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Crystal structure of gephyrin E-domain

Analyse Crystal structure of gephyrin E-domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2FU3
Type
protein
Length
824 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Gephyrin
UniProt
Q03555
Pockets
5 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 19% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGephyrinprotein40520% helix, 31% strandQ03555
BGephyrinprotein41918% helix, 31% strandQ03555

Pockets

5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110830.830.84109empty
210610.830.84115empty
39650.810.8289empty
4710.580.8922empty
5930.380.7515empty

Interfaces

1 interface between chains.

  • A–B · 3732 Ų buried · 35 hydrogen bonds · protein-protein

Compared structures

  • 2FU3 · Crystal structure of gephyrin E-domain · the same entry in another collection · chain A against A, TM-score 1.00
  • Q03555 · AlphaFold monomer V2.0 prediction for gephyrin (Q03555) · a predicted model of the same protein · chain B against A, TM-score 0.97

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