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Solution structure of 53BP1 tandem tudor domains in complex with a P53K382ME2 peptide

Analyse Solution structure of 53BP1 tandem tudor domains in complex with a P53K382ME2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2MWP
Type
protein
Length
135 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tumor suppressor P53-binding protein 1; Cellular tumor antigen P53
UniProt
Q12888, P04637
Pockets
2 · best druggability 0.48

Structure

solution nmr · 2 distinct chains · 10% helix, 47% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATumor suppressor P53-binding protein 1protein12311% helix, 52% strandQ12888
BCellular tumor antigen P53protein120% helix, 0% strandP04637

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11070.480.8022empty
2540.340.7821empty

Interfaces

1 interface between chains.

  • A–B · 562 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (methylation).

Compared structures

  • 2MWP · Solution structure of 53BP1 tandem Tudor domains in complex with a p53K382me2 peptide · the same entry in another collection · chain A against A, TM-score 1.00
  • Q12888 · AlphaFold monomer V2.0 prediction for TP53-binding protein 1 (Q12888) · a predicted model of the same protein · chain A against A, TM-score 0.85

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