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Guanylate kinase domains of the maguk family scaffold proteins as specific phospho-protein binding modules

Analyse Guanylate kinase domains of the maguk family scaffold proteins as specific… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3UAT
Type
protein
Length
291 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Disks large homolog 1; Phosphor-lgn peptide
UniProt
Q62696
Pockets
2 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ADisks large homolog 1protein27632% helix, 26% strandQ62696
BPhosphor-lgn peptideprotein1527% helix, 13% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13960.620.7749empty
21830.470.7626empty

Interfaces

1 interface between chains.

  • A–B · 841 Ų buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

  • 3UAT · Guanylate Kinase Domains of the MAGUK Family Scaffold Proteins as Specific… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q62696 · AlphaFold monomer V2.0 prediction for disks large homolog 1 (Q62696) · a predicted model of the same protein · chain A against A, TM-score 0.97

Analyse

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