5GK6

Structure of E.Coli fructose 1,6-bisphosphate aldolase, Citrate bound form

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue ZN A 401

Chain	Residue
A	HIS110
A	HIS264
A	CIT402
A	HOH533

---

site_id	AC2
Number of Residues	8
Details	binding site for residue CIT A 402

Chain	Residue
A	HOH521
A	HOH533
A	HOH588
A	HIS110
A	HIS264
A	GLY265
A	ZN401
A	HOH506

---

site_id	AC3
Number of Residues	7
Details	binding site for residue PEG A 403

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

---

site_id	AC4
Number of Residues	4
Details	binding site for residue ZN B 401

Chain	Residue
B	HIS110
B	HIS264
B	CIT402
B	HOH535

---

site_id	AC5
Number of Residues	8
Details	binding site for residue CIT B 402

Chain	Residue
B	HIS110
B	HIS264
B	GLY265
B	ZN401
B	HOH505
B	HOH521
B	HOH535
B	HOH537

---

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	2
Details	ACT_SITE: Proton donor => ECO:0000269|PubMed:10080900

Chain	Residue	Details
A	ASP109
B	ASP109

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305

Chain	Residue	Details
A	SER61
B	SER61

---

site_id	SWS_FT_FI3
Number of Residues	10
Details	BINDING: BINDING => ECO:0000269|PubMed:10080900, ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754

Chain	Residue	Details
A	HIS264
B	HIS110
B	ASP144
B	GLU174
B	HIS226
B	HIS264
A	HIS110
A	ASP144
A	GLU174
A	HIS226

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING:

Chain	Residue	Details
A	ASN286
B	GLY227
B	GLY265
B	ASN286
A	GLY227
A	GLY265

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122

Chain	Residue	Details
A	LYS8
B	LYS8

---

site_id	SWS_FT_FI6
Number of Residues	14
Details	MOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122

Chain	Residue	Details
A	LYS230
A	LYS250
A	LYS318
A	LYS325
A	LYS347
B	LYS71
B	LYS114
B	LYS230
B	LYS250
B	LYS318
B	LYS325
B	LYS347
A	LYS71
A	LYS114

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 52

Chain	Residue	Details
A	ASP109	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	HIS110	metal ligand
A	GLU182	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	HIS226	metal ligand
A	HIS264	metal ligand
A	ASN286	electrostatic stabiliser, hydrogen bond donor, steric role

---

site_id	MCSA2
Number of Residues	6
Details	M-CSA 52

Chain	Residue	Details
B	ASP109	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	HIS110	metal ligand
B	GLU182	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	HIS226	metal ligand
B	HIS264	metal ligand
B	ASN286	electrostatic stabiliser, hydrogen bond donor, steric role

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