› 4aq0

X-ray diffraction
2.09Å resolution

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:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125901 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ccman5 Chains: A, B
Molecule details ›
Chains: A, B
Length: 790 amino acids
Theoretical weight: 84.29 KDa
Source organism: Cellulosimicrobium cellulans
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: M1E1E9 (Residues: 1-748; Coverage: 100%)
Sequence domains:
Structure domains: Beta-galactosidase; Chain A, domain 5

Ligands and Environments

3 bound ligands:
Ligand CA 2 x CA
Ligand B3P 1 x B3P
Ligand DMJ 1 x DMJ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P2221
Unit cell:
a: 81.62Å b: 91.79Å c: 224.21Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.17 0.203
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

20 review citations

Lysosomal storage diseases: from pathophysiology to therapy.
Parenti et al. (2015)
19 more

1 mention without citation

A structure of substrate-bound Synaptojanin1 provides new insights in its mechanism and the effect of disease mutations.
Paesmans et al. (2020)