4ose

X-ray diffraction
2.4Å resolution

X-ray Crystal Structure of a Putative Hydrolase from Rickettsia typhi

Released:
Entry author: Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
AB hydrolase-1 domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 298 amino acids
Theoretical weight: 34.56 KDa
Source organism: Rickettsia typhi str. Wilmington
Expression system: Escherichia coli
UniProt:
  • Canonical: Q68WT4 (Residues: 1-290; Coverage: 100%)
Gene name: RT0431
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: C2
Unit cell:
a: 154.92Å b: 49.06Å c: 87.29Å
α: 90° β: 94.77° γ: 90°
R-values:
R R work R free
0.203 0.201 0.235
Expression system: Escherichia coli