Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1HN1

E. COLI (LAC Z) BETA-GALACTOSIDASE (ORTHORHOMBIC)

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	0008152	biological_process	metabolic process
A	0009341	cellular_component	beta-galactosidase complex
A	0016787	molecular_function	hydrolase activity
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
A	1901575	biological_process	organic substance catabolic process
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	0008152	biological_process	metabolic process
B	0009341	cellular_component	beta-galactosidase complex
B	0016787	molecular_function	hydrolase activity
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
B	1901575	biological_process	organic substance catabolic process
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	0008152	biological_process	metabolic process
C	0009341	cellular_component	beta-galactosidase complex
C	0016787	molecular_function	hydrolase activity
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
C	1901575	biological_process	organic substance catabolic process
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	0008152	biological_process	metabolic process
D	0009341	cellular_component	beta-galactosidase complex
D	0016787	molecular_function	hydrolase activity
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
D	1901575	biological_process	organic substance catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 3001

Chain	Residue
A	ASN102
A	ASP201
A	GLU416
A	HIS418
A	GLU461

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 3002

Chain	Residue
A	ASP193
A	ASP15
A	ASN18
A	VAL21
A	GLN163

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA A 3101

Chain	Residue
A	ASP201
A	PHE601
A	ASN604

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA A 3102

Chain	Residue
A	PHE556
A	TYR559
A	PRO560
A	LEU562

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG B 3001

Chain	Residue
B	ASN102
B	GLU416
B	HIS418
B	GLU461

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 3002

Chain	Residue
B	ASP15
B	ASN18
B	VAL21
B	GLN163
B	ASP193

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA B 3102

Chain	Residue
B	PHE556
B	TYR559
B	PRO560
B	LEU562

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA B 3103

Chain	Residue
B	PHE931
B	PRO932
B	LEU967
B	THR970

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG C 3001

Chain	Residue
C	ASN102
C	GLU416
C	HIS418
C	GLU461

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 3002

Chain	Residue
C	ASP15
C	ASN18
C	VAL21
C	GLN163
C	ASP193

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA C 3101

Chain	Residue
C	ASP201
C	PHE601
C	ASN604

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA C 3102

Chain	Residue
C	PHE556
C	TYR559
C	PRO560
C	LEU562

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG D 3001

Chain	Residue
D	ASN102
D	GLU416
D	HIS418
D	GLU461

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 3002

Chain	Residue
D	ASP15
D	ASN18
D	VAL21
D	GLN163
D	ASP193

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA D 3102

Chain	Residue
D	PHE556
D	TYR559
D	LEU562

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	SER462
B	SER462
C	SER462
D	SER462

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

Chain	Residue	Details
A	TYR538
B	TYR538
C	TYR538
D	TYR538

site_id	SWS_FT_FI3
Number of Residues	28
Details	BINDING:

Chain	Residue	Details
A	VAL103
B	SER462
B	TYR538
B	CYS602
B	GLY605
B	SER1000
C	VAL103
C	MET202
C	SER462
C	TYR538
C	CYS602
A	MET202
C	GLY605
C	SER1000
D	VAL103
D	MET202
D	SER462
D	TYR538
D	CYS602
D	GLY605
D	SER1000
A	SER462
A	TYR538
A	CYS602
A	GLY605
A	SER1000
B	VAL103
B	MET202

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

Chain	Residue	Details
A	THR417
D	THR417
D	GLY419
D	ASP598
A	GLY419
A	ASP598
B	THR417
B	GLY419
B	ASP598
C	THR417
C	GLY419
C	ASP598

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

Chain	Residue	Details
A	GLU358
A	TYR392
B	GLU358
B	TYR392
C	GLU358
C	TYR392
D	GLU358
D	TYR392

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	SER1000
B	SER1000
C	SER1000
D	SER1000

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	10
Details	M-CSA 422

Chain	Residue	Details
A	MET202
A	GLY605
A	GLU358
A	TYR392
A	THR417
A	GLY419
A	SER462
A	TYR538
A	ASP598
A	CYS602

site_id	MCSA2
Number of Residues	10
Details	M-CSA 422

Chain	Residue	Details
B	MET202
B	GLY605
B	GLU358
B	TYR392
B	THR417
B	GLY419
B	SER462
B	TYR538
B	ASP598
B	CYS602

site_id	MCSA3
Number of Residues	10
Details	M-CSA 422

Chain	Residue	Details
C	MET202
C	GLY605
C	GLU358
C	TYR392
C	THR417
C	GLY419
C	SER462
C	TYR538
C	ASP598
C	CYS602

site_id	MCSA4
Number of Residues	10
Details	M-CSA 422

Chain	Residue	Details
D	MET202
D	GLY605
D	GLU358
D	TYR392
D	THR417
D	GLY419
D	SER462
D	TYR538
D	ASP598
D	CYS602

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