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7VT4

Crystal structure of mutant E393Q of MtGlu5

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0008422molecular_functionbeta-glucosidase activity
A0008810molecular_functioncellulase activity
A0009251biological_processglucan catabolic process
A0009986cellular_componentcell surface
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0071704biological_processorganic substance metabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005576cellular_componentextracellular region
B0005975biological_processcarbohydrate metabolic process
B0008422molecular_functionbeta-glucosidase activity
B0008810molecular_functioncellulase activity
B0009251biological_processglucan catabolic process
B0009986cellular_componentcell surface
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0071704biological_processorganic substance metabolic process
Functional Information from PROSITE/UniProt
site_idPS00659
Number of Residues10
DetailsGLYCOSYL_HYDROL_F5 Glycosyl hydrolases family 5 signature. VYFELLNEPH
ChainResidueDetails
AVAL142-HIS151

221051

PDB entries from 2024-06-12

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