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Crystal structure of wild-type LYS48-linked diubiquitin in an open conformation

Analyse Crystal structure of wild-type LYS48-linked diubiquitin in an open conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3AUL
Type
protein
Length
149 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Polyubiquitin-C
UniProt
P0CG48
Pockets
1 · best druggability 0.43

Structure

x-ray diffraction · 2 distinct chains · 24% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APolyubiquitin-Cprotein7624% helix, 33% strandP0CG48
BPolyubiquitin-Cprotein7325% helix, 34% strandP0CG48

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11130.430.7725empty

Interfaces

1 interface between chains.

  • A–B · 390 Ų buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 isopeptide (isopeptide).

Compared structures

  • 3AUL · Crystal structure of wild-type Lys48-linked diubiquitin in an open conformation · the same entry in another collection · chain A against A, TM-score 1.00

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