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Structure of Lph2 , a novel bidirectional nuclear transport receptor in S. cerevisiae

Analyse Structure of Lph2 , a novel bidirectional nuclear transport receptor in S.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6FVB
Type
protein
Length
1,001 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
3.297
Source
Saccharomyces cerevisiae S288c
Molecule
Importin beta-like protein KAP120
UniProt
Q02932
Pockets
14 · best druggability 0.62

Structure

x-ray diffraction · resolution 3.297 · 1 distinct chain · 72% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AImportin beta-like protein KAP120protein100172% helix, 0% strandQ02932

Pockets

14 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12950.620.7941empty
21110.610.8627empty
32410.560.7823empty
4880.430.7919empty
5940.430.7822empty

Modifications

Observed in the structure: 18 modified (engineered).

Compared structures

  • 6FVB · Structure of LPH2 , a novel bidirectional nuclear transport receptor in S. cerevisiae · the same entry in another collection · chain A against A, TM-score 1.00
  • Q02932 · AlphaFold monomer V2.0 prediction for importin beta-like protein KAP120 (Q02932) · a predicted model of the same protein · chain A against A, TM-score 0.95

Analyse

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