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Solution structure of lipase binding domain LID1 of foldase from Pseudomonas aeruginosa

Analyse Solution structure of lipase binding domain LID1 of foldase from Pseudomonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6GSF
Type
protein
Length
82 residues
Chains
1
Method
solution nmr
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
NOT
Source
Pseudomonas aeruginosa PAO1
Molecule
Lipase chaperone
UniProt
Q01725
Pockets
2 · best druggability 0.39

Structure

solution nmr · resolution NOT · 1 distinct chain · 52% helix, 9% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALipase chaperoneprotein8252% helix, 9% strandQ01725

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1550.390.8014empty
2910.360.7514empty

Compared structures

  • 6GSF · Solution structure of lipase binding domain LID1 of foldase from pseudomonas aeruginosa · the same entry in another collection · chain A against A, TM-score 1.00
  • Q01725 · AlphaFold monomer V2.0 prediction for lipase chaperone (Q01725) · a predicted model of the same protein · chain A against A, TM-score 0.74

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