Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7BZM

Crystal structure of rice Os3BGlu7 with glucoimidazole

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	0004567	molecular_function	beta-mannosidase activity
A	0005576	cellular_component	extracellular region
A	0005975	biological_process	carbohydrate metabolic process
A	0008422	molecular_function	beta-glucosidase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0033907	molecular_function	beta-D-fucosidase activity
A	0042803	molecular_function	protein homodimerization activity
A	0042973	molecular_function	glucan endo-1,3-beta-D-glucosidase activity
A	0047668	molecular_function	amygdalin beta-glucosidase activity
A	0047701	molecular_function	beta-L-arabinosidase activity
A	0050224	molecular_function	prunasin beta-glucosidase activity
A	0080079	molecular_function	cellobiose glucosidase activity
A	0080083	molecular_function	beta-gentiobiose beta-glucosidase activity
A	0102483	molecular_function	scopolin beta-glucosidase activity
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0004565	molecular_function	beta-galactosidase activity
B	0004567	molecular_function	beta-mannosidase activity
B	0005576	cellular_component	extracellular region
B	0005975	biological_process	carbohydrate metabolic process
B	0008422	molecular_function	beta-glucosidase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0033907	molecular_function	beta-D-fucosidase activity
B	0042803	molecular_function	protein homodimerization activity
B	0042973	molecular_function	glucan endo-1,3-beta-D-glucosidase activity
B	0047668	molecular_function	amygdalin beta-glucosidase activity
B	0047701	molecular_function	beta-L-arabinosidase activity
B	0050224	molecular_function	prunasin beta-glucosidase activity
B	0080079	molecular_function	cellobiose glucosidase activity
B	0080083	molecular_function	beta-gentiobiose beta-glucosidase activity
B	0102483	molecular_function	scopolin beta-glucosidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	binding site for residue GIM A 501

Chain	Residue
A	GLN29
A	TRP441
A	PHE449
A	HIS130
A	ASN175
A	GLU176
A	TYR315
A	TRP358
A	GLU386
A	TRP433
A	GLU440

site_id	AC2
Number of Residues	7
Details	binding site for residue MES A 502

Chain	Residue
A	GLY278
A	HIS279
A	TYR280
A	GLN285
A	LYS294
A	PHE295
A	HOH669

site_id	AC3
Number of Residues	4
Details	binding site for residue ZN A 503

Chain	Residue
A	ASP65
A	HIS68
B	ASP65
B	HIS68

site_id	AC4
Number of Residues	4
Details	binding site for residue SO4 A 504

Chain	Residue
A	THR163
A	ASN166
A	ARG167
A	HOH689

site_id	AC5
Number of Residues	11
Details	binding site for residue GIM B 501

Chain	Residue
B	GLN29
B	HIS130
B	ASN175
B	GLU176
B	TYR315
B	TRP358
B	GLU386
B	TRP433
B	GLU440
B	TRP441
B	PHE449

site_id	AC6
Number of Residues	8
Details	binding site for residue MES B 502

Chain	Residue
A	LEU395
B	GLY278
B	HIS279
B	TYR280
B	GLN285
B	LYS294
B	PHE295
B	HOH608

site_id	AC7
Number of Residues	4
Details	binding site for residue SO4 B 503

Chain	Residue
B	THR163
B	ASN166
B	ARG167
B	HOH683

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000269\|PubMed:25252199

Chain	Residue	Details
A	GLU176
B	GLU176

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Nucleophile => ECO:0000269\|PubMed:25252199

Chain	Residue	Details
A	GLU386
B	GLU386

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000305\|PubMed:18308333, ECO:0000305\|PubMed:20884352, ECO:0000305\|PubMed:25252199, ECO:0007744\|PDB:2RGM, ECO:0007744\|PDB:3AHT, ECO:0007744\|PDB:3F5J, ECO:0007744\|PDB:3F5K, ECO:0007744\|PDB:3F5L, ECO:0007744\|PDB:4QLK

Chain	Residue	Details
A	GLN29
A	GLU440
B	GLN29
B	GLU440

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305\|PubMed:20884352, ECO:0000305\|PubMed:25252199, ECO:0007744\|PDB:3AHT, ECO:0007744\|PDB:3F5J, ECO:0007744\|PDB:3F5K, ECO:0007744\|PDB:3F5L, ECO:0007744\|PDB:4QLK

Chain	Residue	Details
A	HIS130
B	HIS130

site_id	SWS_FT_FI5
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305\|PubMed:18308333, ECO:0000305\|PubMed:20884352, ECO:0000305\|PubMed:25252199, ECO:0007744\|PDB:2RGM, ECO:0007744\|PDB:3F5K, ECO:0007744\|PDB:3F5L, ECO:0007744\|PDB:4QLK

Chain	Residue	Details
A	ASN175
B	ASN175

site_id	SWS_FT_FI6
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305\|PubMed:18308333, ECO:0000305\|PubMed:20884352, ECO:0000305\|PubMed:25252199, ECO:0007744\|PDB:2RGM, ECO:0007744\|PDB:3AHT, ECO:0007744\|PDB:3F5K, ECO:0007744\|PDB:3F5L, ECO:0007744\|PDB:4QLK

Chain	Residue	Details
A	TYR315
B	TYR315

site_id	SWS_FT_FI7
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:Q9SPP9

Chain	Residue	Details
A	GLU386
B	GLU386

site_id	SWS_FT_FI8
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305, ECO:0007744\|PDB:3SCW

Chain	Residue	Details
A	TRP433
B	TRP433

site_id	SWS_FT_FI9
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:Q1XH05

Chain	Residue	Details
A	PHE449
B	PHE449

site_id	SWS_FT_FI10
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255\|PROSITE-ProRule:PRU00498

Chain	Residue	Details
A	ASN252
A	ASN394
B	ASN252
B	ASN394

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