3gb8

X-ray diffraction
2.9Å resolution

Crystal structure of CRM1/Snurportin-1 complex

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
Non-polymer only dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Exportin-1 Chain: A
Molecule details ›
Chain: A
Length: 1071 amino acids
Theoretical weight: 123.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O14980 (Residues: 1-1071; Coverage: 100%)
Gene names: CRM1, XPO1
Sequence domains:
Structure domains: Leucine-rich Repeat Variant
Snurportin-1 Chain: B
Molecule details ›
Chain: B
Length: 329 amino acids
Theoretical weight: 37.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O95149 (Residues: 1-328; Coverage: 91%)
Gene names: RNUT1, SNUPN, SPN1
Sequence domains: Snurportin1
Structure domains: DNA ligase/mRNA capping enzyme

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P6422
Unit cell:
a: 250.4Å b: 250.4Å c: 190.4Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.238 0.236 0.267
Expression system: Escherichia coli