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Structure of a viral otu domain protease bound to ubiquitin

Analyse Structure of a viral otu domain protease bound to ubiquitin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3PT2
Type
protein
Length
239 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
RNA polymerase; Ubiquitin B
UniProt
Q6TQF5, Q5U5U6
Ligands
3CN, SO4
Pockets
1 · best druggability 0.32

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARNA polymeraseprotein16439% helix, 25% strandQ6TQF5
BUbiquitin Bprotein7524% helix, 35% strandQ5U5U6

Ligands and binding sites

  • 3CN · 3-aminopropane · ligand · chains A, B
  • SO4 · Sulfate ion · ion · 3 copies · chains A, B
  • ACT · Acetate ion · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1550.320.7715empty

Interfaces

1 interface between chains.

  • A–B · 1024 Ų buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 modified, 2 covalent (engineered, covalent ligand).

Compared structures

  • 3PT2 · Structure of a viral OTU domain protease bound to Ubiquitin · the same entry in another collection · chain A against A, TM-score 1.00

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