 domain.
Richter K, Rufer AC, Muller M, Burger D, Casagrande F, Grossenbacher T, Huber S, Hug MN, Koldewey P, D'Osualdo A, Schlatter D, Stoll T, Rudolph MG
OpenAccess logo J Biol Chem 295 7849-7864 (2020)
PMID: 32317279

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147691 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
SH2/SH3 adapter protein NCK1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 82 amino acids
Theoretical weight: 9.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P16333 (Residues: 4-59; Coverage: 15%)
Gene names: NCK, NCK1
Sequence domains: SH3 domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P212121
Unit cell:
a: 40.07Å b: 48.87Å c: 55.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.171 0.219
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Sinner or Saint?: Nck Adaptor Proteins in Vascular Biology.
Alfaidi et al. (2021)
6 other articles