4azg

X-ray diffraction
2.4Å resolution

Differential inhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, StrH

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-155969 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-N-acetylhexosaminidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 443 amino acids
Theoretical weight: 49.79 KDa
Source organism: Streptococcus pneumoniae TIGR4
Expression system: Escherichia coli
UniProt:
  • Canonical: P49610 (Residues: 627-1064; Coverage: 34%)
Gene names: SP_0057, strH
Sequence domains: Glycosyl hydrolase family 20, catalytic domain
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P212121
Unit cell:
a: 66.7Å b: 115.2Å c: 129.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.19 0.248
Expression system: Escherichia coli