Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3T09

E. coli (LacZ) beta-galactosidase (S796A) galactonolactone complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0003824	molecular_function	catalytic activity
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0004565	molecular_function	beta-galactosidase activity
A	0005975	biological_process	carbohydrate metabolic process
A	0005990	biological_process	lactose catabolic process
A	0009056	biological_process	catabolic process
A	0009341	cellular_component	beta-galactosidase complex
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0030246	molecular_function	carbohydrate binding
A	0031420	molecular_function	alkali metal ion binding
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
B	0000287	molecular_function	magnesium ion binding
B	0003824	molecular_function	catalytic activity
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0004565	molecular_function	beta-galactosidase activity
B	0005975	biological_process	carbohydrate metabolic process
B	0005990	biological_process	lactose catabolic process
B	0009056	biological_process	catabolic process
B	0009341	cellular_component	beta-galactosidase complex
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0030246	molecular_function	carbohydrate binding
B	0031420	molecular_function	alkali metal ion binding
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
C	0000287	molecular_function	magnesium ion binding
C	0003824	molecular_function	catalytic activity
C	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
C	0004565	molecular_function	beta-galactosidase activity
C	0005975	biological_process	carbohydrate metabolic process
C	0005990	biological_process	lactose catabolic process
C	0009056	biological_process	catabolic process
C	0009341	cellular_component	beta-galactosidase complex
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0030246	molecular_function	carbohydrate binding
C	0031420	molecular_function	alkali metal ion binding
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
D	0000287	molecular_function	magnesium ion binding
D	0003824	molecular_function	catalytic activity
D	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
D	0004565	molecular_function	beta-galactosidase activity
D	0005975	biological_process	carbohydrate metabolic process
D	0005990	biological_process	lactose catabolic process
D	0009056	biological_process	catabolic process
D	0009341	cellular_component	beta-galactosidase complex
D	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
D	0030246	molecular_function	carbohydrate binding
D	0031420	molecular_function	alkali metal ion binding
D	0042802	molecular_function	identical protein binding
D	0046872	molecular_function	metal ion binding

Functional Information from PROSITE/UniProt

site_id	PS00608
Number of Residues	15
Details	GLYCOSYL_HYDROL_F2_2 Glycosyl hydrolases family 2 acid/base catalyst. DRNHPSVIIWSlg.NE

Chain	Residue	Details
A	ASP447-GLU461

site_id	PS00719
Number of Residues	26
Details	GLYCOSYL_HYDROL_F2_1 Glycosyl hydrolases family 2 signature 1. NaVRCSHYPnhplWYtlcDryGLYVV

Chain	Residue	Details
A	ASN385-VAL410

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton donor => ECO:0000269\|PubMed:6420154

Chain	Residue	Details
A	GLU461
B	GLU461
C	GLU461
D	GLU461

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Nucleophile => ECO:0000269\|PubMed:1350782

Chain	Residue	Details
A	GLU537
B	GLU537
C	GLU537
D	GLU537

site_id	SWS_FT_FI3
Number of Residues	28
Details	BINDING:

Chain	Residue	Details
A	ASN102
B	GLU461
B	GLU537
B	PHE601
B	ASN604
B	TRP999
C	ASN102
C	ASP201
C	GLU461
C	GLU537
C	PHE601
A	ASP201
C	ASN604
C	TRP999
D	ASN102
D	ASP201
D	GLU461
D	GLU537
D	PHE601
D	ASN604
D	TRP999
A	GLU461
A	GLU537
A	PHE601
A	ASN604
A	TRP999
B	ASN102
B	ASP201

site_id	SWS_FT_FI4
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:11045615

Chain	Residue	Details
A	GLU416
D	GLU416
D	HIS418
D	ASN597
A	HIS418
A	ASN597
B	GLU416
B	HIS418
B	ASN597
C	GLU416
C	HIS418
C	ASN597

site_id	SWS_FT_FI5
Number of Residues	8
Details	SITE: Transition state stabilizer

Chain	Residue	Details
A	HIS357
A	HIS391
B	HIS357
B	HIS391
C	HIS357
C	HIS391
D	HIS357
D	HIS391

site_id	SWS_FT_FI6
Number of Residues	4
Details	SITE: Important for ensuring that an appropriate proportion of lactose is converted to allolactose

Chain	Residue	Details
A	TRP999
B	TRP999
C	TRP999
D	TRP999

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	10
Details	M-CSA 422

Chain	Residue	Details
A	ASP201
A	ASN604
A	HIS357
A	HIS391
A	GLU416
A	HIS418
A	GLU461
A	GLU537
A	ASN597
A	PHE601

site_id	MCSA2
Number of Residues	10
Details	M-CSA 422

Chain	Residue	Details
B	ASP201
B	ASN604
B	HIS357
B	HIS391
B	GLU416
B	HIS418
B	GLU461
B	GLU537
B	ASN597
B	PHE601

site_id	MCSA3
Number of Residues	10
Details	M-CSA 422

Chain	Residue	Details
C	ASP201
C	ASN604
C	HIS357
C	HIS391
C	GLU416
C	HIS418
C	GLU461
C	GLU537
C	ASN597
C	PHE601

site_id	MCSA4
Number of Residues	10
Details	M-CSA 422

Chain	Residue	Details
D	ASP201
D	ASN604
D	HIS357
D	HIS391
D	GLU416
D	HIS418
D	GLU461
D	GLU537
D	ASN597
D	PHE601

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)