› 3cqg

X-ray diffraction
3Å resolution

Nucleoporin Nup107/Nup133 interaction complex, delta finger mutant

Released:
DOI: 10.2210/pdb3cqg/pdb
PDB entry 3cqg coloured by chain, front view.
PDB entry 3cqg coloured by chain, side view.
PDB entry 3cqg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and functional studies of Nup107/Nup133 interaction and its implications for the architecture of the nuclear pore complex.
Boehmer T, Jeudy S, Berke IC, Schwartz TU
Mol Cell 30 721-31 (2008)
PMID: 18570875

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157619 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Nuclear pore complex protein Nup107 Chain: A
Molecule details ›
Chain: A
Length: 246 amino acids
Theoretical weight: 28.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P57740 (Residues: 658-771, 802-925; Coverage: 26%)
Gene name: NUP107
Sequence domains: Nuclear pore protein 84 / 107
Structure domains: Delta-Endotoxin; domain 1
Nuclear pore complex protein Nup133 Chain: B
Molecule details ›
Chain: B
Length: 227 amino acids
Theoretical weight: 26.18 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8WUM0 (Residues: 934-1156; Coverage: 19%)
Gene name: NUP133
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P212121
Unit cell:
a: 47.655Å b: 65.533Å c: 193.23Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.243 0.239 0.288
Expression system: Escherichia coli

Quick links

Citations

20 review citations

The structure of the nuclear pore complex.
Hoelz et al. (2011)
19 more

4 mentions without citation

Three-dimensional structure and flexibility of a membrane-coating module of the nuclear pore complex.
Kampmann et al. (2009)
3 more