› 2oit

X-ray diffraction
1.65Å resolution

Crystal Structure of the N-terminal Domain of the Human Proto-oncogene Nup214/CAN

Released:
DOI: 10.2210/pdb2oit/pdb
PDB entry 2oit coloured by chain, front view.
PDB entry 2oit coloured by chain, side view.
PDB entry 2oit coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the N-terminal domain of the human protooncogene Nup214/CAN.
Napetschnig J, Blobel G, Hoelz A
Proc Natl Acad Sci U S A 104 1783-8 (2007)
PMID: 17264208

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152987 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nuclear pore complex protein Nup214 Chain: A
Molecule details ›
Chain: A
Length: 434 amino acids
Theoretical weight: 48.12 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P35658 (Residues: 1-434; Coverage: 21%)
Gene names: CAIN, CAN, KIAA0023, NUP214

Ligands and Environments

1 bound ligand:
Ligand MES 1 x MES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1, NSLS BEAMLINE X9A
Spacegroup: P212121
Unit cell:
a: 52.381Å b: 81.14Å c: 102.607Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.199 0.237
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

10 review citations

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

6 mentions without citation

Structural mechanism of ATP-independent transcription initiation by RNA polymerase I.
Han et al. (2017)
5 more