5VJE

Class II fructose-1,6-bisphosphate aldolase of Escherichia coli with D-glucitol 1,6-bisphosphate

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	8
Details	binding site for residue NA A 401

Chain	Residue
A	GLN59
A	HIS107
A	ASP109
A	MET142
A	GLU172
A	HIS264
A	LYS284
A	ASN286

---

site_id	AC2
Number of Residues	6
Details	binding site for residue NA A 402

Chain	Residue
A	GLY227
A	GLY265
A	SER267
A	GOS403
A	HOH790
A	VAL225

---

site_id	AC3
Number of Residues	23
Details	binding site for residue GOS A 403

Chain	Residue
A	SER61
A	ASP109
A	HIS110
A	HIS226
A	GLY227
A	HIS264
A	GLY265
A	GLY266
A	SER267
A	ASN286
A	ILE287
A	ASP288
A	THR289
A	NA402
A	HOH501
A	HOH508
A	HOH532
A	HOH568
A	HOH632
A	HOH639
A	HOH734
A	HOH797
B	ARG331

---

site_id	AC4
Number of Residues	7
Details	binding site for residue NA B 401

Chain	Residue
B	HIS107
B	ASP109
B	MET142
B	GLU172
B	HIS264
B	LYS284
B	ASN286

---

site_id	AC5
Number of Residues	6
Details	binding site for residue NA B 402

Chain	Residue
B	VAL225
B	GLY227
B	GLY265
B	SER267
B	GOS403
B	HOH691

---

site_id	AC6
Number of Residues	23
Details	binding site for residue GOS B 403

Chain	Residue
A	ARG331
A	HOH630
B	SER61
B	ASP109
B	HIS110
B	HIS226
B	GLY227
B	HIS264
B	GLY265
B	SER267
B	ASN286
B	ILE287
B	ASP288
B	THR289
B	NA402
B	HOH504
B	HOH520
B	HOH530
B	HOH578
B	HOH595
B	HOH674
B	HOH704
B	HOH759

---

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	HIS110
B	HIS264
A	ASP144
A	GLU174
A	HIS226
A	HIS264
B	HIS110
B	ASP144
B	GLU174
B	HIS226

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING:

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

---

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	LYS71
B	LYS230
B	LYS250
B	LYS318
B	LYS325
B	LYS347
A	LYS114
A	LYS230
A	LYS250
A	LYS318
A	LYS325
A	LYS347
B	LYS71
B	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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