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NMR structure of UHRF1 tandem tudor domains in a complex with histone H3 peptide

Analyse NMR structure of UHRF1 tandem tudor domains in a complex with histone H3 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2L3R
Type
protein
Length
172 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
E3 ubiquitin-protein ligase UHRF1; Histone H3
UniProt
Q96T88, Q3BDD9
Pockets
1 · best druggability 0.44

Structure

solution nmr · 2 distinct chains · 5% helix, 40% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AE3 ubiquitin-protein ligase UHRF1protein1616% helix, 42% strandQ96T88
BHistone H3protein110% helix, 0% strandQ3BDD9

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1630.440.8214empty

Interfaces

1 interface between chains.

  • A–B · 827 Ų buried · 23 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (methylation).

Compared structures

  • 2L3R · NMR structure of UHRF1 Tandem Tudor Domains in a complex with Histone H3 peptide · the same entry in another collection · chain A against A, TM-score 1.00
  • Q96T88 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase UHRF1 (Q96T88) · a predicted model of the same protein · chain A against A, TM-score 0.79

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