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:
Structure analysis Details
Assembly composition:
hetero pentamer (preferred)
PDBe Complex ID:
PDB-CPX-229834 (preferred)
Entry contents:
5 distinct polypeptide molecules
Macromolecules (5 distinct):
HLA class I histocompatibility antigen, A alpha chain
Molecule details ›
Chains: A, F
Length: 275 amino acids
Theoretical weight: 31.85 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 275 amino acids
Theoretical weight: 31.85 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P04439 (Residues: 25-299; Coverage: 81%)
Sequence domains:
Structure domains:
Beta-2-microglobulin
Molecule details ›
Chains: B, G
Length: 100 amino acids
Theoretical weight: 11.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Immunoglobulin C1-set domain
Structure domains: Immunoglobulins
Length: 100 amino acids
Theoretical weight: 11.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P61769 (Residues: 21-119; Coverage: 100%)
Sequence domains: Immunoglobulin C1-set domain
Structure domains: Immunoglobulins
Serine protease/helicase NS3
Molecule details ›
Chains: C, H
Length: 10 amino acids
Theoretical weight: 998 Da
UniProt:
Length: 10 amino acids
Theoretical weight: 998 Da
UniProt:
- Canonical: P27958 (Residues: 1406-1415; Coverage: 0%)
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
APS BEAMLINE 22-ID
Spacegroup:
P3121
Expression systems:
- Escherichia coli
- Escherichia coli 'BL21-Gold(DE3)pLysS AG'
