› 2hd0

X-ray diffraction
2.28Å resolution

Structure of the catalytic domain of hepatitis C virus NS2

Released:
DOI: 10.2210/pdb2hd0/pdb
PDB entry 2hd0 coloured by chain, front view.
PDB entry 2hd0 coloured by chain, side view.
PDB entry 2hd0 coloured by chain, top view.
Source organism: Hepacivirus hominis
Primary publication:
Structure of the catalytic domain of the hepatitis C virus NS2-3 protease.
Lorenz IC, Marcotrigiano J, Dentzer TG, Rice CM
Nature 442 831-5 (2006)
PMID: 16862121

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:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151128 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protease NS2 Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 128 amino acids
Theoretical weight: 13.93 KDa
Source organism: Hepacivirus hominis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P27958 (Residues: 903-1026; Coverage: 4%)
Sequence domains: Hepatitis C virus non-structural protein NS2
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand BOG 11 x BOG
Ligand DMU 1 x DMU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9A, NSLS BEAMLINE X29A
Spacegroup: P21
Unit cell:
a: 109.812Å b: 68.819Å c: 125.162Å
α: 90° β: 105.88° γ: 90°
R-values:
R R work R free
0.226 0.226 0.268
Expression system: Escherichia coli BL21(DE3)

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Citations

26 review citations

Replication of hepatitis C virus.
Moradpour et al. (2007)
25 more

14 mentions without citation

Structural and functional studies of nonstructural protein 2 of the hepatitis C virus reveal its key role as organizer of virion assembly.
Jirasko et al. (2010)
13 more