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Structure of the karyopherin BETA2-ran gppnhp nuclear transport complex

Analyse Structure of the karyopherin BETA2-ran gppnhp nuclear transport complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1QBK
Type
protein
Length
1,070 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Karyopherin BETA2; Ran
UniProt
Q92973, P62826
Ligands
GNP, MG
Pockets
15 · best druggability 0.87

Structure

x-ray diffraction · 2 distinct chains · 51% helix, 4% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
BKaryopherin BETA2protein88058% helix, 0% strandQ92973
CRanprotein19018% helix, 21% strandP62826

Ligands and binding sites

  • GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · chains C
  • MG · Magnesium ion · metal · chains C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

15 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17570.870.9080empty
23810.820.9149empty
37570.750.8069empty
42490.720.8640empty
54980.710.8141empty

Interfaces

1 interface between chains.

  • B–C · 2206 Ų buried · 32 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 27 modified (engineered).

Compared structures

  • 1QBK · Structure of the karyopherin BETA2-ran gppnhp nuclear transport complex · the same entry in another collection · chain B against B, TM-score 1.00
  • Q92973 · AlphaFold monomer V2.0 prediction for transportin-1 (Q92973) · a predicted model of the same protein · chain B against A, TM-score 0.79

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