› 1t0o

X-ray diffraction
1.96Å resolution

The structure of alpha-galactosidase from Trichoderma reesei complexed with beta-D-galactose

Released:
DOI: 10.2210/pdb1t0o/pdb
PDB entry 1t0o coloured by chain, front view.
PDB entry 1t0o coloured by chain, side view.
PDB entry 1t0o coloured by chain, top view.
Source organism: Trichoderma reesei
Primary publication:
Crystal structure of alpha-galactosidase from Trichoderma reesei and its complex with galactose: implications for catalytic mechanism.
Golubev AM, Nagem RA, Brandão Neto JR, Neustroev KN, Eneyskaya EV, Kulminskaya AA, Shabalin KA, Savel'ev AN, Polikarpov I
J Mol Biol 339 413-22 (2004)
PMID: 15136043

Function and Biology Details

Reaction catalysed: 
Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187664 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
Alpha-galactosidase Chain: A
Molecule details ›
Chain: A
Length: 417 amino acids
Theoretical weight: 45.61 KDa
Source organism: Trichoderma reesei
UniProt:
  • Canonical: Q92456 (Residues: 28-444; Coverage: 100%)
Gene name: agl1
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
1 bound ligand:
Ligand GAL 1 x GAL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE D03B-MX1
Spacegroup: P212121
Unit cell:
a: 57.834Å b: 58.313Å c: 153.66Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.151 0.205

Quick links

Citations

3 review citations

α-Glucosidases and α-1,4-glucan lyases: structures, functions, and physiological actions.
Okuyama et al. (2016)
2 more

2 mentions without citation

Glycosyl Oxocarbenium Ions: Structure, Conformation, Reactivity, and Interactions.
Franconetti et al. (2021)
1 more