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Crystal structure of listeria monocytogenes hfq

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

PDB
4NL2
Type
protein
Length
440 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein hfq
UniProt
B8DG33
Pockets
3 · best druggability 0.62

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
D, A, EProtein hfqprotein7321% helix, 44% strandB8DG33
BProtein hfqprotein7221% helix, 44% strandB8DG33
CProtein hfqprotein7420% helix, 43% strandB8DG33
FProtein hfqprotein7520% helix, 44% strandB8DG33

Ligands and binding sites

  • PGO · S-1,2-propanediol · additive · 7 copies · chains D, A, B, C, F

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16830.620.7355empty
2680.360.7817empty
3560.310.7612PGO

Interfaces

7 interfaces between chains.

  • A–B · 892 Ų buried · 17 hydrogen bonds · protein-protein
  • C–F · 879 Ų buried · 17 hydrogen bonds · protein-protein
  • E–F · 864 Ų buried · 16 hydrogen bonds · protein-protein
  • D–A · 861 Ų buried · 16 hydrogen bonds · protein-protein
  • B–F · 348 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 4NL2 · Crystal Structure of Listeria monocytogenes Hfq · the same entry in another collection · chain D against D, TM-score 1.00

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