Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3WEZ

Crystal structure of human beta-galactosidase in complex with NOEV

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0004565	molecular_function	beta-galactosidase activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005737	cellular_component	cytoplasm
A	0005764	cellular_component	lysosome
A	0005773	cellular_component	vacuole
A	0005794	cellular_component	Golgi apparatus
A	0005975	biological_process	carbohydrate metabolic process
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0016936	molecular_function	galactoside binding
A	0019388	biological_process	galactose catabolic process
A	0030200	biological_process	heparan sulfate proteoglycan catabolic process
A	0035578	cellular_component	azurophil granule lumen
A	0042340	biological_process	keratan sulfate catabolic process
A	0042803	molecular_function	protein homodimerization activity
A	0043202	cellular_component	lysosomal lumen
A	0043231	cellular_component	intracellular membrane-bounded organelle
A	0046479	biological_process	glycosphingolipid catabolic process
A	0048471	cellular_component	perinuclear region of cytoplasm
A	0051413	biological_process	response to cortisone
A	0070062	cellular_component	extracellular exosome
A	1904016	biological_process	response to Thyroglobulin triiodothyronine
A	1904813	cellular_component	ficolin-1-rich granule lumen
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0004565	molecular_function	beta-galactosidase activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0005737	cellular_component	cytoplasm
B	0005764	cellular_component	lysosome
B	0005773	cellular_component	vacuole
B	0005794	cellular_component	Golgi apparatus
B	0005975	biological_process	carbohydrate metabolic process
B	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0016936	molecular_function	galactoside binding
B	0019388	biological_process	galactose catabolic process
B	0030200	biological_process	heparan sulfate proteoglycan catabolic process
B	0035578	cellular_component	azurophil granule lumen
B	0042340	biological_process	keratan sulfate catabolic process
B	0042803	molecular_function	protein homodimerization activity
B	0043202	cellular_component	lysosomal lumen
B	0043231	cellular_component	intracellular membrane-bounded organelle
B	0046479	biological_process	glycosphingolipid catabolic process
B	0048471	cellular_component	perinuclear region of cytoplasm
B	0051413	biological_process	response to cortisone
B	0070062	cellular_component	extracellular exosome
B	1904016	biological_process	response to Thyroglobulin triiodothyronine
B	1904813	cellular_component	ficolin-1-rich granule lumen
C	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
C	0004565	molecular_function	beta-galactosidase activity
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005615	cellular_component	extracellular space
C	0005737	cellular_component	cytoplasm
C	0005764	cellular_component	lysosome
C	0005773	cellular_component	vacuole
C	0005794	cellular_component	Golgi apparatus
C	0005975	biological_process	carbohydrate metabolic process
C	0016787	molecular_function	hydrolase activity
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0016936	molecular_function	galactoside binding
C	0019388	biological_process	galactose catabolic process
C	0030200	biological_process	heparan sulfate proteoglycan catabolic process
C	0035578	cellular_component	azurophil granule lumen
C	0042340	biological_process	keratan sulfate catabolic process
C	0042803	molecular_function	protein homodimerization activity
C	0043202	cellular_component	lysosomal lumen
C	0043231	cellular_component	intracellular membrane-bounded organelle
C	0046479	biological_process	glycosphingolipid catabolic process
C	0048471	cellular_component	perinuclear region of cytoplasm
C	0051413	biological_process	response to cortisone
C	0070062	cellular_component	extracellular exosome
C	1904016	biological_process	response to Thyroglobulin triiodothyronine
C	1904813	cellular_component	ficolin-1-rich granule lumen
D	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
D	0004565	molecular_function	beta-galactosidase activity
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0005615	cellular_component	extracellular space
D	0005737	cellular_component	cytoplasm
D	0005764	cellular_component	lysosome
D	0005773	cellular_component	vacuole
D	0005794	cellular_component	Golgi apparatus
D	0005975	biological_process	carbohydrate metabolic process
D	0016787	molecular_function	hydrolase activity
D	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
D	0016936	molecular_function	galactoside binding
D	0019388	biological_process	galactose catabolic process
D	0030200	biological_process	heparan sulfate proteoglycan catabolic process
D	0035578	cellular_component	azurophil granule lumen
D	0042340	biological_process	keratan sulfate catabolic process
D	0042803	molecular_function	protein homodimerization activity
D	0043202	cellular_component	lysosomal lumen
D	0043231	cellular_component	intracellular membrane-bounded organelle
D	0046479	biological_process	glycosphingolipid catabolic process
D	0048471	cellular_component	perinuclear region of cytoplasm
D	0051413	biological_process	response to cortisone
D	0070062	cellular_component	extracellular exosome
D	1904016	biological_process	response to Thyroglobulin triiodothyronine
D	1904813	cellular_component	ficolin-1-rich granule lumen

Functional Information from PROSITE/UniProt

site_id	PS01182
Number of Residues	13
Details	GLYCOSYL_HYDROL_F35 Glycosyl hydrolases family 35 putative active site. GGPVItvQvENEY

Chain	Residue	Details
A	GLY177-TYR189

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton donor => ECO:0000305\|PubMed:22128166

Chain	Residue	Details
A	GLU188
B	GLU188
C	GLU188
D	GLU188

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Nucleophile => ECO:0000305\|PubMed:22128166

Chain	Residue	Details
A	GLU268
B	GLU268
C	GLU268
D	GLU268

site_id	SWS_FT_FI3
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269\|PubMed:22128166, ECO:0000269\|PubMed:24737316, ECO:0007744\|PDB:3THC, ECO:0007744\|PDB:3WF3

Chain	Residue	Details
A	TYR83
C	GLU129
C	ASN187
C	TYR333
D	TYR83
D	GLU129
D	ASN187
D	TYR333
A	GLU129
A	ASN187
A	TYR333
B	TYR83
B	GLU129
B	ASN187
B	TYR333
C	TYR83

site_id	SWS_FT_FI4
Number of Residues	12
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN26
D	ASN26
D	ASN542
D	ASN545
A	ASN542
A	ASN545
B	ASN26
B	ASN542
B	ASN545
C	ASN26
C	ASN542
C	ASN545

site_id	SWS_FT_FI5
Number of Residues	8
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:22128166, ECO:0000269\|PubMed:24737316, ECO:0007744\|PDB:3THC, ECO:0007744\|PDB:3THD, ECO:0007744\|PDB:3WEZ, ECO:0007744\|PDB:3WF0, ECO:0007744\|PDB:3WF1, ECO:0007744\|PDB:3WF2, ECO:0007744\|PDB:3WF3, ECO:0007744\|PDB:3WF4

Chain	Residue	Details
A	ASN247
A	ASN498
B	ASN247
B	ASN498
C	ASN247
C	ASN498
D	ASN247
D	ASN498

site_id	SWS_FT_FI6
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:16263699, ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:22128166, ECO:0000269\|PubMed:24737316, ECO:0007744\|PDB:3THC, ECO:0007744\|PDB:3THD, ECO:0007744\|PDB:3WEZ, ECO:0007744\|PDB:3WF0, ECO:0007744\|PDB:3WF1, ECO:0007744\|PDB:3WF2, ECO:0007744\|PDB:3WF3, ECO:0007744\|PDB:3WF4

Chain	Residue	Details
A	ASN464
B	ASN464
C	ASN464
D	ASN464

site_id	SWS_FT_FI7
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:22128166, ECO:0000269\|PubMed:24737316, ECO:0007744\|PDB:3THC, ECO:0007744\|PDB:3THD, ECO:0007744\|PDB:3WEZ, ECO:0007744\|PDB:3WF0, ECO:0007744\|PDB:3WF1, ECO:0007744\|PDB:3WF2, ECO:0007744\|PDB:3WF3, ECO:0007744\|PDB:3WF4

Chain	Residue	Details
A	ASN555
B	ASN555
C	ASN555
D	ASN555

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