Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3WDP

Structural analysis of a beta-glucosidase mutant derived from a hyperthermophilic tetrameric structure

Functional Information from GO Data

Chain	GOid	namespace	contents
P	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
P	0005975	biological_process	carbohydrate metabolic process
P	0008422	molecular_function	beta-glucosidase activity
P	0016787	molecular_function	hydrolase activity
P	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
Q	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
Q	0005975	biological_process	carbohydrate metabolic process
Q	0008422	molecular_function	beta-glucosidase activity
Q	0016787	molecular_function	hydrolase activity
Q	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
R	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
R	0005975	biological_process	carbohydrate metabolic process
R	0008422	molecular_function	beta-glucosidase activity
R	0016787	molecular_function	hydrolase activity
R	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
S	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
S	0005975	biological_process	carbohydrate metabolic process
S	0008422	molecular_function	beta-glucosidase activity
S	0016787	molecular_function	hydrolase activity
S	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL P 501

Chain	Residue
P	GLN17
P	GOL504
P	HIS150
P	ASN206
P	GLU207
P	GLU372
P	TRP410
P	GLU417
P	TRP418
P	GOL503

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL P 502

Chain	Residue
P	THR143
P	MET201
P	HOH928
P	HOH978

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL P 503

Chain	Residue
P	PHE344
P	GLU417
P	GOL501
P	GOL504
P	HOH622
P	HOH903

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL P 504

Chain	Residue
P	GLU207
P	ALA264
P	TYR307
P	GOL501
P	GOL503
P	HOH714

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 P 505

Chain	Residue
P	PHE422
P	ARG425
P	HOH803
P	HOH936
P	HOH1013
Q	PHE468

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 P 506

Chain	Residue
P	PHE91
P	LYS179
P	GLU183
P	LYS186
P	HOH687
P	HOH1021

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 P 507

Chain	Residue
P	ASN213
P	LYS237
P	HOH621
P	HOH676
P	HOH844
P	HOH845

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 P 508

Chain	Residue
P	ILE106
P	LYS298
P	HOH619
P	HOH734
P	HOH736

site_id	AC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL Q 501

Chain	Residue
Q	GLN17
Q	HIS150
Q	ASN206
Q	GLU207
Q	GLU372
Q	TRP410
Q	GLU417
Q	TRP418
Q	GOL502
Q	GOL503

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL Q 502

Chain	Residue
Q	PHE344
Q	GLU417
Q	GOL501
Q	GOL503
Q	HOH626

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL Q 503

Chain	Residue
Q	GLU207
Q	VAL210
Q	ALA264
Q	TYR307
Q	GOL501
Q	GOL502
Q	HOH712

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 Q 504

Chain	Residue
Q	ASP37
Q	GLU39
Q	ILE161
Q	LYS165
Q	HOH786

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 Q 505

Chain	Residue
P	PHE468
Q	PHE422
Q	ARG425
Q	HOH797
Q	HOH798
Q	HOH1014

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 Q 506

Chain	Residue
Q	PHE91
Q	LYS94
Q	LYS179
Q	GLU183
Q	LYS186
Q	HOH706
Q	HOH980

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 Q 507

Chain	Residue
Q	ASN213
Q	LYS237
Q	HOH612
Q	HOH676
Q	HOH869
Q	HOH892

site_id	BC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL R 501

Chain	Residue
R	GLU372
R	TRP410
R	GLU417
R	TRP418
R	GOL503
R	GLN17
R	HIS150
R	ASN206
R	GLU207

site_id	BC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL R 502

Chain	Residue
Q	GLU128
Q	ARG131
R	ARG131
R	LYS132
R	SER135
R	HOH665
R	HOH874

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL R 503

Chain	Residue
R	GLU207
R	VAL210
R	TYR307
R	GOL501
R	HOH869

site_id	CC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 R 504

Chain	Residue
R	PHE91
R	LYS94
R	LYS179
R	VAL182
R	GLU183
R	LYS186
R	HOH685
R	HOH790

site_id	CC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 R 505

Chain	Residue
R	TYR212
R	ASN213
R	GLU234
R	LYS237
R	HOH656
R	HOH892

site_id	CC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 R 506

Chain	Residue
R	ASP269
R	PRO270
R	ARG309
R	HOH831

site_id	CC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL S 501

Chain	Residue
S	GLN17
S	HIS150
S	ASN206
S	GLU207
S	GLU372
S	TRP410
S	GLU417
S	TRP418

site_id	CC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 S 502

Chain	Residue
S	PHE91
S	LYS179
S	VAL182
S	GLU183
S	LYS186
S	HOH710
S	HOH829

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
P	MET368-ALA376

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

Chain	Residue	Details
P	PHE7-GLY21

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