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Crystal structure of NS3/4A protease variant R155K in complex with vaniprevir

Analyse Crystal structure of NS3/4A protease variant R155K in complex with vaniprevir in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3SU4
Type
protein
Length
384 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
NS3 PROTEASE,NS4A protein
UniProt
A8DG50, B4YYL7
Ligands
SU3, ZN, SO4
Pockets
1 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 16% helix, 46% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BNS3 PROTEASE,NS4A proteinprotein19216% helix, 46% strandA8DG50, B4YYL7

Ligands and binding sites

  • SU3 · (5R,7S,10S)-10-tert-butyl-N-{(1R,2R)-1-[(cyclopropylsulfonyl)carbamoyl]-2-ethylcyclopropyl}-15,15-dimethyl-3,9,12-trioxo-6,7,9,10,11,12,14,15,16,17,18,19-dodecahydro-1H,5H-2,23:5,8-dimethano-4,13,2,8,11-benzodioxatriazacyclohenicosine-7(3H)-carboxamide · ligand · 2 copies · chains A, B
  • ZN · Zinc ion · metal · 2 copies · chains A, B
  • SO4 · Sulfate ion · ion · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17440.660.7464SU3, SO4

Interfaces

1 interface between chains.

  • A–B · 280 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 3SU4 · Crystal structure of NS3/4A protease variant R155K in complex with vaniprevir · the same entry in another collection · chain B against B, TM-score 1.00

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