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1BYH

MOLECULAR AND ACTIVE-SITE STRUCTURE OF A BACILLUS (1-3,1-4)-BETA-GLUCANASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0042972molecular_functionlicheninase activity
Functional Information from PROSITE/UniProt
site_idPS01034
Number of Residues11
DetailsGH16_1 Glycosyl hydrolases family 16 active sites. EIDI.EflGKdT
ChainResidueDetails
AGLU105-THR115

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10064
ChainResidueDetails
AGLU105

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10064
ChainResidueDetails
AGLU109

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 2ayh
ChainResidueDetails
AGLU109
AASP107
AGLU105

site_idMCSA1
Number of Residues2
DetailsM-CSA 924
ChainResidueDetails
AGLU105covalent catalysis
AGLU109proton shuttle (general acid/base)

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PDB entries from 2025-06-18

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