3tev

X-ray diffraction
2.3Å resolution

The crystal structure of glycosyl hydrolase from Deinococcus radiodurans R1

Released:
Source organism: Deinococcus radiodurans R1
Entry authors: Chang C, Hatzos-Skintges C, Kohler M, Clancy S, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

Reaction catalysed:
Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-193281 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
beta-N-acetylhexosaminidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 351 amino acids
Theoretical weight: 38.07 KDa
Source organism: Deinococcus radiodurans R1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9RUP9 (Residues: 1-348; Coverage: 100%)
Gene name: DR_1333
Sequence domains: Glycosyl hydrolase family 3 N terminal domain
Structure domains: Glycoside hydrolase, family 3, N-terminal domain

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: I4
Unit cell:
a: 146.841Å b: 146.841Å c: 108.733Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.181 0.218
Expression system: Escherichia coli BL21(DE3)