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Structual basis for the recognition of UBC13 by the shigella flexneri effector ospi

Analyse Structual basis for the recognition of UBC13 by the shigella flexneri effector… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3W30
Type
protein
Length
384 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ORF169B
UniProt
Q8VSD5
Pockets
3 · best druggability 0.38

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BORF169Bprotein19240% helix, 16% strandQ8VSD5

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1680.380.7820empty
2500.330.7814empty
3520.280.7521empty

Compared structures

  • 3W30 · Structual basis for the recognition of Ubc13 by the Shigella flexneri effector OspI · the same entry in another collection · chain A against A, TM-score 1.00

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