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Structure of OTUD2 OTU domain

Analyse Structure of OTUD2 OTU domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4BOQ
Type: protein
Length: 175 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.47
Source: HOMO SAPIENS
Molecule: Ubiquitin thioesterase OTU1
EC: 3.4.19.12
UniProt: Q5VVQ6

Structure

x-ray diffraction · resolution 1.47 · 1 distinct chain · 38% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ubiquitin thioesterase OTU1 (EC 3.4.19.12)	protein	175	38% helix, 18% strand	Q5VVQ6

Ligands and binding sites

GOL · Glycerol · additive · 4 copies · chains A

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

Compared structures

4BOQ · Structure of OTUD2 otu domain · the same entry in another collection · chain A against A, TM-score 1.00
Q5VVQ6 · AlphaFold monomer V2.0 prediction for ubiquitin thioesterase OTU1 (Q5VVQ6) · a predicted model of the same protein · chain A against A, TM-score 0.95

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q5VVQ6
Elsewhere: RCSB PDB 4BOQ · PDBe 4BOQ · UniProt Q5VVQ6

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