› 3mrj

X-ray diffraction
1.87Å resolution

Crystal Structure of MHC class I HLA-A2 molecule complexed with HCV NS3-1073-1081 nonapeptide V5M variant

Released:
DOI: 10.2210/pdb3mrj/pdb
PDB entry 3mrj coloured by chain, front view.
PDB entry 3mrj coloured by chain, side view.
PDB entry 3mrj coloured by chain, top view.
Source organisms:
Entry authors: Reiser J-B, Le Gorrec M, Chouquet A, Debeaupuis E, Echasserieau K, Saulquin X, Bonneville M, Housset D

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:
Sequence domains:

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
Molecule details ›
Chain: P
Length: 9 amino acids
Theoretical weight: 1.03 KDa
Source organism: Hepatitis C virus isolate HC-J1
Expression system: Not provided
UniProt:
  • Canonical: Q03463 (Residues: 1073-1081; Coverage: 0%)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21
Unit cell:
a: 54.58Å b: 80.1Å c: 57.88Å
α: 90° β: 114.96° γ: 90°
R-values:
R R work R free
0.19 0.188 0.23
Expression systems:
  • Escherichia coli
  • Not provided

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