› 7fe1

X-ray diffraction
1.72Å resolution

Crystal structure of GH92 alpha-1,2-mannosidase from Enterococcus faecalis ATCC 10100 in complex with methyl alpha-1,2-C-mannobioside

Released:
DOI: 10.2210/pdb7fe1/pdb
PDB entry 7fe1 coloured by chain, front view.
PDB entry 7fe1 coloured by chain, side view.
PDB entry 7fe1 coloured by chain, top view.
Source organism: Enterococcus faecalis ATCC 10100
Primary publication:
Unlocking the Hydrolytic Mechanism of GH92 α-1,2-Mannosidases: Computation Inspires the use of C-Glycosides as Michaelis Complex Mimics.
Alonso-Gil S, Parkan K, Kaminský J, Pohl R, Miyazaki T
OpenAccess logo Chemistry 28 e202200148 (2022)
PMID: 35049087

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-566899 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-1,2-mannosidase, putative Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 721 amino acids
Theoretical weight: 82.73 KDa
Source organism: Enterococcus faecalis ATCC 10100
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q832K9 (Residues: 1-713; Coverage: 100%)
Gene name: EF_2217
Sequence domains:

Ligands and Environments

6 bound ligands:
Ligand 5II 4 x 5II
Ligand MAN 4 x MAN
Ligand CA 4 x CA
Ligand NA 4 x NA
Ligand ACY 2 x ACY
Ligand EDO 18 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: C2221
Unit cell:
a: 163.162Å b: 169.601Å c: 258.659Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.15 0.149 0.171
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 mention without citation

Unlocking the Hydrolytic Mechanism of GH92 α-1,2-Mannosidases: Computation Inspires the use of C-Glycosides as Michaelis Complex Mimics.
Alonso-Gil et al. (2022)