Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1UYP

The three-dimensional structure of beta-fructosidase (invertase) from Thermotoga maritima

Replaces: 1UTW

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	0005975	biological_process	carbohydrate metabolic process
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	0005975	biological_process	carbohydrate metabolic process
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	0005975	biological_process	carbohydrate metabolic process
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	0005975	biological_process	carbohydrate metabolic process
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	0005975	biological_process	carbohydrate metabolic process
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	0005975	biological_process	carbohydrate metabolic process
F	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A1433

Chain	Residue
A	TRP41
A	GLY42
A	ASN43
A	ILE44
A	HIS71
A	ASP94

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A1434

Chain	Residue
A	ARG250
D	ASP249
A	TYR28
A	THR248
A	ASP249

site_id	AC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SO4 A1435

Chain	Residue
A	LEU265

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA A1438

Chain	Residue
A	MET109
A	CIT1436
A	HOH2012

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 B1433

Chain	Residue
B	ARG360
B	HOH2312
C	TYR266
C	PRO267
C	THR268
C	LYS269
C	ARG270

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B1434

Chain	Residue
B	ARG93
B	LYS99
B	LYS102

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B1435

Chain	Residue
B	GLU101
B	GLU103
B	HIS134
B	ALA135
B	ARG137
B	GLU188

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B1437

Chain	Residue
B	TYR28
B	THR248
B	ASP249
B	ARG250

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C1433

Chain	Residue
C	TYR28
C	THR248
C	ASP249
C	ARG250

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C1434

Chain	Residue
C	ARG37
C	LYS38
C	HOH2029
C	HOH2297

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C1435

Chain	Residue
C	GLU101
C	GLU103
C	HIS134
C	ALA135
C	ARG137

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 E1433

Chain	Residue
E	TYR28
E	THR248
E	ASP249
E	ARG250

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 F1433

Chain	Residue
F	LEU1
F	ARG270
F	GLU271

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 F1434

Chain	Residue
F	TYR266
F	PRO267
F	LYS269
F	ARG270
F	HOH2277

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 F1435

Chain	Residue
F	TYR28
F	THR248
F	ASP249
F	ARG250

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CIT A1436

Chain	Residue
A	VAL117
A	LYS118
A	TYR119
A	ASP120
A	NA1438
A	HOH2289

site_id	BC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A1437

Chain	Residue
A	ASN16
A	ASP17
A	GLN33
A	TRP41
A	PHE74
A	SER75
A	ARG137
A	ASP138
A	HOH2014

site_id	BC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B1436

Chain	Residue
B	ASN16
B	ASP17
B	GLN33
B	TRP41
B	PHE74
B	SER75
B	ASP138

site_id	CC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL C1436

Chain	Residue
C	ASN16
C	GLN33
C	TRP41
C	PHE74
C	SER75
C	ARG137
C	HOH2298

site_id	CC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL D1433

Chain	Residue
D	ASP138
D	ASN16
D	ASP17
D	GLN33
D	TRP41
D	PHE74
D	SER75

site_id	CC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL E1434

Chain	Residue
E	ASN16
E	ASP17
E	GLN33
E	TRP41
E	PHE74
E	SER75
E	ARG137
E	ASP138

site_id	CC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL F1436

Chain	Residue
F	ASN16
F	ASP17
F	GLN33
F	TRP41
F	PHE74
F	SER75
F	ASP138

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

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

site_id	SWS_FT_FI2
Number of Residues	54
Details	BINDING:

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

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