Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1OK4

Archaeal fructose 1,6-bisphosphate aldolase covalently bound to the substrate dihydroxyacetone phosphate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004332	molecular_function	fructose-bisphosphate aldolase activity
A	0005737	cellular_component	cytoplasm
A	0006096	biological_process	glycolytic process
A	0016829	molecular_function	lyase activity
B	0003824	molecular_function	catalytic activity
B	0004332	molecular_function	fructose-bisphosphate aldolase activity
B	0005737	cellular_component	cytoplasm
B	0006096	biological_process	glycolytic process
B	0016829	molecular_function	lyase activity
C	0003824	molecular_function	catalytic activity
C	0004332	molecular_function	fructose-bisphosphate aldolase activity
C	0005737	cellular_component	cytoplasm
C	0006096	biological_process	glycolytic process
C	0016829	molecular_function	lyase activity
D	0003824	molecular_function	catalytic activity
D	0004332	molecular_function	fructose-bisphosphate aldolase activity
D	0005737	cellular_component	cytoplasm
D	0006096	biological_process	glycolytic process
D	0016829	molecular_function	lyase activity
E	0003824	molecular_function	catalytic activity
E	0004332	molecular_function	fructose-bisphosphate aldolase activity
E	0005737	cellular_component	cytoplasm
E	0006096	biological_process	glycolytic process
E	0016829	molecular_function	lyase activity
F	0003824	molecular_function	catalytic activity
F	0004332	molecular_function	fructose-bisphosphate aldolase activity
F	0005737	cellular_component	cytoplasm
F	0006096	biological_process	glycolytic process
F	0016829	molecular_function	lyase activity
G	0003824	molecular_function	catalytic activity
G	0004332	molecular_function	fructose-bisphosphate aldolase activity
G	0005737	cellular_component	cytoplasm
G	0006096	biological_process	glycolytic process
G	0016829	molecular_function	lyase activity
H	0003824	molecular_function	catalytic activity
H	0004332	molecular_function	fructose-bisphosphate aldolase activity
H	0005737	cellular_component	cytoplasm
H	0006096	biological_process	glycolytic process
H	0016829	molecular_function	lyase activity
I	0003824	molecular_function	catalytic activity
I	0004332	molecular_function	fructose-bisphosphate aldolase activity
I	0005737	cellular_component	cytoplasm
I	0006096	biological_process	glycolytic process
I	0016829	molecular_function	lyase activity
J	0003824	molecular_function	catalytic activity
J	0004332	molecular_function	fructose-bisphosphate aldolase activity
J	0005737	cellular_component	cytoplasm
J	0006096	biological_process	glycolytic process
J	0016829	molecular_function	lyase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 13P A1254

Chain	Residue
A	ALA22
A	GLY231
A	ARG232
A	HOH2072
A	ASP24
A	HIS25
A	TRP144
A	LYS177
A	GLY203
A	GLY204
A	ALA229
A	VAL230

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 13P B1254

Chain	Residue
B	ALA22
B	ASP24
B	HIS25
B	TRP144
B	LYS177
B	GLY203
B	GLY204
B	ALA229
B	VAL230
B	GLY231
B	ARG232
B	HOH2066

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 13P C1254

Chain	Residue
C	ALA22
C	ASP24
C	HIS25
C	TRP144
C	LYS177
C	SER202
C	GLY203
C	GLY204
C	ALA229
C	VAL230
C	GLY231
C	ARG232
C	HOH2056

site_id	AC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 13P D1254

Chain	Residue
D	ASP24
D	HIS25
D	TRP144
D	LYS177
D	SER202
D	GLY203
D	GLY204
D	ALA229
D	VAL230
D	GLY231
D	ARG232
D	HOH2052
D	HOH2053

site_id	AC5
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 13P E1256

Chain	Residue
E	ALA22
E	ASP24
E	HIS25
E	TRP144
E	LYS177
E	SER202
E	GLY203
E	GLY204
E	ALA229
E	VAL230
E	GLY231
E	ARG232
E	HOH2061
E	HOH2062
E	HOH2063

site_id	AC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 13P F1254

Chain	Residue
F	ASP24
F	HIS25
F	TRP144
F	LYS177
F	SER202
F	GLY203
F	GLY204
F	ALA229
F	VAL230
F	GLY231
F	ARG232
F	HOH2050
F	HOH2051

site_id	AC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 13P G1254

Chain	Residue
G	ALA22
G	ASP24
G	HIS25
G	TRP144
G	LYS177
G	GLY203
G	GLY204
G	ALA229
G	VAL230
G	GLY231
G	ARG232
G	HOH2076

site_id	AC8
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 13P H1254

Chain	Residue
H	VAL230
H	GLY231
H	ARG232
H	HOH2067
H	HOH2068
H	ALA22
H	ASP24
H	HIS25
H	TRP144
H	TYR146
H	LYS177
H	GLY203
H	GLY204
H	ALA229

site_id	AC9
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 13P I1254

Chain	Residue
I	ALA22
I	ASP24
I	HIS25
I	TRP144
I	LYS177
I	SER202
I	GLY203
I	GLY204
I	ALA229
I	VAL230
I	GLY231
I	ARG232
I	HOH2070
I	HOH2071

site_id	BC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 13P J1254

Chain	Residue
J	ALA22
J	ASP24
J	HIS25
J	TRP144
J	LYS177
J	SER202
J	GLY203
J	GLY204
J	ALA229
J	VAL230
J	GLY231
J	ARG232
J	HOH2063
J	HOH2064
J	HOH2065

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	10
Details	ACT_SITE: Proton donor

Chain	Residue	Details
A	TYR146
J	TYR146
B	TYR146
C	TYR146
D	TYR146
E	TYR146
F	TYR146
G	TYR146
H	TYR146
I	TYR146

site_id	SWS_FT_FI2
Number of Residues	10
Details	ACT_SITE: Schiff-base intermediate with dihydroxyacetone-P

Chain	Residue	Details
A	LYS177
J	LYS177
B	LYS177
C	LYS177
D	LYS177
E	LYS177
F	LYS177
G	LYS177
H	LYS177
I	LYS177

site_id	SWS_FT_FI3
Number of Residues	80
Details	BINDING:

Chain	Residue	Details
A	ASP24
B	HIS29
B	ASP33
B	TRP144
B	ARG148
B	LYS177
B	SER202
B	GLY231
C	ASP24
C	HIS29
C	ASP33
A	HIS29
C	TRP144
C	ARG148
C	LYS177
C	SER202
C	GLY231
D	ASP24
D	HIS29
D	ASP33
D	TRP144
D	ARG148
A	ASP33
D	LYS177
D	SER202
D	GLY231
E	ASP24
E	HIS29
E	ASP33
E	TRP144
E	ARG148
E	LYS177
E	SER202
A	TRP144
E	GLY231
F	ASP24
F	HIS29
F	ASP33
F	TRP144
F	ARG148
F	LYS177
F	SER202
F	GLY231
G	ASP24
A	ARG148
G	HIS29
G	ASP33
G	TRP144
G	ARG148
G	LYS177
G	SER202
G	GLY231
H	ASP24
H	HIS29
H	ASP33
A	LYS177
H	TRP144
H	ARG148
H	LYS177
H	SER202
H	GLY231
I	ASP24
I	HIS29
I	ASP33
I	TRP144
I	ARG148
A	SER202
I	LYS177
I	SER202
I	GLY231
J	ASP24
J	HIS29
J	ASP33
J	TRP144
J	ARG148
J	LYS177
J	SER202
A	GLY231
J	GLY231
B	ASP24

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 12941964, 11705376

Chain	Residue	Details
A	ASP24
A	LYS177
A	TYR146

site_id	CSA10
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 12941964, 11705376

Chain	Residue	Details
J	ASP24
J	LYS177
J	TYR146

site_id	CSA2
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 12941964, 11705376

Chain	Residue	Details
B	ASP24
B	LYS177
B	TYR146

site_id	CSA3
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 12941964, 11705376

Chain	Residue	Details
C	ASP24
C	LYS177
C	TYR146

site_id	CSA4
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 12941964, 11705376

Chain	Residue	Details
D	ASP24
D	LYS177
D	TYR146

site_id	CSA5
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 12941964, 11705376

Chain	Residue	Details
E	ASP24
E	LYS177
E	TYR146

site_id	CSA6
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 12941964, 11705376

Chain	Residue	Details
F	ASP24
F	LYS177
F	TYR146

site_id	CSA7
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 12941964, 11705376

Chain	Residue	Details
G	ASP24
G	LYS177
G	TYR146

site_id	CSA8
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 12941964, 11705376

Chain	Residue	Details
H	ASP24
H	LYS177
H	TYR146

site_id	CSA9
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 12941964, 11705376

Chain	Residue	Details
I	ASP24
I	LYS177
I	TYR146

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