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Crystal structure of an otu deubiquitinase from escherichia albertii bound to ubiquitin

Analyse Crystal structure of an otu deubiquitinase from escherichia albertii bound to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6W9S
Type
protein
Length
255 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Otu domain-containing protein eschotu; Ubiquitin
UniProt
B1EF49, P0CG48
Ligands
NEH
Pockets
1 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AOtu domain-containing protein eschotuprotein17850% helix, 10% strandB1EF49
BUbiquitinprotein7725% helix, 34% strandP0CG48

Ligands and binding sites

  • NEH · Ethanamine · ligand · chains A, B
  • FMT · Formic acid · additive · 3 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12830.590.7824empty

Interfaces

1 interface between chains.

  • A–B · 895 Ų buried · 18 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

  • 6W9S · Crystal structure of an OTU deubiquitinase from Escherichia albertii bound to ubiquitin · the same entry in another collection · chain A against A, TM-score 1.00

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