Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4RXG

Fructose-6-phosphate aldolase Q59E from E.coli

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	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	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	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	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	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	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	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	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	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	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	8
Details	BINDING SITE FOR RESIDUE GOL A 301

Chain	Residue
A	ASP6
A	THR26
A	THR27
A	ASN28
A	LYS85
A	TYR131
A	ALA165
A	GOL302

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 302

Chain	Residue
A	ASN28
A	SER166
A	GOL301
A	ASP6

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B 301

Chain	Residue
B	ASP6
B	THR27
B	ASN28
B	LYS85
B	TYR131
B	ALA165
B	GOL302

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL B 302

Chain	Residue
B	ASP6
B	ASN28
B	ARG134
B	SER166
B	GOL301

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL C 301

Chain	Residue
C	ASP6
C	THR26
C	THR27
C	ASN28
C	LYS85
C	TYR131
C	ALA165
C	GOL302

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 302

Chain	Residue
C	ASP6
C	ASN28
C	ARG134
C	SER166
C	GOL301
C	HOH408

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL D 301

Chain	Residue
D	ASP6
D	THR26
D	THR27
D	ASN28
D	LYS85
D	TYR131
D	ALA165
D	GOL302

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL D 302

Chain	Residue
D	ASP6
D	ASN28
D	ARG134
D	SER166
D	GOL301
D	HOH446
D	HOH494

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL E 301

Chain	Residue
E	ASP6
E	THR27
E	ASN28
E	LYS85
E	TYR131
E	ALA165
E	GOL302

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL E 302

Chain	Residue
E	ASP6
E	ASN28
E	TYR131
E	ARG134
E	SER166
E	GOL301
E	HOH476

site_id	BC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL F 301

Chain	Residue
F	ASP6
F	THR26
F	THR27
F	ASN28
F	LYS85
F	TYR131
F	ALA165
F	GOL302

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL F 302

Chain	Residue
F	ASP6
F	ASN28
F	TYR131
F	ARG134
F	SER166
F	GOL301
F	HOH509

site_id	BC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL G 301

Chain	Residue
G	ASP6
G	THR27
G	ASN28
G	LYS85
G	TYR131
G	ALA165
G	HOH469

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL H 301

Chain	Residue
H	ASP6
H	THR27
H	ASN28
H	LYS85
H	TYR131
H	ALA165
H	GOL302

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL H 302

Chain	Residue
H	ARG134
H	SER166
H	GOL301
H	ASP6
H	ASN28
H	TYR131

site_id	BC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL I 301

Chain	Residue
I	ASP6
I	THR27
I	ASN28
I	LYS85
I	TYR131
I	ALA165
I	GOL302

site_id	BC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL I 302

Chain	Residue
I	ASP6
I	ASN28
I	ARG134
I	SER166
I	GOL301
I	HOH464
I	HOH475

site_id	BC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 1PE I 303

Chain	Residue
C	GLY139
H	ARG171
H	LEU174
H	TYR197
I	GLY113
I	ALA114
I	ALA115
I	GLN116
I	THR145
I	ASP148
I	HOH421

site_id	CC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL J 301

Chain	Residue
J	ASP6
J	THR26
J	THR27
J	ASN28
J	LYS85
J	TYR131
J	ALA165
J	GOL302

site_id	CC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL J 302

Chain	Residue
J	ASP6
J	ASN28
J	ARG134
J	SER166
J	GOL301
J	HOH426

site_id	CC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL J 303

Chain	Residue
J	THR7
J	SER8
J	ASP9
J	ILE31
J	ALA34
J	HOH430

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

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