1W2T

beta-fructosidase from Thermotoga maritima in complex with raffinose

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
A	0004564	molecular_function	beta-fructofuranosidase activity
A	0004575	molecular_function	sucrose alpha-glucosidase activity
A	0005975	biological_process	carbohydrate metabolic process
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
B	0004564	molecular_function	beta-fructofuranosidase activity
B	0004575	molecular_function	sucrose alpha-glucosidase activity
B	0005975	biological_process	carbohydrate metabolic process
B	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
C	0004564	molecular_function	beta-fructofuranosidase activity
C	0004575	molecular_function	sucrose alpha-glucosidase activity
C	0005975	biological_process	carbohydrate metabolic process
C	0016787	molecular_function	hydrolase activity
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
D	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
D	0004564	molecular_function	beta-fructofuranosidase activity
D	0004575	molecular_function	sucrose alpha-glucosidase activity
D	0005975	biological_process	carbohydrate metabolic process
D	0016787	molecular_function	hydrolase activity
D	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
E	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
E	0004564	molecular_function	beta-fructofuranosidase activity
E	0004575	molecular_function	sucrose alpha-glucosidase activity
E	0005975	biological_process	carbohydrate metabolic process
E	0016787	molecular_function	hydrolase activity
E	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
F	0004553	molecular_function	hydrolase activity, hydrolyzing O-glycosyl compounds
F	0004564	molecular_function	beta-fructofuranosidase activity
F	0004575	molecular_function	sucrose alpha-glucosidase activity
F	0005975	biological_process	carbohydrate metabolic process
F	0016787	molecular_function	hydrolase activity
F	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds

Functional Information from PROSITE/UniProt

site_id	PS00609
Number of Residues	14
Details	GLYCOSYL_HYDROL_F32 Glycosyl hydrolases family 32 active site. HffPitgwMNDPNG

Chain	Residue	Details
A	HIS7-GLY20

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	ACT_SITE:

Chain	Residue	Details
A	ASP17
B	ASP17
C	ASP17
D	ASP17
E	ASP17
F	ASP17

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site_id	SWS_FT_FI2
Number of Residues	54
Details	BINDING:

Chain	Residue	Details
A	TRP14
B	TRP14
B	GLN33
B	TRP41
B	PHE74
B	TYR92
B	ARG137
B	GLU188
B	THR208
B	TRP260
C	TRP14
A	GLN33
C	GLN33
C	TRP41
C	PHE74
C	TYR92
C	ARG137
C	GLU188
C	THR208
C	TRP260
D	TRP14
D	GLN33
A	TRP41
D	TRP41
D	PHE74
D	TYR92
D	ARG137
D	GLU188
D	THR208
D	TRP260
E	TRP14
E	GLN33
E	TRP41
A	PHE74
E	PHE74
E	TYR92
E	ARG137
E	GLU188
E	THR208
E	TRP260
F	TRP14
F	GLN33
F	TRP41
F	PHE74
A	TYR92
F	TYR92
F	ARG137
F	GLU188
F	THR208
F	TRP260
A	ARG137
A	GLU188
A	THR208
A	TRP260

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1y9m

Chain	Residue	Details
A	ASP17
A	ASP190

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site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1y9m

Chain	Residue	Details
B	ASP17
B	ASP190

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site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1y9m

Chain	Residue	Details
C	ASP17
C	ASP190

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site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1y9m

Chain	Residue	Details
D	ASP17
D	ASP190

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site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1y9m

Chain	Residue	Details
E	ASP17
E	ASP190

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site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1y9m

Chain	Residue	Details
F	ASP17
F	ASP190

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