Structure analysis

Crystal structure of a CRM1-RanGTP-SPN1 export complex bound to a 113 amino acid FG-repeat containing fragment of Nup214

X-ray diffraction
2.85Å resolution
Assembly composition:
hetero tetramer (preferred)
Entry contents: 4 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero tetramer
Accessible surface area: 80915.51 Å2
Buried surface area: 15233.59 Å2
Dissociation area: 2,228.03 Å2
Dissociation energy (ΔGdiss): 3.65 kcal/mol
Dissociation entropy (TΔSdiss): 13.71 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-127257

Macromolecules

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Chain: B
Length: 172 amino acids
Theoretical weight: 19.81 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62826 (Residues: 8-179; Coverage: 80%)
Gene names: ARA24, OK/SW-cl.81, RAN
Pfam: Ras family
InterPro:
CATH: P-loop containing nucleotide triphosphate hydrolases

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Chain: C
Length: 289 amino acids
Theoretical weight: 33.28 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O95149 (Residues: 1-287; Coverage: 80%)
Gene names: RNUT1, SNUPN, SPN1
Pfam: Snurportin1
InterPro:
CATH: DNA ligase/mRNA capping enzyme

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Chain: D
Length: 479 amino acids
Theoretical weight: 50.58 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: P0AEX9 (Residues: 32-387; Coverage: 96%)
  • Canonical: P35658 (Residues: 1916-2027; Coverage: 5%)
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Gene names: CAIN, CAN, JW3994, KIAA0023, NUP214, b4034, malE
Pfam:
InterPro:

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