3sgg

X-ray diffraction
1.25Å resolution

Crystal structure of a putative hydrolase (BT_2193) from Bacteroides thetaiotaomicron VPI-5482 at 1.25 A resolution

Released:
Source organism: Bacteroides thetaiotaomicron
Entry author: Joint Center for Structural Genomics (JCSG)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-183695 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidase S26A, signal peptidase Chain: A
Molecule details ›
Chain: A
Length: 536 amino acids
Theoretical weight: 60.09 KDa
Source organism: Bacteroides thetaiotaomicron
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8A5P5 (Residues: 23-557; Coverage: 100%)
Gene name: BT_2193
Sequence domains:
Structure domains: GxGYxYP glycoside hydrolase, C-terminal domain

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: C2
Unit cell:
a: 161.915Å b: 49.37Å c: 71.359Å
α: 90° β: 114.45° γ: 90°
R-values:
R R work R free
0.152 0.151 0.176
Expression system: Escherichia coli