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R17A mutant of hfq protein from neisseria meningitidis

Analyse R17A mutant of hfq protein from neisseria meningitidis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7OH8
Type
protein
Length
203 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
RNA-binding protein hfq
UniProt
B9VV05
Pockets
1 · best druggability 0.29

Structure

x-ray diffraction · 2 distinct chains · 21% helix, 45% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARNA-binding protein hfqprotein6721% helix, 46% strandB9VV05
B, CRNA-binding protein hfqprotein6821% helix, 44% strandB9VV05

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1630.290.7414empty

Interfaces

2 interfaces between chains.

  • B–C · 812 Ų buried · 15 hydrogen bonds · protein-protein
  • A–B · 798 Ų buried · 14 hydrogen bonds · protein-protein

Compared structures

  • 7OH8 · R17A mutant of Hfq protein from Neisseria meningitidis · the same entry in another collection · chain A against A, TM-score 1.00

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