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Crystal structure of the hfq protein from escherichia COLI

Analyse Crystal structure of the hfq protein from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1HK9
Type
protein
Length
388 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein hfq
UniProt
P0A6X3
Pockets
3 · best druggability 0.64

Structure

x-ray diffraction · 5 distinct chains · 21% helix, 46% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein hfqprotein6420% helix, 47% strandP0A6X3
B, CProtein hfqprotein6322% helix, 48% strandP0A6X3
DProtein hfqprotein6621% helix, 45% strandP0A6X3
EProtein hfqprotein6721% helix, 45% strandP0A6X3
FProtein hfqprotein6520% helix, 46% strandP0A6X3

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14450.640.7722empty
22950.510.7337empty
3510.300.7617empty

Interfaces

6 interfaces between chains.

  • A–F · 763 Ų buried · 10 hydrogen bonds · protein-protein
  • B–C · 751 Ų buried · 9 hydrogen bonds · protein-protein
  • D–E · 747 Ų buried · 11 hydrogen bonds · protein-protein
  • C–D · 729 Ų buried · 13 hydrogen bonds · protein-protein
  • E–F · 725 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 1HK9 · Crystal structure of the Hfq protein from Escherichia coli · the same entry in another collection · chain F against F, TM-score 1.00
  • P0A6X3 · AlphaFold monomer V2.0 prediction for RNA-binding protein hfq (P0A6X3) · a predicted model of the same protein · chain A against A, TM-score 0.98

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