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Crystal structure of the rat USP11 dusp-ubl domains

Analyse Crystal structure of the rat USP11 dusp-ubl domains in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4MEM
Type
protein
Length
428 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ubiquitin carboxyl-terminal hydrolase 11
EC
3.4.19.12
UniProt
Q5D006
Pockets
3 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 25% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUbiquitin carboxyl-terminal hydrolase 11 (EC 3.4.19.12)protein21225% helix, 29% strandQ5D006
BUbiquitin carboxyl-terminal hydrolase 11 (EC 3.4.19.12)protein21625% helix, 29% strandQ5D006

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13280.620.7926empty
21220.410.7615empty
31510.410.7424empty

Interfaces

1 interface between chains.

  • A–B · 158 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 4MEM · Crystal Structure of the rat USP11 DUSP-UBL domains · the same entry in another collection · chain A against A, TM-score 1.00
  • Q5D006 · AlphaFold monomer V2.0 prediction for ubiquitin carboxyl-terminal hydrolase 11 (Q5D006) · a predicted model of the same protein · chain A against A, TM-score 0.89

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