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Double tudor domain complex structure

Analyse Double tudor domain complex structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2GFA
Type
protein
Length
231 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Jumonji domain-containing protein 2A; Peptide
UniProt
O75164
Pockets
2 · best druggability 0.43

Structure

x-ray diffraction · 3 distinct chains · 5% helix, 54% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AJumonji domain-containing protein 2Aprotein1076% helix, 56% strandO75164
BJumonji domain-containing protein 2Aprotein1105% helix, 54% strandO75164
C, DPeptideprotein70% helix, 14% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11540.430.7432empty
2950.380.7621empty

Interfaces

6 interfaces between chains.

  • A–B · 560 Ų buried · 9 hydrogen bonds · protein-protein
  • B–D · 544 Ų buried · 10 hydrogen bonds · protein-protein
  • A–C · 532 Ų buried · 16 hydrogen bonds · protein-protein
  • B–C · 77 Ų buried · 2 hydrogen bonds · protein-protein
  • A–D · 36 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (methylation).

Compared structures

  • 2GFA · double tudor domain complex structure · the same entry in another collection · chain A against A, TM-score 1.00

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