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3mrh

X-ray diffraction
2.4Å resolution

Crystal Structure of MHC class I HLA-A2 molecule complexed with HCV NS3-1073-1081 nonapeptide N3S variant

Released:
Model geometry
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Function and Biology Details

Reactions catalysed:
RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate.
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 orAla in P1'.
a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate+ phosphate + H(+).
ATP + H2O = ADP + phosphate + H(+).

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-137803 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
HLA class I histocompatibility antigen, A alpha chain Chain: A
Molecule details ›
Chain: A
Length: 293 amino acids
Theoretical weight: 34.01 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04439 (Residues: 25-304; Coverage: 81%)
Gene names: HLA-A, HLAA
Sequence domains:
Structure domains:
Beta-2-microglobulin Chain: B
Molecule details ›
Chain: B
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%)
Gene names: B2M, CDABP0092, HDCMA22P
Sequence domains: Immunoglobulin C1-set domain
Structure domains: Immunoglobulins
Serine protease/helicase NS3 Chain: P

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P21
Unit cell:
a: 52.978Å b: 80.06Å c: 57.057Å
α: 90° β: 113.72° γ: 90°
R-values:
R R work R free
0.217 0.222 0.308
Expression systems:
  • Escherichia coli
  • Not provided