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7EZT

The structure and functional mechanism of nucleotide regulated acetylhexosaminidase Am2136 from Akkermansia muciniphila

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004563molecular_functionbeta-N-acetylhexosaminidase activity
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0102148molecular_functionN-acetyl-beta-D-galactosaminidase activity
B0000272biological_processpolysaccharide catabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0004563molecular_functionbeta-N-acetylhexosaminidase activity
B0005975biological_processcarbohydrate metabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0102148molecular_functionN-acetyl-beta-D-galactosaminidase activity
C0000272biological_processpolysaccharide catabolic process
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0004563molecular_functionbeta-N-acetylhexosaminidase activity
C0005975biological_processcarbohydrate metabolic process
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0102148molecular_functionN-acetyl-beta-D-galactosaminidase activity
D0000272biological_processpolysaccharide catabolic process
D0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
D0004563molecular_functionbeta-N-acetylhexosaminidase activity
D0005975biological_processcarbohydrate metabolic process
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0102148molecular_functionN-acetyl-beta-D-galactosaminidase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system => ECO:0000305|PubMed:31345574, ECO:0007744|PDB:6JQF
ChainResidueDetails
DASN272
DHIS344
DGLU413

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:31345574, ECO:0007744|PDB:6JQF
ChainResidueDetails
DARG243
DASP412
DTRP464
DTYR490
DTRP536

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PDB entries from 2024-07-24

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