5G2M

Crystal structure of NagZ from Pseudomonas aeruginosa in complex with N-acetylglucosamine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0004563	molecular_function	beta-N-acetylhexosaminidase activity
A	0005737	cellular_component	cytoplasm
A	0005975	biological_process	carbohydrate metabolic process
A	0007049	biological_process	cell cycle
A	0008152	biological_process	metabolic process
A	0008360	biological_process	regulation of cell shape
A	0009252	biological_process	peptidoglycan biosynthetic process
A	0009254	biological_process	peptidoglycan turnover
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0046677	biological_process	response to antibiotic
A	0051301	biological_process	cell division
A	0071555	biological_process	cell wall organization
A	0102148	molecular_function	N-acetyl-beta-D-galactosaminidase activity
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0004563	molecular_function	beta-N-acetylhexosaminidase activity
B	0005737	cellular_component	cytoplasm
B	0005975	biological_process	carbohydrate metabolic process
B	0007049	biological_process	cell cycle
B	0008152	biological_process	metabolic process
B	0008360	biological_process	regulation of cell shape
B	0009252	biological_process	peptidoglycan biosynthetic process
B	0009254	biological_process	peptidoglycan turnover
B	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0046677	biological_process	response to antibiotic
B	0051301	biological_process	cell division
B	0071555	biological_process	cell wall organization
B	0102148	molecular_function	N-acetyl-beta-D-galactosaminidase activity

Functional Information from PROSITE/UniProt

site_id	PS00775
Number of Residues	18
Details	GLYCOSYL_HYDROL_F3 Glycosyl hydrolases family 3 active site. ILRgElkfdGVIFSDdlS

Chain	Residue	Details
A	ILE230-SER247

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00364

Chain	Residue	Details
A	HIS174
B	HIS174

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00364

Chain	Residue	Details
A	ASP244
B	ASP244

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00364

Chain	Residue	Details
A	ASP62
A	ARG70
A	ARG131
A	LYS161
B	ASP62
B	ARG70
B	ARG131
B	LYS161

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	SITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_00364

Chain	Residue	Details
A	ASP172
B	ASP172

---