5brp

X-ray diffraction
2.05Å resolution

Crystal structure of Bacillus licheniformis trehalose-6-phosphate hydrolase (TreA), mutant R201Q, in complex with PNG

Released:

Function and Biology Details

Reaction catalysed:
Alpha,alpha-trehalose 6-phosphate + H(2)O = D-glucose + D-glucose 6-phosphate
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-179221 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha,alpha-phosphotrehalase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 568 amino acids
Theoretical weight: 66.61 KDa
Source organism: Bacillus licheniformis DSM 13 = ATCC 14580
Expression system: Escherichia coli M15
UniProt:
  • Canonical: Q65MI2 (Residues: 1-562; Coverage: 100%)
Gene names: BL03069, treA
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL15A1
Spacegroup: P1
Unit cell:
a: 60.252Å b: 97.388Å c: 108.539Å
α: 80.3° β: 88.15° γ: 72.18°
R-values:
R R work R free
0.171 0.171 0.214
Expression system: Escherichia coli M15