› 2wyh

X-ray diffraction
1.9Å resolution

Structure of the Streptococcus pyogenes family GH38 alpha-mannosidase

Released:
DOI: 10.2210/pdb2wyh/pdb
PDB 2wyh coloured by chain and viewed from the front.
PDB 2wyh coloured by chain and viewed from the side.
PDB 2wyh coloured by chain and viewed from the top.
Source organism: Streptococcus pyogenes M1 GAS
Entry authors: Suits MDL, Zhu Y, Taylor EJ, Zechel DL, Gilbert HJ, Davies GJ

Function and Biology Details

Reaction catalysed: 
Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-mann_mid domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 923 amino acids
Theoretical weight: 105.24 KDa
Source organism: Streptococcus pyogenes M1 GAS
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q99YP5 (Residues: 1-901; Coverage: 100%)
Gene name: SPy_1604
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand ZN 2 x ZN
Ligand GOL 12 x GOL
Ligand TRS 1 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21
Unit cell:
a: 92.573Å b: 88.502Å c: 134.688Å
α: 90° β: 108.97° γ: 90°
R-values:
R R work R free
0.179 0.177 0.205
Expression system: Escherichia coli BL21(DE3)

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Citations

4 review citations

Glycan-metabolizing enzymes in microbe-host interactions: the Streptococcus pneumoniae paradigm.
Hobbs et al. (2018)
3 more

2 mentions without citation

Higher-order assemblies of oligomeric cargo receptor complexes form the membrane scaffold of the Cvt vesicle.
Bertipaglia et al. (2016)
1 more