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6JTI

Crystal structure of native NagZ from Neisseria gonorrhoeae

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
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0051301biological_processcell division
A0071555biological_processcell wall organization
A0102148molecular_functionN-acetyl-beta-D-galactosaminidase activity
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
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0051301biological_processcell division
B0071555biological_processcell wall organization
B0102148molecular_functionN-acetyl-beta-D-galactosaminidase activity
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0004563molecular_functionbeta-N-acetylhexosaminidase activity
C0005737cellular_componentcytoplasm
C0005975biological_processcarbohydrate metabolic process
C0008360biological_processregulation of cell shape
C0009252biological_processpeptidoglycan biosynthetic process
C0009254biological_processpeptidoglycan turnover
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0051301biological_processcell division
C0071555biological_processcell wall organization
C0102148molecular_functionN-acetyl-beta-D-galactosaminidase activity
D0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
D0004563molecular_functionbeta-N-acetylhexosaminidase activity
D0005737cellular_componentcytoplasm
D0005975biological_processcarbohydrate metabolic process
D0008360biological_processregulation of cell shape
D0009252biological_processpeptidoglycan biosynthetic process
D0009254biological_processpeptidoglycan turnover
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0051301biological_processcell division
D0071555biological_processcell wall organization
D0102148molecular_functionN-acetyl-beta-D-galactosaminidase activity
E0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
E0004563molecular_functionbeta-N-acetylhexosaminidase activity
E0005737cellular_componentcytoplasm
E0005975biological_processcarbohydrate metabolic process
E0008360biological_processregulation of cell shape
E0009252biological_processpeptidoglycan biosynthetic process
E0009254biological_processpeptidoglycan turnover
E0016798molecular_functionhydrolase activity, acting on glycosyl bonds
E0051301biological_processcell division
E0071555biological_processcell wall organization
E0102148molecular_functionN-acetyl-beta-D-galactosaminidase activity
F0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
F0004563molecular_functionbeta-N-acetylhexosaminidase activity
F0005737cellular_componentcytoplasm
F0005975biological_processcarbohydrate metabolic process
F0008360biological_processregulation of cell shape
F0009252biological_processpeptidoglycan biosynthetic process
F0009254biological_processpeptidoglycan turnover
F0016798molecular_functionhydrolase activity, acting on glycosyl bonds
F0051301biological_processcell division
F0071555biological_processcell wall organization
F0102148molecular_functionN-acetyl-beta-D-galactosaminidase activity
Functional Information from PROSITE/UniProt
site_idPS00775
Number of Residues18
DetailsGLYCOSYL_HYDROL_F3 Glycosyl hydrolases family 3 active site. ILRrDigfkGVIFSDdlT
ChainResidueDetails
AILE244-THR261

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00364
ChainResidueDetails
AHIS187
BHIS187
CHIS187
DHIS187
EHIS187
FHIS187

site_idSWS_FT_FI2
Number of Residues6
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00364
ChainResidueDetails
AASP258
BASP258
CASP258
DASP258
EASP258
FASP258

site_idSWS_FT_FI3
Number of Residues24
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00364
ChainResidueDetails
EARG144
ELYS174
FASP69
FARG77
FARG144
FLYS174
AASP69
AARG77
AARG144
ALYS174
BASP69
BARG77
BARG144
BLYS174
CASP69
CARG77
CARG144
CLYS174
DASP69
DARG77
DARG144
DLYS174
EASP69
EARG77

site_idSWS_FT_FI4
Number of Residues6
DetailsSITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_00364
ChainResidueDetails
AASP185
BASP185
CASP185
DASP185
EASP185
FASP185

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PDB entries from 2024-06-12

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