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Crystal structure of the glycine receptor-gephyrin complex

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

PDB
2FTS
Type
protein
Length
432 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Gephyrin; Glycine receptor beta chain precursor
UniProt
Q03555, P20781
Pockets
2 · best druggability 0.41

Structure

x-ray diffraction · 2 distinct chains · 20% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGephyrinprotein41920% helix, 33% strandQ03555
PGlycine receptor beta chain precursorprotein1323% helix, 0% strandP20781

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11230.410.7620empty
21200.390.7522empty

Interfaces

1 interface between chains.

  • A–P · 776 Ų buried · 9 hydrogen bonds · protein-protein

Compared structures

  • 2FTS · Crystal structure of the glycine receptor-gephyrin complex · 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 A against A, TM-score 0.97
  • P20781 · AlphaFold monomer V2.0 prediction for glycine receptor subunit beta (P20781) · a predicted model of the same protein · chain P against A, TM-score 0.37

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