1GYN

Class II fructose 1,6-bisphosphate aldolase with Cadmium (not Zinc) in the active site

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CD A 401

Chain	Residue
A	HIS110
A	HIS264
A	HOH2055
A	HOH2059
A	HOH2060
A	HOH2120

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CD A 402

Chain	Residue
A	HOH2079
A	HOH2080
A	ASP144
A	SER146
A	GLU174

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CD A 403

Chain	Residue
A	HIS91
A	HIS129
A	HOH2043
A	HOH2045
A	HOH2046

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site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD A 404

Chain	Residue
A	SER1
A	ASN27
A	GLU246
A	HIS256

---

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CD A 405

Chain	Residue
A	HIS252
A	HOH2039
A	HOH2098

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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

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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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000269|PubMed:10080900

Chain	Residue	Details
A	HIS110

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000305

Chain	Residue	Details
A	ASN62

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site_id	SWS_FT_FI3
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269|PubMed:10080900, ECO:0000269|PubMed:8836102, ECO:0000269|PubMed:8939754

Chain	Residue	Details
A	CYS111
A	LEU145
A	LEU175
A	GLY227
A	GLY265

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING:

Chain	Residue	Details
A	VAL228
A	GLY266
A	ILE287

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122

Chain	Residue	Details
A	PRO9

---

site_id	SWS_FT_FI6
Number of Residues	7
Details	MOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122

Chain	Residue	Details
A	GLY72
A	LEU115
A	PRO231
A	LYS251
A	GLY319
A	LYS326
A	ALA348

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1b57

Chain	Residue	Details
A	ASP109
A	ASN286

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site_id	MCSA1
Number of Residues	6
Details	M-CSA 52

Chain	Residue	Details
A	HIS110	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	CYS111	metal ligand
A	ASP183	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	GLY227	metal ligand
A	GLY265	metal ligand
A	ILE287	electrostatic stabiliser, hydrogen bond donor, steric role

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