X-ray diffraction
1.9Å resolution

Crystal Structure of MHC class I HLA-A2 molecule complexed with HCV NS3-1406-1415 decapeptide

Source organisms:
Entry authors: Gras S, Echasserieau K, Saulquin X, Bonneville M, Housset D

Function and Biology Details

Reactions catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
NTP + H(2)O = NDP + phosphate
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'.
ATP + H(2)O = ADP + phosphate
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
Non-polymer only trimer (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
  • 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
  • Canonical: P61769 (Residues: 21-119; Coverage: 100%)
Gene names: B2M, CDABP0092, HDCMA22P
Sequence domains: Immunoglobulin C1-set domain
Structure domains: Immunoglobulins
Core protein precursor Chain: P
Molecule details ›
Chain: P
Length: 10 amino acids
Theoretical weight: 998 Da
Source organism: Hepacivirus C
Expression system: Not provided
  • Canonical: Q9DIT6 (Residues: 1406-1415; Coverage: 0%)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P21
Unit cell:
a: 53.223Å b: 80.985Å c: 56.341Å
α: 90° β: 112.24° γ: 90°
R R work R free
0.192 0.19 0.25
Expression systems:
  • Escherichia coli
  • Not provided