Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4RZ4

Fructose-6-phosphate aldolase Q59E Y131F 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	5
Details	BINDING SITE FOR RESIDUE PGE A 301

Chain	Residue
A	ASP6
A	ASN28
A	LYS85
A	PHE131
A	PGE302

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PGE A 302

Chain	Residue
A	HOH439
A	ARG134
A	SER166
A	PGE301
A	HOH430

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 A 303

Chain	Residue
A	ARG134
A	LYS168
A	HOH495
B	LYS206

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 304

Chain	Residue
A	HIS150
A	VAL162
A	GLU182

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PGE B 301

Chain	Residue
B	ASP6
B	ASN28
B	LYS85
B	PHE131
B	PGE302

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PGE B 302

Chain	Residue
B	ASN28
B	ARG134
B	SER166
B	PGE301
B	HOH409
B	HOH417
B	HOH468

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 B 303

Chain	Residue
B	ARG134
B	LYS168
B	HOH468
B	HOH506
C	LYS206

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL B 304

Chain	Residue
B	HIS150
B	VAL162
B	GLU182

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PGE C 301

Chain	Residue
C	ASP6
C	ASN28
C	LYS85
C	PGE302

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PGE C 302

Chain	Residue
C	ASN28
C	ARG134
C	SER166
C	PGE301
C	HOH426
C	HOH430
C	HOH452

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 C 303

Chain	Residue
C	ARG134
C	LYS168
C	HOH452
C	HOH461
C	HOH506
D	LYS206

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL C 304

Chain	Residue
C	HIS150
C	VAL162
C	GLU182

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PGE D 301

Chain	Residue
D	ASP6
D	ASN28
D	LYS85
D	PHE131
D	PGE302

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PGE D 302

Chain	Residue
D	ASN28
D	ARG134
D	SER166
D	PGE301
D	HOH407
D	HOH431

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PO4 D 303

Chain	Residue
D	ARG134
D	LYS168
E	LYS206

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL D 304

Chain	Residue
D	HIS150
D	VAL162
D	GLU182

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PGE E 301

Chain	Residue
E	ASP6
E	ASN28
E	LYS85
E	PGE302

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PGE E 302

Chain	Residue
E	ARG134
E	SER166
E	PGE301
E	HOH423
E	HOH425
E	HOH444

site_id	CC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 E 303

Chain	Residue
A	LYS206
E	ARG134
E	LYS168
E	HOH444

site_id	CC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL E 304

Chain	Residue
E	HIS150
E	VAL162
E	GLU182

site_id	CC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PGE F 301

Chain	Residue
F	ASP6
F	ASN28
F	LYS85
F	PHE131
F	PGE302

site_id	CC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PGE F 302

Chain	Residue
F	HOH412
F	HOH426
F	HOH511
F	ARG134
F	SER166
F	PGE301

site_id	CC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 F 303

Chain	Residue
F	ARG134
F	LYS168
F	HOH484
F	HOH511
J	LYS206

site_id	CC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL F 304

Chain	Residue
F	HIS150
F	VAL162
F	GLU182

site_id	CC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PGE G 301

Chain	Residue
G	ASP6
G	ASN28
G	LYS85
G	PGE302

site_id	CC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PGE G 302

Chain	Residue
G	ARG134
G	SER166
G	PGE301
G	HOH426
G	HOH429
G	HOH468

site_id	CC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 G 303

Chain	Residue
F	LYS206
G	ARG134
G	LYS168
G	HOH468
G	HOH486
G	HOH547

site_id	DC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL G 304

Chain	Residue
G	HIS150
G	VAL162
G	GLU182

site_id	DC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PGE H 301

Chain	Residue
H	ASP6
H	ASN28
H	LYS85
H	PHE131
H	PGE302

site_id	DC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PGE H 302

Chain	Residue
H	ASN28
H	ARG134
H	SER166
H	PGE301
H	HOH453
H	HOH468
H	HOH516

site_id	DC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 H 303

Chain	Residue
G	LYS206
H	ARG134
H	LYS168
H	HOH516

site_id	DC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL H 304

Chain	Residue
H	HIS150
H	VAL162
H	GLU182

site_id	DC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PGE I 301

Chain	Residue
I	ASP6
I	ASN28
I	LYS85
I	PHE131
I	PGE302

site_id	DC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PGE I 302

Chain	Residue
I	ARG134
I	SER166
I	PGE301
I	HOH424
I	HOH463

site_id	DC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 I 303

Chain	Residue
H	LYS206
I	ARG134
I	LYS168
I	HOH490

site_id	DC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL I 304

Chain	Residue
I	HIS150
I	VAL162
I	GLU182

site_id	EC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PGE J 301

Chain	Residue
J	ASP6
J	ASN28
J	LYS85
J	PHE131
J	PGE302

site_id	EC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PGE J 302

Chain	Residue
J	ARG134
J	SER166
J	PGE301
J	HOH419
J	HOH449
J	HOH526

site_id	EC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 J 303

Chain	Residue
J	ARG134
J	LYS168
J	HOH502
J	HOH526
J	HOH548

site_id	EC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL J 304

Chain	Residue
J	HIS150
J	VAL162
J	GLU182

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)