3ksr

X-ray diffraction
2.69Å resolution

CRYSTAL STRUCTURE OF A PUTATIVE SERINE HYDROLASE (XCC3885) FROM XANTHOMONAS CAMPESTRIS PV. CAMPESTRIS AT 2.69 A RESOLUTION

Released:
Entry author: Joint Center for Structural Genomics (JCSG)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-185696 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidase S9 prolyl oligopeptidase catalytic domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 290 amino acids
Theoretical weight: 32.03 KDa
Source organism: Xanthomonas campestris pv. campestris str. ATCC 33913
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8P431 (Residues: 1-289; Coverage: 100%)
Gene name: XCC3885
Sequence domains: Prolyl oligopeptidase family
Structure domains:

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P43212
Unit cell:
a: 56.865Å b: 56.865Å c: 220.25Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.197 0.222
Expression system: Escherichia coli