Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1L6W

Fructose-6-phosphate aldolase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0005975	biological_process	carbohydrate metabolic process
A	0006000	biological_process	fructose metabolic process
A	0016829	molecular_function	lyase activity
A	0016832	molecular_function	aldehyde-lyase activity
A	0042182	biological_process	ketone catabolic process
A	0042802	molecular_function	identical protein binding
A	0097023	molecular_function	fructose 6-phosphate aldolase activity
B	0005737	cellular_component	cytoplasm
B	0005975	biological_process	carbohydrate metabolic process
B	0006000	biological_process	fructose metabolic process
B	0016829	molecular_function	lyase activity
B	0016832	molecular_function	aldehyde-lyase activity
B	0042182	biological_process	ketone catabolic process
B	0042802	molecular_function	identical protein binding
B	0097023	molecular_function	fructose 6-phosphate aldolase activity
C	0005737	cellular_component	cytoplasm
C	0005975	biological_process	carbohydrate metabolic process
C	0006000	biological_process	fructose metabolic process
C	0016829	molecular_function	lyase activity
C	0016832	molecular_function	aldehyde-lyase activity
C	0042182	biological_process	ketone catabolic process
C	0042802	molecular_function	identical protein binding
C	0097023	molecular_function	fructose 6-phosphate aldolase activity
D	0005737	cellular_component	cytoplasm
D	0005975	biological_process	carbohydrate metabolic process
D	0006000	biological_process	fructose metabolic process
D	0016829	molecular_function	lyase activity
D	0016832	molecular_function	aldehyde-lyase activity
D	0042182	biological_process	ketone catabolic process
D	0042802	molecular_function	identical protein binding
D	0097023	molecular_function	fructose 6-phosphate aldolase activity
E	0005737	cellular_component	cytoplasm
E	0005975	biological_process	carbohydrate metabolic process
E	0006000	biological_process	fructose metabolic process
E	0016829	molecular_function	lyase activity
E	0016832	molecular_function	aldehyde-lyase activity
E	0042182	biological_process	ketone catabolic process
E	0042802	molecular_function	identical protein binding
E	0097023	molecular_function	fructose 6-phosphate aldolase activity
F	0005737	cellular_component	cytoplasm
F	0005975	biological_process	carbohydrate metabolic process
F	0006000	biological_process	fructose metabolic process
F	0016829	molecular_function	lyase activity
F	0016832	molecular_function	aldehyde-lyase activity
F	0042182	biological_process	ketone catabolic process
F	0042802	molecular_function	identical protein binding
F	0097023	molecular_function	fructose 6-phosphate aldolase activity
G	0005737	cellular_component	cytoplasm
G	0005975	biological_process	carbohydrate metabolic process
G	0006000	biological_process	fructose metabolic process
G	0016829	molecular_function	lyase activity
G	0016832	molecular_function	aldehyde-lyase activity
G	0042182	biological_process	ketone catabolic process
G	0042802	molecular_function	identical protein binding
G	0097023	molecular_function	fructose 6-phosphate aldolase activity
H	0005737	cellular_component	cytoplasm
H	0005975	biological_process	carbohydrate metabolic process
H	0006000	biological_process	fructose metabolic process
H	0016829	molecular_function	lyase activity
H	0016832	molecular_function	aldehyde-lyase activity
H	0042182	biological_process	ketone catabolic process
H	0042802	molecular_function	identical protein binding
H	0097023	molecular_function	fructose 6-phosphate aldolase activity
I	0005737	cellular_component	cytoplasm
I	0005975	biological_process	carbohydrate metabolic process
I	0006000	biological_process	fructose metabolic process
I	0016829	molecular_function	lyase activity
I	0016832	molecular_function	aldehyde-lyase activity
I	0042182	biological_process	ketone catabolic process
I	0042802	molecular_function	identical protein binding
I	0097023	molecular_function	fructose 6-phosphate aldolase activity
J	0005737	cellular_component	cytoplasm
J	0005975	biological_process	carbohydrate metabolic process
J	0006000	biological_process	fructose metabolic process
J	0016829	molecular_function	lyase activity
J	0016832	molecular_function	aldehyde-lyase activity
J	0042182	biological_process	ketone catabolic process
J	0042802	molecular_function	identical protein binding
J	0097023	molecular_function	fructose 6-phosphate aldolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 250

Chain	Residue
A	ASP6
A	THR27
A	ASN28
A	LYS85
A	TYR131
A	HOH894
A	HOH1760

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B 250

Chain	Residue
B	ASN28
B	LYS85
B	TYR131
B	HOH579
B	HOH1762
B	ASP6
B	THR27

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL C 250

Chain	Residue
C	ASP6
C	THR26
C	THR27
C	ASN28
C	LYS85
C	ALA129
C	TYR131
C	HOH636
C	HOH1764

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL D 250

Chain	Residue
D	ASP6
D	THR27
D	ASN28
D	LYS85
D	TYR131
D	LEU163
D	HOH513
D	HOH1767

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL E 250

Chain	Residue
E	ASP6
E	THR27
E	ASN28
E	LYS85
E	TYR131
E	HOH1768

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL F 250

Chain	Residue
F	ASP6
F	THR27
F	ASN28
F	LYS85
F	TYR131
F	HOH663
F	HOH1771

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL G 250

Chain	Residue
G	ASP6
G	THR27
G	ASN28
G	LYS85
G	TYR131
G	HOH614
G	HOH1772

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL H 250

Chain	Residue
H	ASP6
H	THR27
H	ASN28
H	LYS85
H	TYR131
H	HOH769
H	HOH1774

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL I 250

Chain	Residue
I	ASP6
I	THR27
I	ASN28
I	LYS85
I	TYR131
I	HOH615
I	HOH1776

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL J 250

Chain	Residue
J	ASP6
J	THR27
J	ASN28
J	LYS85
J	TYR131
J	HOH514
J	HOH1778

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE82-LEU99

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

Chain	Residue	Details
A	GLY24-ILE32

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	10
Details	Active site: {"description":"Schiff-base intermediate with substrate","evidences":[{"source":"PubMed","id":"11120740","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12051943","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1onr

Chain	Residue	Details
A	ASP6
A	LYS85
A	GLN59

site_id	CSA10
Number of Residues	3
Details	Annotated By Reference To The Literature 1onr

Chain	Residue	Details
J	ASP6
J	LYS85
J	GLN59

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1onr

Chain	Residue	Details
B	ASP6
B	LYS85
B	GLN59

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1onr

Chain	Residue	Details
C	ASP6
C	LYS85
C	GLN59

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1onr

Chain	Residue	Details
D	ASP6
D	LYS85
D	GLN59

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1onr

Chain	Residue	Details
E	ASP6
E	LYS85
E	GLN59

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1onr

Chain	Residue	Details
F	ASP6
F	LYS85
F	GLN59

site_id	CSA7
Number of Residues	3
Details	Annotated By Reference To The Literature 1onr

Chain	Residue	Details
G	ASP6
G	LYS85
G	GLN59

site_id	CSA8
Number of Residues	3
Details	Annotated By Reference To The Literature 1onr

Chain	Residue	Details
H	ASP6
H	LYS85
H	GLN59

site_id	CSA9
Number of Residues	3
Details	Annotated By Reference To The Literature 1onr

Chain	Residue	Details
I	ASP6
I	LYS85
I	GLN59

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