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4GYK

Crystal structure of mutant (D318N) bacillus subtilis family 3 glycoside hydrolase (nagz) in complex with glcnac-murnac (space group P1211)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004563molecular_functionbeta-N-acetylhexosaminidase activity
A0005576cellular_componentextracellular region
A0005886cellular_componentplasma membrane
A0005975biological_processcarbohydrate metabolic process
A0008360biological_processregulation of cell shape
A0009252biological_processpeptidoglycan biosynthetic process
A0009254biological_processpeptidoglycan turnover
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0071555biological_processcell wall organization
A0102148molecular_functionN-acetyl-beta-D-galactosaminidase activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0004563molecular_functionbeta-N-acetylhexosaminidase activity
B0005576cellular_componentextracellular region
B0005886cellular_componentplasma membrane
B0005975biological_processcarbohydrate metabolic process
B0008360biological_processregulation of cell shape
B0009252biological_processpeptidoglycan biosynthetic process
B0009254biological_processpeptidoglycan turnover
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0071555biological_processcell wall organization
B0102148molecular_functionN-acetyl-beta-D-galactosaminidase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:20826810, ECO:0000305|PubMed:23177201
ChainResidueDetails
AHIS234
BHIS234

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:20826810, ECO:0000305|PubMed:23177201
ChainResidueDetails
AASN318
BASN318

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:20826810, ECO:0000269|PubMed:23177201
ChainResidueDetails
AASP123
AARG131
AARG191
ALYS221
BASP123
BARG131
BARG191
BLYS221

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Important for catalytic activity => ECO:0000305|PubMed:20826810
ChainResidueDetails
AASP232
BASP232

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PDB entries from 2024-07-24

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