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4IIS

Crystal structure of a glycosylated beta-1,3-glucanase (HEV B 2), An allergen from Hevea Brasiliensis (Space group P41)

Replaces:  3F55
Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0042973molecular_functionglucan endo-1,3-beta-D-glucosidase activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0042973molecular_functionglucan endo-1,3-beta-D-glucosidase activity
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0005975biological_processcarbohydrate metabolic process
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0042973molecular_functionglucan endo-1,3-beta-D-glucosidase activity
D0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
D0005975biological_processcarbohydrate metabolic process
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0042973molecular_functionglucan endo-1,3-beta-D-glucosidase activity
Functional Information from PROSITE/UniProt
site_idPS00587
Number of Residues14
DetailsGLYCOSYL_HYDROL_F17 Glycosyl hydrolases family 17 signature. LeVVVSESGWPSaG
ChainResidueDetails
ALEU234-GLY247

222415

PDB entries from 2024-07-10

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