X-ray diffraction
2Å resolution

Crystal structure of a retropepsin-like aspartic protease from Rickettsia conorii

Source organism: Rickettsia conorii
Primary publication:
Structure of RC1339/APRc from Rickettsia conorii, a retropepsin-like aspartic protease.
Acta Crystallogr. D Biol. Crystallogr. 71 2109-18 (2015)
PMID: 26457434

Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
ApRick protease Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 139 amino acids
Theoretical weight: 15.72 KDa
Source organism: Rickettsia conorii
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q92FY8 (Residues: 105-231; Coverage: 55%)
Gene name: RC1339
Sequence domains: gag-polyprotein putative aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 50.102Å b: 94.153Å c: 118.636Å
α: 90° β: 90° γ: 90°
R R work R free
0.2 0.199 0.255
Expression system: Escherichia coli BL21(DE3)