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5OKG

Non-conservatively refined structure of Gan1D-E170Q, a catalytic mutant of a putative 6-phospho-beta-galactosidase from Geobacillus stearothermophilus, in complex with cellobiose-6-phosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0033920molecular_function6-phospho-beta-galactosidase activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0033920molecular_function6-phospho-beta-galactosidase activity
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0005975biological_processcarbohydrate metabolic process
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0033920molecular_function6-phospho-beta-galactosidase activity
D0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
D0005975biological_processcarbohydrate metabolic process
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0033920molecular_function6-phospho-beta-galactosidase activity
Functional Information from PROSITE/UniProt
site_idPS00572
Number of Residues9
DetailsGLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. ILITENGLG
ChainResidueDetails
AILE374-GLY382

site_idPS00653
Number of Residues15
DetailsGLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FlWGaAsAAYQvEgA
ChainResidueDetails
APHE13-ALA27

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PDB entries from 2024-07-17

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