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4GVG

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004563molecular_functionbeta-N-acetylhexosaminidase activity
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0008360biological_processregulation of cell shape
A0009252biological_processpeptidoglycan biosynthetic process
A0009254biological_processpeptidoglycan turnover
A0016231molecular_functionbeta-N-acetylglucosaminidase 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
B0005975biological_processcarbohydrate metabolic process
B0008360biological_processregulation of cell shape
B0009252biological_processpeptidoglycan biosynthetic process
B0009254biological_processpeptidoglycan turnover
B0016231molecular_functionbeta-N-acetylglucosaminidase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0046677biological_processresponse to antibiotic
B0051301biological_processcell division
B0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MES A 7001
ChainResidue
APHE32
ATHR33
AARG34
AARG70
AMET252
AASN280
AHOH7317

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MES B 7001
ChainResidue
AASP316
AHOH7427
BSER310
BHOH7196
BHOH7289
BHOH7385
AARG311
AARG312

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 Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:23177201
ChainResidueDetails
AHIS176
BHIS176

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00364, ECO:0000269|PubMed:23177201
ChainResidueDetails
AASP248
BASP248

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING:
ChainResidueDetails
AASP62
AARG133
ALYS163
BASP62
BARG133
BLYS163

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00364
ChainResidueDetails
AARG70
BARG70

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_00364
ChainResidueDetails
AASP174
BASP174

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PDB entries from 2024-11-06

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