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1GLH

CATION BINDING TO A BACILLUS (1,3-1,4)-BETA-GLUCANASE. GEOMETRY, AFFINITY AND EFFECT ON PROTEIN STABILITY

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0042972molecular_functionlicheninase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 330
ChainResidue
APRO9
AGLY45
ATYR56
AASP207

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 2024-09-18

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