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The structure of the PP2A B56 subunit double phosphorylated BUBR1 complex

Analyse The structure of the PP2A B56 subunit double phosphorylated BUBR1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5SWF
Type
protein
Length
331 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
SERINE/THREONINE-protein phosphatase 2A 56 kda regulatory subunit gamma isoform; Double…
UniProt
Q13362
Pockets
2 · best druggability 0.53

Structure

x-ray diffraction · 2 distinct chains · 70% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASERINE/THREONINE-protein phosphatase 2A 56 kda regulatory subunit gamma isoformprotein32372% helix, 0% strandQ13362
BDouble phosphorylated BUBR1protein80% helix, 0% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1670.530.8614empty
21040.410.7720empty

Interfaces

1 interface between chains.

  • A–B · 586 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

  • 5SWF · The structure of the PP2A B56 subunit double phosphorylated BubR1 complex · the same entry in another collection · chain A against A, TM-score 1.00
  • Q13362 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein phosphatase 2A 56 kda… · a predicted model of the same protein · chain A against A, TM-score 0.95

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