Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5LY7

Crystal structure of NagZ H174A mutant from Pseudomonas aeruginosa in complex with the inhibitor 2-acetamido-1,2-dideoxynojirimycin

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
A0046677biological_processresponse to antibiotic
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
B0046677biological_processresponse to antibiotic
B0051301biological_processcell division
B0071555biological_processcell wall organization
B0102148molecular_functionN-acetyl-beta-D-galactosaminidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue PEG A 401
ChainResidue
AGLN289
AARG290
BARG290

site_idAC2
Number of Residues7
Detailsbinding site for residue NOK A 402
ChainResidue
AMET248
APHE33
AASP62
AARG131
ALYS161
AHIS162
AASP244

site_idAC3
Number of Residues6
Detailsbinding site for residue PEG B 401
ChainResidue
AGLN73
AARG77
BARG77
BLEU330
BILE331
BASP332

site_idAC4
Number of Residues8
Detailsbinding site for residue NOK B 402
ChainResidue
BPHE33
BASP62
BARG131
BLYS161
BHIS162
BHIS166
BASP244
BMET248

Functional Information from PROSITE/UniProt
site_idPS00775
Number of Residues18
DetailsGLYCOSYL_HYDROL_F3 Glycosyl hydrolases family 3 active site. ILRgElkfdGVIFSDdlS
ChainResidueDetails
AILE230-SER247

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00364
ChainResidueDetails
AALA174
BALA174

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00364
ChainResidueDetails
AASP244
BASP244

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00364
ChainResidueDetails
AASP62
AARG70
AARG131
ALYS161
BASP62
BARG70
BARG131
BLYS161

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_00364
ChainResidueDetails
AASP172
BASP172

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon