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1HJQ

Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0015926molecular_functionglucosidase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016998biological_processcell wall macromolecule catabolic process
A0030247molecular_functionpolysaccharide binding
A0031218molecular_functionarabinogalactan endo-1,4-beta-galactosidase activity
A0045490biological_processpectin catabolic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P48841
ChainResidueDetails
AGLU135

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P48841
ChainResidueDetails
AGLU245

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12761390
ChainResidueDetails
AASN111

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1fhl
ChainResidueDetails
AGLU245
AGLU135
AARG45

225158

PDB entries from 2024-09-18

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