1BK4

CRYSTAL STRUCTURE OF RABBIT LIVER FRUCTOSE-1,6-BISPHOSPHATASE AT 2.3 ANGSTROM RESOLUTION

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005975	biological_process	carbohydrate metabolic process
A	0005986	biological_process	sucrose biosynthetic process
A	0006000	biological_process	fructose metabolic process
A	0006002	biological_process	fructose 6-phosphate metabolic process
A	0006094	biological_process	gluconeogenesis
A	0006111	biological_process	regulation of gluconeogenesis
A	0016208	molecular_function	AMP binding
A	0016787	molecular_function	hydrolase activity
A	0016791	molecular_function	phosphatase activity
A	0030308	biological_process	negative regulation of cell growth
A	0030388	biological_process	fructose 1,6-bisphosphate metabolic process
A	0042132	molecular_function	fructose 1,6-bisphosphate 1-phosphatase activity
A	0042578	molecular_function	phosphoric ester hydrolase activity
A	0042802	molecular_function	identical protein binding
A	0045820	biological_process	negative regulation of glycolytic process
A	0046580	biological_process	negative regulation of Ras protein signal transduction
A	0046872	molecular_function	metal ion binding
A	0048029	molecular_function	monosaccharide binding
A	0071286	biological_process	cellular response to magnesium ion
A	0071466	biological_process	cellular response to xenobiotic stimulus

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 338

Chain	Residue
A	GLU97
A	ASP118
A	ASP121
A	GLU280

---

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 A 339

Chain	Residue
A	TYR215
A	ARG243
A	TYR244
A	TYR264
A	LYS274
A	HOH398
A	HOH414
A	ASN212

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A 340

Chain	Residue
A	GLY26
A	THR27
A	GLY28
A	GLU29
A	MET30
A	LYS112
A	TYR113

---

site_id	MG
Number of Residues	4
Details	THE MG2+ BINDING SITE IS NEAR THE CATALYTIC CLEFT OF THE EN A SULFATE (SO4 328) BINDS AT THE PHOSPHATE BINDING SITE OF

Chain	Residue
A	GLU97
A	ASP118
A	ASP121
A	GLU280

---

Functional Information from PROSITE/UniProt

site_id	PS00124
Number of Residues	13
Details	FBPASE Fructose-1-6-bisphosphatase active site. GKLrlLYEcnPMA

Chain	Residue	Details
A	GLY273-ALA285

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	25
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P00636","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10089399","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BK4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9QXD6","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q9QXD6","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P09467","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	GLU98
A	ASP74

---