3cih

X-ray diffraction
2.33Å resolution

Crystal structure of a putative alpha-rhamnosidase from Bacteroides thetaiotaomicron

Released:
Entry authors: Kumaran D, Burley SK, Swaminathan S, New York SGX Research Center for Structural Genomics (NYSGXRC)

Function and Biology Details

Reaction catalysed:
Hydrolysis of terminal non-reducing alpha-L-rhamnose residues in alpha-L-rhamnosides
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183769 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
alpha-L-rhamnosidase Chain: A
Molecule details ›
Chain: A
Length: 739 amino acids
Theoretical weight: 86.4 KDa
Source organism: Bacteroides thetaiotaomicron VPI-5482
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8A916 (Residues: 2-729; Coverage: 100%)
Gene name: BT_1001
Sequence domains:
Structure domains: Galactose-binding domain-like

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: I422
Unit cell:
a: 146.895Å b: 146.895Å c: 198.847Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.203 0.233
Expression system: Escherichia coli BL21(DE3)