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Structure of the complex of ubiquitin and the ubiquitin-like (ubl) domain of DDI1

Analyse Structure of the complex of ubiquitin and the ubiquitin-like (ubl) domain of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2MWS
Type
protein
Length
155 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ubiquitin; DNA damage-inducible protein 1
UniProt
P0CG48, P40087
Pockets
1 · best druggability 0.46

Structure

solution nmr · 2 distinct chains · 22% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUbiquitinprotein7624% helix, 34% strandP0CG48
BDNA damage-inducible protein 1protein7920% helix, 24% strandP40087

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11010.460.7919empty

Interfaces

1 interface between chains.

  • A–B · 747 Ų buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (nonstandard).

Compared structures

  • 2MWS · Structure of the complex of ubiquitin and the ubiquitin-like (UBL) domain of Ddi1 · the same entry in another collection · chain A against A, TM-score 1.00
  • P40087 · AlphaFold monomer V2.0 prediction for DNA damage-inducible protein 1 (P40087) · a predicted model of the same protein · chain B against A, TM-score 0.79

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