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4GVF

Crystal structure of Salmonella typhimurium family 3 glycoside hydrolase (NagZ) bound to GlcNAc

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004563molecular_functionbeta-N-acetylhexosaminidase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0008360biological_processregulation of cell shape
A0009252biological_processpeptidoglycan biosynthetic process
A0009254biological_processpeptidoglycan turnover
A0016231molecular_functionbeta-N-acetylglucosaminidase activity
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0046677biological_processresponse to antibiotic
A0051301biological_processcell division
A0071555biological_processcell wall organization
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0004563molecular_functionbeta-N-acetylhexosaminidase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0008360biological_processregulation of cell shape
B0009252biological_processpeptidoglycan biosynthetic process
B0009254biological_processpeptidoglycan turnover
B0016231molecular_functionbeta-N-acetylglucosaminidase activity
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0046677biological_processresponse to antibiotic
B0051301biological_processcell division
B0071555biological_processcell wall organization
Functional Information from PROSITE/UniProt
site_idPS00775
Number of Residues18
DetailsGLYCOSYL_HYDROL_F3 Glycosyl hydrolases family 3 active site. VLRqElgfdGVIFSDdlS
ChainResidueDetails
AVAL234-SER251

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues19
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues15
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"23177201","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_00364","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23177201","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00364","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsSite: {"description":"Important for catalytic activity","evidences":[{"source":"HAMAP-Rule","id":"MF_00364","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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