› 1u8x

X-ray diffraction
2.05Å resolution

CRYSTAL STRUCTURE OF GLVA FROM BACILLUS SUBTILIS, A METAL-REQUIRING, NAD-DEPENDENT 6-PHOSPHO-ALPHA-GLUCOSIDASE

Released:
DOI: 10.2210/pdb1u8x/pdb
PDB entry 1u8x coloured by chain, front view.
PDB entry 1u8x coloured by chain, side view.
PDB entry 1u8x coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Novel catalytic mechanism of glycoside hydrolysis based on the structure of an NAD+/Mn2+ -dependent phospho-alpha-glucosidase from Bacillus subtilis.
Rajan SS, Yang X, Collart F, Yip VL, Withers SG, Varrot A, Thompson J, Davies GJ, Anderson WF
Structure 12 1619-29 (2004)
PMID: 15341727

Function and Biology Details

Reaction catalysed: 
Alpha-maltose 6'-phosphate + H(2)O = D-glucose + D-glucose 6-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157077 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Maltose-6'-phosphate glucosidase Chain: X
Molecule details ›
Chain: X
Length: 472 amino acids
Theoretical weight: 54.08 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P54716 (Residues: 1-449; Coverage: 100%)
Gene names: BSU08180, glv-1, glvA, glvG, malA
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 1 x NAD
2 bound ligands:
Ligand G6P 1 x G6P
Ligand MN 1 x MN
1 modified residue:
Ligand MSE 18 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 5ID-B
Spacegroup: I222
Unit cell:
a: 82.604Å b: 102.017Å c: 144.748Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.195 0.221
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

10 review citations

Mechanistic insights into glycosidase chemistry.
Vocadlo et al. (2008)
9 more

5 mentions without citation

Toward the estimation of the absolute quality of individual protein structure models.
Benkert et al. (2011)
4 more