Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3R8R

Transaldolase from Bacillus subtilis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004801	molecular_function	transaldolase activity
A	0005737	cellular_component	cytoplasm
A	0005975	biological_process	carbohydrate metabolic process
A	0006098	biological_process	pentose-phosphate shunt
A	0016740	molecular_function	transferase activity
A	0016832	molecular_function	aldehyde-lyase activity
A	0042802	molecular_function	identical protein binding
B	0004801	molecular_function	transaldolase activity
B	0005737	cellular_component	cytoplasm
B	0005975	biological_process	carbohydrate metabolic process
B	0006098	biological_process	pentose-phosphate shunt
B	0016740	molecular_function	transferase activity
B	0016832	molecular_function	aldehyde-lyase activity
B	0042802	molecular_function	identical protein binding
C	0004801	molecular_function	transaldolase activity
C	0005737	cellular_component	cytoplasm
C	0005975	biological_process	carbohydrate metabolic process
C	0006098	biological_process	pentose-phosphate shunt
C	0016740	molecular_function	transferase activity
C	0016832	molecular_function	aldehyde-lyase activity
C	0042802	molecular_function	identical protein binding
D	0004801	molecular_function	transaldolase activity
D	0005737	cellular_component	cytoplasm
D	0005975	biological_process	carbohydrate metabolic process
D	0006098	biological_process	pentose-phosphate shunt
D	0016740	molecular_function	transferase activity
D	0016832	molecular_function	aldehyde-lyase activity
D	0042802	molecular_function	identical protein binding
E	0004801	molecular_function	transaldolase activity
E	0005737	cellular_component	cytoplasm
E	0005975	biological_process	carbohydrate metabolic process
E	0006098	biological_process	pentose-phosphate shunt
E	0016740	molecular_function	transferase activity
E	0016832	molecular_function	aldehyde-lyase activity
E	0042802	molecular_function	identical protein binding
F	0004801	molecular_function	transaldolase activity
F	0005737	cellular_component	cytoplasm
F	0005975	biological_process	carbohydrate metabolic process
F	0006098	biological_process	pentose-phosphate shunt
F	0016740	molecular_function	transferase activity
F	0016832	molecular_function	aldehyde-lyase activity
F	0042802	molecular_function	identical protein binding
G	0004801	molecular_function	transaldolase activity
G	0005737	cellular_component	cytoplasm
G	0005975	biological_process	carbohydrate metabolic process
G	0006098	biological_process	pentose-phosphate shunt
G	0016740	molecular_function	transferase activity
G	0016832	molecular_function	aldehyde-lyase activity
G	0042802	molecular_function	identical protein binding
H	0004801	molecular_function	transaldolase activity
H	0005737	cellular_component	cytoplasm
H	0005975	biological_process	carbohydrate metabolic process
H	0006098	biological_process	pentose-phosphate shunt
H	0016740	molecular_function	transferase activity
H	0016832	molecular_function	aldehyde-lyase activity
H	0042802	molecular_function	identical protein binding
I	0004801	molecular_function	transaldolase activity
I	0005737	cellular_component	cytoplasm
I	0005975	biological_process	carbohydrate metabolic process
I	0006098	biological_process	pentose-phosphate shunt
I	0016740	molecular_function	transferase activity
I	0016832	molecular_function	aldehyde-lyase activity
I	0042802	molecular_function	identical protein binding
J	0004801	molecular_function	transaldolase activity
J	0005737	cellular_component	cytoplasm
J	0005975	biological_process	carbohydrate metabolic process
J	0006098	biological_process	pentose-phosphate shunt
J	0016740	molecular_function	transferase activity
J	0016832	molecular_function	aldehyde-lyase activity
J	0042802	molecular_function	identical protein binding
K	0004801	molecular_function	transaldolase activity
K	0005737	cellular_component	cytoplasm
K	0005975	biological_process	carbohydrate metabolic process
K	0006098	biological_process	pentose-phosphate shunt
K	0016740	molecular_function	transferase activity
K	0016832	molecular_function	aldehyde-lyase activity
K	0042802	molecular_function	identical protein binding
L	0004801	molecular_function	transaldolase activity
L	0005737	cellular_component	cytoplasm
L	0005975	biological_process	carbohydrate metabolic process
L	0006098	biological_process	pentose-phosphate shunt
L	0016740	molecular_function	transferase activity
L	0016832	molecular_function	aldehyde-lyase activity
L	0042802	molecular_function	identical protein binding
M	0004801	molecular_function	transaldolase activity
M	0005737	cellular_component	cytoplasm
M	0005975	biological_process	carbohydrate metabolic process
M	0006098	biological_process	pentose-phosphate shunt
M	0016740	molecular_function	transferase activity
M	0016832	molecular_function	aldehyde-lyase activity
M	0042802	molecular_function	identical protein binding
N	0004801	molecular_function	transaldolase activity
N	0005737	cellular_component	cytoplasm
N	0005975	biological_process	carbohydrate metabolic process
N	0006098	biological_process	pentose-phosphate shunt
N	0016740	molecular_function	transferase activity
N	0016832	molecular_function	aldehyde-lyase activity
N	0042802	molecular_function	identical protein binding
P	0004801	molecular_function	transaldolase activity
P	0005737	cellular_component	cytoplasm
P	0005975	biological_process	carbohydrate metabolic process
P	0006098	biological_process	pentose-phosphate shunt
P	0016740	molecular_function	transferase activity
P	0016832	molecular_function	aldehyde-lyase activity
P	0042802	molecular_function	identical protein binding
R	0004801	molecular_function	transaldolase activity
R	0005737	cellular_component	cytoplasm
R	0005975	biological_process	carbohydrate metabolic process
R	0006098	biological_process	pentose-phosphate shunt
R	0016740	molecular_function	transferase activity
R	0016832	molecular_function	aldehyde-lyase activity
R	0042802	molecular_function	identical protein binding
T	0004801	molecular_function	transaldolase activity
T	0005737	cellular_component	cytoplasm
T	0005975	biological_process	carbohydrate metabolic process
T	0006098	biological_process	pentose-phosphate shunt
T	0016740	molecular_function	transferase activity
T	0016832	molecular_function	aldehyde-lyase activity
T	0042802	molecular_function	identical protein binding
U	0004801	molecular_function	transaldolase activity
U	0005737	cellular_component	cytoplasm
U	0005975	biological_process	carbohydrate metabolic process
U	0006098	biological_process	pentose-phosphate shunt
U	0016740	molecular_function	transferase activity
U	0016832	molecular_function	aldehyde-lyase activity
U	0042802	molecular_function	identical protein binding
V	0004801	molecular_function	transaldolase activity
V	0005737	cellular_component	cytoplasm
V	0005975	biological_process	carbohydrate metabolic process
V	0006098	biological_process	pentose-phosphate shunt
V	0016740	molecular_function	transferase activity
V	0016832	molecular_function	aldehyde-lyase activity
V	0042802	molecular_function	identical protein binding
W	0004801	molecular_function	transaldolase activity
W	0005737	cellular_component	cytoplasm
W	0005975	biological_process	carbohydrate metabolic process
W	0006098	biological_process	pentose-phosphate shunt
W	0016740	molecular_function	transferase activity
W	0016832	molecular_function	aldehyde-lyase activity
W	0042802	molecular_function	identical protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 221

Chain	Residue
A	ASP6
A	ASN28
A	LYS84
A	PHE130
A	ALA164
A	SER165
A	SO4301

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A 301

Chain	Residue
A	ARG167
A	GOL221
A	HOH1036
A	HOH2390
A	HOH2431
A	ARG133
A	SER165

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 301

Chain	Residue
B	ARG133
B	SER165
B	ARG167
B	GOL221
B	HOH349

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B 221

Chain	Residue
B	ASP6
B	ASN28
B	LYS84
B	PHE130
B	ALA164
B	SER165
B	SO4301

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 301

Chain	Residue
C	ARG133
C	SER165
C	ARG167
C	HOH3338

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 D 301

Chain	Residue
D	ARG133
D	SER165
D	ARG167

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 E 301

Chain	Residue
E	ARG133
E	SER165
E	ARG167
E	GOL221
E	HOH935

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 F 301

Chain	Residue
F	ARG133
F	SER165
F	ARG167
F	GOL221
F	HOH1992

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL E 221

Chain	Residue
E	ASP6
E	ASN28
E	LYS84
E	PHE130
E	ALA164
E	SER165
E	SO4301

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 G 301

Chain	Residue
G	ARG133
G	SER165
G	ARG167
G	HOH2688

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 H 301

Chain	Residue
H	ARG133
H	SER165
H	ARG167
H	HOH2522

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL F 221

Chain	Residue
F	ASP6
F	ASN28
F	LYS84
F	PHE130
F	SER165
F	SO4301

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 I 301

Chain	Residue
I	ARG133
I	SER165
I	ARG167

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 J 301

Chain	Residue
J	ARG133
J	SER165
J	ARG167

site_id	BC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL G 221

Chain	Residue
G	ASP6
G	ASN28
G	LYS84
G	PHE130
G	ALA164
G	SER165
G	HOH214

site_id	BC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 V 301

Chain	Residue
V	ARG133
V	SER165
V	ARG167
V	GOL221
V	HOH683
V	HOH1877
V	HOH3214

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 K 301

Chain	Residue
K	ARG133
K	SER165
K	ARG167
K	HOH1965

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 L 301

Chain	Residue
L	ARG133
L	SER165
L	ARG167
L	GOL221

site_id	CC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 M 301

Chain	Residue
M	ARG133
M	SER165
M	ARG167

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 N 301

Chain	Residue
N	HOH3317
N	ARG133
N	SER165
N	ARG167
N	HOH2996

site_id	CC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL V 221

Chain	Residue
V	ASP6
V	ASN28
V	LYS84
V	PHE130
V	ALA164
V	SER165
V	SO4301

site_id	CC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 W 301

Chain	Residue
W	ARG133
W	SER165
W	ARG167
W	GOL221

site_id	CC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 P 301

Chain	Residue
P	ARG133
P	SER165
P	ARG167
P	HOH1731
P	HOH2853
P	HOH3292

site_id	CC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 R 301

Chain	Residue
R	ARG133
R	SER165
R	ARG167
R	GOL221

site_id	CC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL L 221

Chain	Residue
L	ASP6
L	ASN28
L	LYS84
L	PHE130
L	ALA164
L	SER165
L	SO4301

site_id	CC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 T 301

Chain	Residue
T	ARG133
T	SER165
T	ARG167
T	HOH2343
T	HOH3088

site_id	CC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 U 301

Chain	Residue
U	ARG133
U	SER165
U	ARG167
U	GOL221
U	HOH1629

site_id	DC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL W 221

Chain	Residue
W	ASP6
W	ASN28
W	LYS84
W	PHE130
W	ARG133
W	ALA164
W	SER165
W	SO4301

site_id	DC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL R 221

Chain	Residue
R	ASP6
R	ASN28
R	LYS84
R	PHE130
R	ALA164
R	SER165
R	SO4301

site_id	DC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL U 221

Chain	Residue
U	ASP6
U	ASN28
U	LYS84
U	PHE130
U	ALA164
U	SER165
U	SO4301

Functional Information from PROSITE/UniProt

site_id	PS00958
Number of Residues	18
Details	TRANSALDOLASE_2 Transaldolase active site. ItVKIPmTsDGLkAvRaL

Chain	Residue	Details
A	ILE81-LEU98

site_id	PS01054
Number of Residues	9
Details	TRANSALDOLASE_1 Transaldolase signature 1. GVTTNPSLV

Chain	Residue	Details
A	GLY24-VAL32

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	20
Details	Active site: {"description":"Schiff-base intermediate with substrate","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	17
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17218307","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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