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Hfq protein from pseudomonas aeruginosa. high-salt crystals

Analyse Hfq protein from pseudomonas aeruginosa. high-salt crystals in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1U1T
Type
protein
Length
398 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hfq protein
UniProt
Q9HUM0
Pockets
1 · best druggability 0.71

Structure

x-ray diffraction · 4 distinct chains · 20% helix, 44% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, DHfq proteinprotein6620% helix, 45% strandQ9HUM0
B, FHfq proteinprotein6620% helix, 44% strandQ9HUM0
CHfq proteinprotein6520% helix, 45% strandQ9HUM0
EHfq proteinprotein6919% helix, 43% strandQ9HUM0

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19170.710.7567empty

Interfaces

6 interfaces between chains.

  • D–E · 807 Ų buried · 11 hydrogen bonds · protein-protein
  • A–F · 784 Ų buried · 11 hydrogen bonds · protein-protein
  • C–D · 777 Ų buried · 11 hydrogen bonds · protein-protein
  • E–F · 725 Ų buried · 11 hydrogen bonds · protein-protein
  • A–B · 720 Ų buried · 11 hydrogen bonds · protein-protein

Compared structures

  • 1U1T · Hfq protein from Pseudomonas aeruginosa. High-salt crystals · the same entry in another collection · chain F against F, TM-score 1.00
  • Q9HUM0 · AlphaFold monomer V2.0 prediction for RNA-binding protein hfq (Q9HUM0) · a predicted model of the same protein · chain C against A, TM-score 0.99

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