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1GHS

THE THREE-DIMENSIONAL STRUCTURES OF TWO PLANT BETA-GLUCAN ENDOHYDROLASES WITH DISTINCT SUBSTRATE SPECIFICITIES

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0006076biological_process(1->3)-beta-D-glucan catabolic process
A0006952biological_processdefense response
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0042973molecular_functionglucan endo-1,3-beta-D-glucosidase activity
A0050832biological_processdefense response to fungus
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0006076biological_process(1->3)-beta-D-glucan catabolic process
B0006952biological_processdefense response
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0042973molecular_functionglucan endo-1,3-beta-D-glucosidase activity
B0050832biological_processdefense response to fungus
Functional Information from PROSITE/UniProt
site_idPS00587
Number of Residues14
DetailsGLYCOSYL_HYDROL_F17 Glycosyl hydrolases family 17 signature. VkVVVSESGWPSaG
ChainResidueDetails
AVAL225-GLY238

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:O22317
ChainResidueDetails
AGLU94
BGLU94

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:O22317
ChainResidueDetails
AGLU231
BGLU231

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 580
ChainResidueDetails
AGLU231covalently attached, electrostatic stabiliser, nucleofuge, nucleophile
AGLU279activator, modifies pKa
ALYS282activator, modifies pKa
AGLU288activator, increase nucleophilicity, proton acceptor, proton donor

site_idMCSA2
Number of Residues4
DetailsM-CSA 580
ChainResidueDetails
BGLU231covalently attached, electrostatic stabiliser, nucleofuge, nucleophile
BGLU279activator, modifies pKa
BLYS282activator, modifies pKa
BGLU288activator, increase nucleophilicity, proton acceptor, proton donor

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PDB entries from 2024-09-11

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