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Structure of the catalytic domain of USP28 (insertion deleted)

Analyse Structure of the catalytic domain of USP28 (insertion deleted) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6HEH
Type
protein
Length
339 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ubiquitin carboxyl-terminal hydrolase 28,UBIQUITIN carboxyl-terminal hydrolase 28
EC
3.4.19.12
UniProt
Q96RU2
Ligands
CL
Pockets
3 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUbiquitin carboxyl-terminal hydrolase 28,UBIQUITIN carboxyl-terminal hydrolase 28 (EC 3.4.19.12)protein33941% helix, 24% strandQ96RU2

Ligands and binding sites

  • CL · Chloride ion · ion · chains A
  • EDO · 1,2-ethanediol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11530.620.8433empty
21620.500.7829empty
3880.380.7620empty

Compared structures

  • 6HEH · Structure of the catalytic domain of USP28 (insertion deleted) · the same entry in another collection · chain A against A, TM-score 1.00
  • Q96RU2 · AlphaFold monomer V2.0 prediction for ubiquitin carboxyl-terminal hydrolase 28 (Q96RU2) · a predicted model of the same protein · chain A against A, TM-score 0.97

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