4GZE

Crystal structure of 6-phospho-beta-glucosidase from Lactobacillus plantarum (apo form)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0005829	cellular_component	cytosol
A	0005975	biological_process	carbohydrate metabolic process
A	0008422	molecular_function	beta-glucosidase activity
A	0008706	molecular_function	6-phospho-beta-glucosidase activity
A	0016052	biological_process	carbohydrate catabolic process
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0005829	cellular_component	cytosol
B	0005975	biological_process	carbohydrate metabolic process
B	0008422	molecular_function	beta-glucosidase activity
B	0008706	molecular_function	6-phospho-beta-glucosidase activity
B	0016052	biological_process	carbohydrate catabolic process
B	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
C	0005829	cellular_component	cytosol
C	0005975	biological_process	carbohydrate metabolic process
C	0008422	molecular_function	beta-glucosidase activity
C	0008706	molecular_function	6-phospho-beta-glucosidase activity
C	0016052	biological_process	carbohydrate catabolic process
C	0016787	molecular_function	hydrolase activity
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
D	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
D	0005829	cellular_component	cytosol
D	0005975	biological_process	carbohydrate metabolic process
D	0008422	molecular_function	beta-glucosidase activity
D	0008706	molecular_function	6-phospho-beta-glucosidase activity
D	0016052	biological_process	carbohydrate catabolic process
D	0016787	molecular_function	hydrolase activity
D	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
E	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
E	0005829	cellular_component	cytosol
E	0005975	biological_process	carbohydrate metabolic process
E	0008422	molecular_function	beta-glucosidase activity
E	0008706	molecular_function	6-phospho-beta-glucosidase activity
E	0016052	biological_process	carbohydrate catabolic process
E	0016787	molecular_function	hydrolase activity
E	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
F	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
F	0005829	cellular_component	cytosol
F	0005975	biological_process	carbohydrate metabolic process
F	0008422	molecular_function	beta-glucosidase activity
F	0008706	molecular_function	6-phospho-beta-glucosidase activity
F	0016052	biological_process	carbohydrate catabolic process
F	0016787	molecular_function	hydrolase activity
F	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL A 501

Chain	Residue
A	ARG366

---

site_id	AC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL A 502

Chain	Residue
A	HIS21

---

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A 503

Chain	Residue
A	MSE318
A	SER319

---

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL D 501

Chain	Residue
D	MSE318
D	SER319

---

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL D 502

Chain	Residue
D	HIS21
D	ALA431
D	HOH658

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL D 503

Chain	Residue
C	TRP362
C	ARG366
C	HOH508
D	TRP362
D	ARG366

---

Functional Information from PROSITE/UniProt

site_id	PS00572
Number of Residues	9
Details	GLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. LFIVENGLG

Chain	Residue	Details
A	LEU371-GLY379

---

site_id	PS00653
Number of Residues	15
Details	GLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FlWGgAvAAHQlEgG

Chain	Residue	Details
A	PHE12-GLY26

---