› 5ac4

X-ray diffraction
2.08Å resolution

GH20C, Beta-hexosaminidase from Streptococcus pneumoniae in complex with GalNAc

Released:
DOI: 10.2210/pdb5ac4/pdb
Model geometry
Fit model/data
PDB entry 5ac4 coloured by chain, front view.
PDB entry 5ac4 coloured by chain, side view.
PDB entry 5ac4 coloured by chain, top view.
Source organism: Streptococcus pneumoniae TIGR4
Primary publication:
A Second β-Hexosaminidase Encoded in the Streptococcus pneumoniae Genome Provides an Expanded Biochemical Ability to Degrade Host Glycans.
Robb M, Robb CS, Higgins MA, Hobbs JK, Paton JC, Boraston AB
J Biol Chem 290 30888-900 (2015)
PMID: 26491009

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:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-101497 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycosyl hydrolase-related protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 649 amino acids
Theoretical weight: 74.18 KDa
Source organism: Streptococcus pneumoniae TIGR4
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0H2US73 (Residues: 1-626; Coverage: 100%)
Gene name: SP_2141
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand NGA 2 x NGA
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P212121
Unit cell:
a: 95.55Å b: 99.05Å c: 133.45Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.163 0.161 0.198
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Epidemiology, virulence factors and management of the pneumococcus.
Feldman et al. (2016)
2 more

2 mentions without citation

A Second β-Hexosaminidase Encoded in the Streptococcus pneumoniae Genome Provides an Expanded Biochemical Ability to Degrade Host Glycans.
Robb et al. (2015)
1 more