3slz

X-ray diffraction
1.4Å resolution

The crystal structure of XMRV protease complexed with TL-3

Released:

Function and Biology Details

Reactions catalysed:
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
Endonucleolytic cleavage to 5'-phosphomonoester.
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Capsid protein p30 Chains: A, B
Molecule details ›
Chains: A, B
Length: 132 amino acids
Theoretical weight: 14.35 KDa
Source organism: DG-75 Murine leukemia virus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9E7M1 (Residues: 533-657; Coverage: 7%)
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 46.483Å b: 65.546Å c: 69.732Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.176 0.201
Expression system: Escherichia coli BL21(DE3)