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6Q3R

ASPERGILLUS ACULEATUS GALACTANASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0015926molecular_functionglucosidase activity
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031218molecular_functionarabinogalactan endo-1,4-beta-galactosidase activity
A0045490biological_processpectin catabolic process
B0015926molecular_functionglucosidase activity
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0031218molecular_functionarabinogalactan endo-1,4-beta-galactosidase activity
B0045490biological_processpectin catabolic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 658
ChainResidueDetails
AARG45electrostatic stabiliser, hydrogen bond donor, increase nucleophilicity, modifies pKa
AGLU136activator, increase nucleophilicity, proton acceptor, proton donor
AGLU246covalently attached, hydrogen bond acceptor, nucleofuge, nucleophile

site_idMCSA2
Number of Residues3
DetailsM-CSA 658
ChainResidueDetails
BARG45electrostatic stabiliser, hydrogen bond donor, increase nucleophilicity, modifies pKa
BGLU136activator, increase nucleophilicity, proton acceptor, proton donor
BGLU246covalently attached, hydrogen bond acceptor, nucleofuge, nucleophile

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PDB entries from 2026-01-21

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