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Viral protease

Analyse Viral protease in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7E6K
Type
protein
Length
305 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
3C-like proteinase
EC
3.4.22.69
UniProt
P0DTD1
Ligands
HYR, SO4
Pockets
3 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A3C-like proteinase (EC 3.4.22.69)protein30525% helix, 29% strandP0DTD1

Ligands and binding sites

  • HYR · N-(2-phenoxyethyl)methanethioamide · ligand · 3 copies · chains A
  • SO4 · Sulfate ion · ion · 2 copies · chains A
  • DMS · Dimethyl sulfoxide · additive · 2 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12040.470.7533HYR, DMS
2700.320.7514empty
3500.280.7512empty

Modifications

Observed in the structure: 3 covalent (covalent ligand).

Compared structures

  • 7E6K · Viral protease · the same entry in another collection · chain A against A, TM-score 1.00

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