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Structure of D212, a nuclease from a fusselovirus.

Analyse Structure of D212, a nuclease from a fusselovirus. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2W8M
Type
protein
Length
333 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Orf D212
UniProt
Q6TRV5
Pockets
5 · best druggability 0.40

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AOrf D212protein16541% helix, 26% strandQ6TRV5
BOrf D212protein16839% helix, 30% strandQ6TRV5

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11290.400.7419empty
2820.360.7621empty
3980.330.7318empty
4950.330.7319empty
5590.290.7417empty

Interfaces

1 interface between chains.

  • A–B · 1129 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 2W8M · Structure of D212, a nuclease from a fusselovirus. · the same entry in another collection · chain A against A, TM-score 1.00

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