› 6vdl

X-ray diffraction
1.95Å resolution

HCV NS3/4A protease A156T mutant in complex with glecaprevir

Released:
DOI: 10.2210/pdb6vdl/pdb
PDB entry 6vdl coloured by chain, front view.
PDB entry 6vdl coloured by chain, side view.
PDB entry 6vdl coloured by chain, top view.
Source organism: Hepatitis C virus (isolate 1)
Entry authors: Timm J, Schiffer CA

Function and Biology Details

Reactions catalysed: 
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'.
NTP + H(2)O = NDP + phosphate
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150817 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protease NS2 Chain: A
Molecule details ›
Chain: A
Length: 203 amino acids
Theoretical weight: 21.55 KDa
Source organism: Hepatitis C virus (isolate 1)
Expression system: Escherichia coli
UniProt:
  • Canonical: P26664 (Residues: 1013-1026, 1030-1208; Coverage: 6%)
Sequence domains: Hepatitis C virus NS3 protease

Ligands and Environments

4 bound ligands:
Ligand ZN 1 x ZN
Ligand O31 1 x O31
Ligand GOL 2 x GOL
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 54.793Å b: 58.601Å c: 59.89Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.155 0.152 0.2
Expression system: Escherichia coli

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