Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5GK5

Apo structure of fructose 1,6-bisphosphate aldolase from Escherichia coli at 1.9 angstrom resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004332	molecular_function	fructose-bisphosphate aldolase activity
A	0005515	molecular_function	protein binding
A	0005829	cellular_component	cytosol
A	0005975	biological_process	carbohydrate metabolic process
A	0006094	biological_process	gluconeogenesis
A	0006096	biological_process	glycolytic process
A	0008270	molecular_function	zinc ion binding
A	0016829	molecular_function	lyase activity
A	0016832	molecular_function	aldehyde-lyase activity
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0046872	molecular_function	metal ion binding
B	0004332	molecular_function	fructose-bisphosphate aldolase activity
B	0005515	molecular_function	protein binding
B	0005829	cellular_component	cytosol
B	0005975	biological_process	carbohydrate metabolic process
B	0006094	biological_process	gluconeogenesis
B	0006096	biological_process	glycolytic process
B	0008270	molecular_function	zinc ion binding
B	0016829	molecular_function	lyase activity
B	0016832	molecular_function	aldehyde-lyase activity
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0046872	molecular_function	metal ion binding
C	0004332	molecular_function	fructose-bisphosphate aldolase activity
C	0005515	molecular_function	protein binding
C	0005829	cellular_component	cytosol
C	0005975	biological_process	carbohydrate metabolic process
C	0006094	biological_process	gluconeogenesis
C	0006096	biological_process	glycolytic process
C	0008270	molecular_function	zinc ion binding
C	0016829	molecular_function	lyase activity
C	0016832	molecular_function	aldehyde-lyase activity
C	0042802	molecular_function	identical protein binding
C	0042803	molecular_function	protein homodimerization activity
C	0046872	molecular_function	metal ion binding
D	0004332	molecular_function	fructose-bisphosphate aldolase activity
D	0005515	molecular_function	protein binding
D	0005829	cellular_component	cytosol
D	0005975	biological_process	carbohydrate metabolic process
D	0006094	biological_process	gluconeogenesis
D	0006096	biological_process	glycolytic process
D	0008270	molecular_function	zinc ion binding
D	0016829	molecular_function	lyase activity
D	0016832	molecular_function	aldehyde-lyase activity
D	0042802	molecular_function	identical protein binding
D	0042803	molecular_function	protein homodimerization activity
D	0046872	molecular_function	metal ion binding
E	0004332	molecular_function	fructose-bisphosphate aldolase activity
E	0005515	molecular_function	protein binding
E	0005829	cellular_component	cytosol
E	0005975	biological_process	carbohydrate metabolic process
E	0006094	biological_process	gluconeogenesis
E	0006096	biological_process	glycolytic process
E	0008270	molecular_function	zinc ion binding
E	0016829	molecular_function	lyase activity
E	0016832	molecular_function	aldehyde-lyase activity
E	0042802	molecular_function	identical protein binding
E	0042803	molecular_function	protein homodimerization activity
E	0046872	molecular_function	metal ion binding
F	0004332	molecular_function	fructose-bisphosphate aldolase activity
F	0005515	molecular_function	protein binding
F	0005829	cellular_component	cytosol
F	0005975	biological_process	carbohydrate metabolic process
F	0006094	biological_process	gluconeogenesis
F	0006096	biological_process	glycolytic process
F	0008270	molecular_function	zinc ion binding
F	0016829	molecular_function	lyase activity
F	0016832	molecular_function	aldehyde-lyase activity
F	0042802	molecular_function	identical protein binding
F	0042803	molecular_function	protein homodimerization activity
F	0046872	molecular_function	metal ion binding
G	0004332	molecular_function	fructose-bisphosphate aldolase activity
G	0005515	molecular_function	protein binding
G	0005829	cellular_component	cytosol
G	0005975	biological_process	carbohydrate metabolic process
G	0006094	biological_process	gluconeogenesis
G	0006096	biological_process	glycolytic process
G	0008270	molecular_function	zinc ion binding
G	0016829	molecular_function	lyase activity
G	0016832	molecular_function	aldehyde-lyase activity
G	0042802	molecular_function	identical protein binding
G	0042803	molecular_function	protein homodimerization activity
G	0046872	molecular_function	metal ion binding
H	0004332	molecular_function	fructose-bisphosphate aldolase activity
H	0005515	molecular_function	protein binding
H	0005829	cellular_component	cytosol
H	0005975	biological_process	carbohydrate metabolic process
H	0006094	biological_process	gluconeogenesis
H	0006096	biological_process	glycolytic process
H	0008270	molecular_function	zinc ion binding
H	0016829	molecular_function	lyase activity
H	0016832	molecular_function	aldehyde-lyase activity
H	0042802	molecular_function	identical protein binding
H	0042803	molecular_function	protein homodimerization activity
H	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	binding site for residue GOL A 401

Chain	Residue
A	GLN18
A	TYR206
A	PRO214
A	SER258
A	ASN260
A	HOH510
A	HOH532
A	HOH560

site_id	AC2
Number of Residues	5
Details	binding site for residue ZN A 402

Chain	Residue
A	GLU174
A	HIS226
A	HIS264
A	HOH573
A	HIS110

site_id	AC3
Number of Residues	6
Details	binding site for residue ZN A 403

Chain	Residue
A	HIS110
A	HIS226
A	HIS264
A	HOH576
A	HOH617
A	HOH631

site_id	AC4
Number of Residues	8
Details	binding site for residue GOL B 401

Chain	Residue
B	PRO214
B	SER258
B	LEU259
B	ASN260
B	HOH528
B	HOH550
B	HOH593
G	HOH564

site_id	AC5
Number of Residues	9
Details	binding site for residue PEG B 402

Chain	Residue
A	SER88
A	HIS91
A	HIS92
A	GLN95
B	SER88
B	HIS91
B	HIS92
B	GLN95
B	HOH553

site_id	AC6
Number of Residues	5
Details	binding site for residue ZN B 403

Chain	Residue
B	HIS110
B	GLU174
B	HIS226
B	HIS264
B	HOH578

site_id	AC7
Number of Residues	9
Details	binding site for residue GOL C 401

Chain	Residue
C	GLN18
C	TYR206
C	PRO214
C	SER258
C	LEU259
C	ASN260
C	HOH1204
C	HOH1225
C	HOH1262

site_id	AC8
Number of Residues	13
Details	binding site for residue PEG C 402

Chain	Residue
C	VAL37
C	GLY38
C	THR39
C	ASP40
C	HOH1201
C	HOH1207
C	HOH1209
D	VAL37
D	GLY38
D	THR39
D	ASP40
D	HOH524
D	HOH541

site_id	AC9
Number of Residues	5
Details	binding site for residue ZN C 403

Chain	Residue
C	HIS110
C	GLU174
C	HIS226
C	HIS264
C	HOH1223

site_id	AD1
Number of Residues	6
Details	binding site for residue ZN C 404

Chain	Residue
C	HIS110
C	HIS226
C	HIS264
C	HOH1227
C	HOH1308
C	HOH1322

site_id	AD2
Number of Residues	8
Details	binding site for residue GOL D 401

Chain	Residue
D	GLN18
D	PRO214
D	SER258
D	LEU259
D	HOH508
D	HOH516
D	HOH585
D	HOH606

site_id	AD3
Number of Residues	7
Details	binding site for residue PEG D 402

Chain	Residue
C	SER88
C	HIS91
C	HIS92
C	GLN95
D	SER88
D	HIS91
D	HIS92

site_id	AD4
Number of Residues	5
Details	binding site for residue ZN D 403

Chain	Residue
D	HIS110
D	GLU174
D	HIS226
D	HIS264
D	HOH572

site_id	AD5
Number of Residues	6
Details	binding site for residue ZN D 404

Chain	Residue
D	HOH644
D	HIS110
D	HIS226
D	HIS264
D	HOH556
D	HOH636

site_id	AD6
Number of Residues	9
Details	binding site for residue GOL E 401

Chain	Residue
E	GLN18
E	PRO214
E	PHE216
E	SER258
E	LEU259
E	ASN260
E	HOH531
E	HOH548
E	HOH575

site_id	AD7
Number of Residues	8
Details	binding site for residue PEG E 402

Chain	Residue
E	SER88
E	HIS91
E	HIS92
E	GLN95
E	HOH585
F	SER88
F	HIS91
F	HIS92

site_id	AD8
Number of Residues	5
Details	binding site for residue ZN E 403

Chain	Residue
E	HIS110
E	GLU174
E	HIS226
E	HIS264
E	HOH559

site_id	AD9
Number of Residues	6
Details	binding site for residue ZN E 404

Chain	Residue
E	HIS110
E	HIS226
E	HIS264
E	HOH535
E	HOH619
E	HOH626

site_id	AE1
Number of Residues	5
Details	binding site for residue ZN F 401

Chain	Residue
F	HIS110
F	GLU174
F	HIS226
F	HIS264
F	HOH573

site_id	AE2
Number of Residues	7
Details	binding site for residue GOL G 401

Chain	Residue
G	GLN18
G	PRO214
G	SER258
G	LEU259
G	ASN260
G	HOH509
G	HOH557

site_id	AE3
Number of Residues	15
Details	binding site for residue PEG G 402

Chain	Residue
G	VAL37
G	GLY38
G	THR39
G	ASP40
G	LEU334
G	HOH511
G	HOH515
H	VAL37
H	GLY38
H	THR39
H	ASP40
H	LEU334
H	HOH510
H	HOH518
H	HOH525

site_id	AE4
Number of Residues	8
Details	binding site for residue PEG G 403

Chain	Residue
G	SER88
G	HIS91
G	HIS92
G	GLN95
G	HOH596
H	SER88
H	HIS91
H	HIS92

site_id	AE5
Number of Residues	5
Details	binding site for residue ZN G 404

Chain	Residue
G	HIS110
G	GLU174
G	HIS226
G	HIS264
G	HOH573

site_id	AE6
Number of Residues	6
Details	binding site for residue ZN G 405

Chain	Residue
G	HIS110
G	HIS226
G	HIS264
G	HOH538
G	HOH606
G	HOH624

site_id	AE7
Number of Residues	7
Details	binding site for residue GOL H 401

Chain	Residue
H	PRO214
H	SER258
H	ASN260
H	HOH537
H	HOH548
H	HOH583
H	HOH597

site_id	AE8
Number of Residues	5
Details	binding site for residue ZN H 402

Chain	Residue
H	HIS110
H	GLU174
H	HIS226
H	HIS264
H	HOH516

site_id	AE9
Number of Residues	6
Details	binding site for residue ZN H 403

Chain	Residue
H	HIS110
H	HIS226
H	HIS264
H	HOH531
H	HOH627
H	HOH631

Functional Information from PROSITE/UniProt

site_id	PS00602
Number of Residues	12
Details	ALDOLASE_CLASS_II_1 Fructose-bisphosphate aldolase class-II signature 1. Yg..VPVi.LHtDHC

Chain	Residue	Details
A	TYR100-CYS111

site_id	PS00806
Number of Residues	12
Details	ALDOLASE_CLASS_II_2 Fructose-bisphosphate aldolase class-II signature 2. LEiELGctGGeE

Chain	Residue	Details
A	LEU171-GLU182

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: Proton donor => ECO:0000269\|PubMed:10080900

Chain	Residue	Details
A	ASP109
B	ASP109
C	ASP109
D	ASP109
E	ASP109
F	ASP109
G	ASP109
H	ASP109

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000305

Chain	Residue	Details
A	SER61
B	SER61
C	SER61
D	SER61
E	SER61
F	SER61
G	SER61
H	SER61

site_id	SWS_FT_FI3
Number of Residues	40
Details	BINDING: BINDING => ECO:0000269\|PubMed:10080900, ECO:0000269\|PubMed:8836102, ECO:0000269\|PubMed:8939754

Chain	Residue	Details
A	HIS110
B	HIS264
C	HIS110
C	ASP144
C	GLU174
C	HIS226
C	HIS264
D	HIS110
D	ASP144
D	GLU174
D	HIS226
A	ASP144
D	HIS264
E	HIS110
E	ASP144
E	GLU174
E	HIS226
E	HIS264
F	HIS110
F	ASP144
F	GLU174
F	HIS226
A	GLU174
F	HIS264
G	HIS110
G	ASP144
G	GLU174
G	HIS226
G	HIS264
H	HIS110
H	ASP144
H	GLU174
H	HIS226
A	HIS226
H	HIS264
A	HIS264
B	HIS110
B	ASP144
B	GLU174
B	HIS226

site_id	SWS_FT_FI4
Number of Residues	24
Details	BINDING:

Chain	Residue	Details
A	GLY227
D	GLY227
D	GLY265
D	ASN286
E	GLY227
E	GLY265
E	ASN286
F	GLY227
F	GLY265
F	ASN286
G	GLY227
A	GLY265
G	GLY265
G	ASN286
H	GLY227
H	GLY265
H	ASN286
A	ASN286
B	GLY227
B	GLY265
B	ASN286
C	GLY227
C	GLY265
C	ASN286

site_id	SWS_FT_FI5
Number of Residues	8
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000269\|PubMed:21151122

Chain	Residue	Details
A	LYS8
B	LYS8
C	LYS8
D	LYS8
E	LYS8
F	LYS8
G	LYS8
H	LYS8

site_id	SWS_FT_FI6
Number of Residues	56
Details	MOD_RES: N6-succinyllysine => ECO:0000269\|PubMed:21151122

Chain	Residue	Details
A	LYS71
B	LYS230
B	LYS250
B	LYS318
B	LYS325
B	LYS347
C	LYS71
C	LYS114
C	LYS230
C	LYS250
C	LYS318
A	LYS114
C	LYS325
C	LYS347
D	LYS71
D	LYS114
D	LYS230
D	LYS250
D	LYS318
D	LYS325
D	LYS347
E	LYS71
A	LYS230
E	LYS114
E	LYS230
E	LYS250
E	LYS318
E	LYS325
E	LYS347
F	LYS71
F	LYS114
F	LYS230
F	LYS250
A	LYS250
F	LYS318
F	LYS325
F	LYS347
G	LYS71
G	LYS114
G	LYS230
G	LYS250
G	LYS318
G	LYS325
G	LYS347
A	LYS318
H	LYS71
H	LYS114
H	LYS230
H	LYS250
H	LYS318
H	LYS325
H	LYS347
A	LYS325
A	LYS347
B	LYS71
B	LYS114

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	5
Details	M-CSA 52

Chain	Residue	Details
A	ASP109	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	HIS110	metal ligand
A	HIS226	metal ligand
A	HIS264	metal ligand
A	ASN286	electrostatic stabiliser, hydrogen bond donor, steric role

site_id	MCSA2
Number of Residues	5
Details	M-CSA 52

Chain	Residue	Details
B	ASP109	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	HIS110	metal ligand
B	HIS226	metal ligand
B	HIS264	metal ligand
B	ASN286	electrostatic stabiliser, hydrogen bond donor, steric role

site_id	MCSA3
Number of Residues	5
Details	M-CSA 52

Chain	Residue	Details
C	ASP109	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
C	HIS110	metal ligand
C	HIS226	metal ligand
C	HIS264	metal ligand
C	ASN286	electrostatic stabiliser, hydrogen bond donor, steric role

site_id	MCSA4
Number of Residues	5
Details	M-CSA 52

Chain	Residue	Details
D	ASP109	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
D	HIS110	metal ligand
D	HIS226	metal ligand
D	HIS264	metal ligand
D	ASN286	electrostatic stabiliser, hydrogen bond donor, steric role

site_id	MCSA5
Number of Residues	5
Details	M-CSA 52

Chain	Residue	Details
E	ASP109	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
E	HIS110	metal ligand
E	HIS226	metal ligand
E	HIS264	metal ligand
E	ASN286	electrostatic stabiliser, hydrogen bond donor, steric role

site_id	MCSA6
Number of Residues	5
Details	M-CSA 52

Chain	Residue	Details
F	ASP109	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
F	HIS110	metal ligand
F	HIS226	metal ligand
F	HIS264	metal ligand
F	ASN286	electrostatic stabiliser, hydrogen bond donor, steric role

site_id	MCSA7
Number of Residues	5
Details	M-CSA 52

Chain	Residue	Details
G	ASP109	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
G	HIS110	metal ligand
G	HIS226	metal ligand
G	HIS264	metal ligand
G	ASN286	electrostatic stabiliser, hydrogen bond donor, steric role

site_id	MCSA8
Number of Residues	5
Details	M-CSA 52

Chain	Residue	Details
H	ASP109	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
H	HIS110	metal ligand
H	HIS226	metal ligand
H	HIS264	metal ligand
H	ASN286	electrostatic stabiliser, hydrogen bond donor, steric role

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