4FBP

CONFORMATIONAL TRANSITION OF FRUCTOSE-1,6-BISPHOSPHATASE: STRUCTURE COMPARISON BETWEEN THE AMP COMPLEX (T FORM) AND THE FRUCTOSE 6-PHOSPHATE COMPLEX (R FORM)

Functional Information from GO Data

Chain	GOid	namespace	contents
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	0016311	biological_process	dephosphorylation
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
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005975	biological_process	carbohydrate metabolic process
B	0005986	biological_process	sucrose biosynthetic process
B	0006000	biological_process	fructose metabolic process
B	0006002	biological_process	fructose 6-phosphate metabolic process
B	0006094	biological_process	gluconeogenesis
B	0006111	biological_process	regulation of gluconeogenesis
B	0016208	molecular_function	AMP binding
B	0016311	biological_process	dephosphorylation
B	0016787	molecular_function	hydrolase activity
B	0016791	molecular_function	phosphatase activity
B	0030308	biological_process	negative regulation of cell growth
B	0030388	biological_process	fructose 1,6-bisphosphate metabolic process
B	0042132	molecular_function	fructose 1,6-bisphosphate 1-phosphatase activity
B	0042578	molecular_function	phosphoric ester hydrolase activity
B	0042802	molecular_function	identical protein binding
B	0045820	biological_process	negative regulation of glycolytic process
B	0046580	biological_process	negative regulation of Ras protein signal transduction
B	0046872	molecular_function	metal ion binding
B	0048029	molecular_function	monosaccharide binding
B	0071286	biological_process	cellular response to magnesium ion
B	0071466	biological_process	cellular response to xenobiotic stimulus
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0005975	biological_process	carbohydrate metabolic process
C	0005986	biological_process	sucrose biosynthetic process
C	0006000	biological_process	fructose metabolic process
C	0006002	biological_process	fructose 6-phosphate metabolic process
C	0006094	biological_process	gluconeogenesis
C	0006111	biological_process	regulation of gluconeogenesis
C	0016208	molecular_function	AMP binding
C	0016311	biological_process	dephosphorylation
C	0016787	molecular_function	hydrolase activity
C	0016791	molecular_function	phosphatase activity
C	0030308	biological_process	negative regulation of cell growth
C	0030388	biological_process	fructose 1,6-bisphosphate metabolic process
C	0042132	molecular_function	fructose 1,6-bisphosphate 1-phosphatase activity
C	0042578	molecular_function	phosphoric ester hydrolase activity
C	0042802	molecular_function	identical protein binding
C	0045820	biological_process	negative regulation of glycolytic process
C	0046580	biological_process	negative regulation of Ras protein signal transduction
C	0046872	molecular_function	metal ion binding
C	0048029	molecular_function	monosaccharide binding
C	0071286	biological_process	cellular response to magnesium ion
C	0071466	biological_process	cellular response to xenobiotic stimulus
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0005975	biological_process	carbohydrate metabolic process
D	0005986	biological_process	sucrose biosynthetic process
D	0006000	biological_process	fructose metabolic process
D	0006002	biological_process	fructose 6-phosphate metabolic process
D	0006094	biological_process	gluconeogenesis
D	0006111	biological_process	regulation of gluconeogenesis
D	0016208	molecular_function	AMP binding
D	0016311	biological_process	dephosphorylation
D	0016787	molecular_function	hydrolase activity
D	0016791	molecular_function	phosphatase activity
D	0030308	biological_process	negative regulation of cell growth
D	0030388	biological_process	fructose 1,6-bisphosphate metabolic process
D	0042132	molecular_function	fructose 1,6-bisphosphate 1-phosphatase activity
D	0042578	molecular_function	phosphoric ester hydrolase activity
D	0042802	molecular_function	identical protein binding
D	0045820	biological_process	negative regulation of glycolytic process
D	0046580	biological_process	negative regulation of Ras protein signal transduction
D	0046872	molecular_function	metal ion binding
D	0048029	molecular_function	monosaccharide binding
D	0071286	biological_process	cellular response to magnesium ion
D	0071466	biological_process	cellular response to xenobiotic stimulus

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE AMP A 338

Chain	Residue
A	VAL17
A	LYS112
A	TYR113
A	ARG140
A	VAL160
A	MET177
A	HOH628
A	GLN20
A	GLY21
A	ALA24
A	GLY26
A	THR27
A	GLU29
A	MET30
A	THR31

---

site_id	AC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE AMP B 338

Chain	Residue
B	VAL17
B	GLN20
B	GLY21
B	ALA24
B	GLY26
B	THR27
B	GLY28
B	GLU29
B	MET30
B	THR31
B	LYS112
B	TYR113
B	ARG140
B	MET177
B	HOH465
C	HOH409

---

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE AMP C 338

Chain	Residue
D	VAL17
D	GLN20
D	GLY21
D	THR27
D	GLY28
D	GLU29
D	MET30
D	THR31
D	LYS112
D	TYR113

---

site_id	AC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE AMP D 338

Chain	Residue
C	VAL17
C	GLN20
C	GLY21
C	GLY26
C	THR27
C	GLY28
C	GLU29
C	MET30
C	THR31
C	LYS112
C	TYR113
C	ARG140
C	VAL160
C	MET177
D	HOH543

---

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	12
Details	BINDING: BINDING => ECO:0000269|PubMed:10913263, ECO:0000269|PubMed:15767255, ECO:0000269|PubMed:2164670, ECO:0007744|PDB:1EYJ, ECO:0007744|PDB:1EYK, ECO:0007744|PDB:1FBP, ECO:0007744|PDB:1FJ9, ECO:0007744|PDB:1FPD, ECO:0007744|PDB:1FPE, ECO:0007744|PDB:1FPF, ECO:0007744|PDB:1FPG, ECO:0007744|PDB:1FPI, ECO:0007744|PDB:1FPJ, ECO:0007744|PDB:1FPL, ECO:0007744|PDB:1FRP, ECO:0007744|PDB:1FSA, ECO:0007744|PDB:1KZ8, ECO:0007744|PDB:1NV7, ECO:0007744|PDB:1RDY, ECO:0007744|PDB:1RDZ, ECO:0007744|PDB:1YYZ, ECO:0007744|PDB:1YZ0, ECO:0007744|PDB:2F3D, ECO:0007744|PDB:4FBP, ECO:0007744|PDB:4GBV, ECO:0007744|PDB:4GBW, ECO:0007744|PDB:4GWS, ECO:0007744|PDB:4GWY, ECO:0007744|PDB:4GWZ, ECO:0007744|PDB:4GX4, ECO:0007744|PDB:4GX6, ECO:0007744|PDB:4H46, ECO:0007744|PDB:4KXP

Chain	Residue	Details
A	MET18
D	MET18
D	GLY28
D	TYR113
A	GLY28
A	TYR113
B	MET18
B	GLY28
B	TYR113
C	MET18
C	GLY28
C	TYR113

---

site_id	SWS_FT_FI2
Number of Residues	28
Details	BINDING: BINDING => ECO:0000269|PubMed:2164670

Chain	Residue	Details
A	GLN69
B	PRO119
B	ASP121
B	GLY122
B	LYS141
B	CYS281
C	GLN69
C	GLU98
C	PRO119
C	ASP121
C	GLY122
A	GLU98
C	LYS141
C	CYS281
D	GLN69
D	GLU98
D	PRO119
D	ASP121
D	GLY122
D	LYS141
D	CYS281
A	PRO119
A	ASP121
A	GLY122
A	LYS141
A	CYS281
B	GLN69
B	GLU98

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:10913263, ECO:0000269|PubMed:12595528, ECO:0000269|PubMed:1312721, ECO:0000269|PubMed:14530289, ECO:0000269|PubMed:15767255, ECO:0000269|PubMed:17933867, ECO:0000269|PubMed:1849642, ECO:0000269|PubMed:2157849, ECO:0000269|PubMed:2164670, ECO:0007744|PDB:1CNQ, ECO:0007744|PDB:1EYI, ECO:0007744|PDB:1EYJ, ECO:0007744|PDB:1EYK, ECO:0007744|PDB:1FBP, ECO:0007744|PDB:1FJ6, ECO:0007744|PDB:1FJ9, ECO:0007744|PDB:1FRP, ECO:0007744|PDB:1FSA, ECO:0007744|PDB:1KZ8, ECO:0007744|PDB:1LEV, ECO:0007744|PDB:1NUW, ECO:0007744|PDB:1NUX, ECO:0007744|PDB:1NUY, ECO:0007744|PDB:1NUZ, ECO:0007744|PDB:1NV0, ECO:0007744|PDB:1NV1, ECO:0007744|PDB:1NV2, ECO:0007744|PDB:1NV3, ECO:0007744|PDB:1NV4, ECO:0007744|PDB:1NV5, ECO:0007744|PDB:1NV6, ECO:0007744|PDB:1NV7, ECO:0007744|PDB:1Q9D, ECO:0007744|PDB:1RDY, ECO:0007744|PDB:1RDZ, ECO:0007744|PDB:1YXI, ECO:0007744|PDB:1YYZ, ECO:0007744|PDB:1YZ0, ECO:0007744|PDB:2F3B, ECO:0007744|PDB:2F3D, ECO:0007744|PDB:2QVU, ECO:0007744|PDB:2QVV, ECO:0007744|PDB:3FBP, ECO:0007744|PDB:4GBV, ECO:0007744|PDB:4GBW, ECO:0007744|PDB:4GWS, ECO:0007744|PDB:4GWU, ECO:0007744|PDB:4GWW, ECO:0007744|PDB:4GWX, ECO:0007744|PDB:4GWY, ECO:0007744|PDB:4GWZ, ECO:0007744|PDB:4GX3, ECO:0007744|PDB:4GX4, ECO:0007744|PDB:4GX6, ECO:0007744|PDB:4H45, ECO:0007744|PDB:4H46, ECO:0007744|PDB:4KXP, ECO:0007744|PDB:5FBP

Chain	Residue	Details
A	GLU213
B	GLU213
C	GLU213
D	GLU213

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:10913263, ECO:0000269|PubMed:12595528, ECO:0000269|PubMed:1312721, ECO:0000269|PubMed:14530289, ECO:0000269|PubMed:15767255, ECO:0000269|PubMed:17933867, ECO:0000269|PubMed:1849642, ECO:0000269|PubMed:2157849, ECO:0000269|PubMed:2164670, ECO:0007744|PDB:1CNQ, ECO:0007744|PDB:1EYI, ECO:0007744|PDB:1EYJ, ECO:0007744|PDB:1EYK, ECO:0007744|PDB:1FBP, ECO:0007744|PDB:1FJ6, ECO:0007744|PDB:1FJ9, ECO:0007744|PDB:1FSA, ECO:0007744|PDB:1KZ8, ECO:0007744|PDB:1LEV, ECO:0007744|PDB:1NUW, ECO:0007744|PDB:1NUX, ECO:0007744|PDB:1NUY, ECO:0007744|PDB:1NUZ, ECO:0007744|PDB:1NV0, ECO:0007744|PDB:1NV1, ECO:0007744|PDB:1NV2, ECO:0007744|PDB:1NV3, ECO:0007744|PDB:1NV4, ECO:0007744|PDB:1NV5, ECO:0007744|PDB:1NV6, ECO:0007744|PDB:1NV7, ECO:0007744|PDB:1Q9D, ECO:0007744|PDB:1RDY, ECO:0007744|PDB:1RDZ, ECO:0007744|PDB:1YXI, ECO:0007744|PDB:1YYZ, ECO:0007744|PDB:1YZ0, ECO:0007744|PDB:2F3B, ECO:0007744|PDB:2F3D, ECO:0007744|PDB:4GBV, ECO:0007744|PDB:4GBW, ECO:0007744|PDB:4GWS, ECO:0007744|PDB:4GWW, ECO:0007744|PDB:4GWX, ECO:0007744|PDB:4GWY, ECO:0007744|PDB:4GWZ, ECO:0007744|PDB:4GX3, ECO:0007744|PDB:4GX4, ECO:0007744|PDB:4GX6, ECO:0007744|PDB:4H45, ECO:0007744|PDB:4H46, ECO:0007744|PDB:4KXP, ECO:0007744|PDB:5FBP

Chain	Residue	Details
A	TYR244
B	TYR244
C	TYR244
D	TYR244

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:10913263, ECO:0000269|PubMed:12595528, ECO:0000269|PubMed:1312721, ECO:0000269|PubMed:14530289, ECO:0000269|PubMed:15767255, ECO:0000269|PubMed:17933867, ECO:0000269|PubMed:1849642, ECO:0000269|PubMed:2157849, ECO:0000269|PubMed:2164670, ECO:0007744|PDB:1CNQ, ECO:0007744|PDB:1EYI, ECO:0007744|PDB:1EYJ, ECO:0007744|PDB:1EYK, ECO:0007744|PDB:1FJ6, ECO:0007744|PDB:1FJ9, ECO:0007744|PDB:1FPB, ECO:0007744|PDB:1FRP, ECO:0007744|PDB:1FSA, ECO:0007744|PDB:1KZ8, ECO:0007744|PDB:1LEV, ECO:0007744|PDB:1NUW, ECO:0007744|PDB:1NUX, ECO:0007744|PDB:1NUY, ECO:0007744|PDB:1NUZ, ECO:0007744|PDB:1NV0, ECO:0007744|PDB:1NV1, ECO:0007744|PDB:1NV2, ECO:0007744|PDB:1NV3, ECO:0007744|PDB:1NV4, ECO:0007744|PDB:1NV5, ECO:0007744|PDB:1NV6, ECO:0007744|PDB:1NV7, ECO:0007744|PDB:1Q9D, ECO:0007744|PDB:1RDY, ECO:0007744|PDB:1RDZ, ECO:0007744|PDB:1YXI, ECO:0007744|PDB:1YYZ, ECO:0007744|PDB:1YZ0, ECO:0007744|PDB:2F3B, ECO:0007744|PDB:2F3D, ECO:0007744|PDB:2QVU, ECO:0007744|PDB:2QVV, ECO:0007744|PDB:4GBV, ECO:0007744|PDB:4GBW, ECO:0007744|PDB:4GWS, ECO:0007744|PDB:4GWU, ECO:0007744|PDB:4GWW, ECO:0007744|PDB:4GWX, ECO:0007744|PDB:4GWY, ECO:0007744|PDB:4GWZ, ECO:0007744|PDB:4GX3, ECO:0007744|PDB:4GX4, ECO:0007744|PDB:4GX6, ECO:0007744|PDB:4H45, ECO:0007744|PDB:4H46, ECO:0007744|PDB:4KXP, ECO:0007744|PDB:5FBP

Chain	Residue	Details
A	PRO265
B	PRO265
C	PRO265
D	PRO265

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:10913263, ECO:0000269|PubMed:12595528, ECO:0000269|PubMed:1312721, ECO:0000269|PubMed:14530289, ECO:0000269|PubMed:15767255, ECO:0000269|PubMed:17933867, ECO:0000269|PubMed:1849642, ECO:0000269|PubMed:2157849, ECO:0000269|PubMed:2164670, ECO:0007744|PDB:1CNQ, ECO:0007744|PDB:1EYI, ECO:0007744|PDB:1EYJ, ECO:0007744|PDB:1EYK, ECO:0007744|PDB:1FBP, ECO:0007744|PDB:1FJ6, ECO:0007744|PDB:1FJ9, ECO:0007744|PDB:1FSA, ECO:0007744|PDB:1KZ8, ECO:0007744|PDB:1LEV, ECO:0007744|PDB:1NUW, ECO:0007744|PDB:1NUX, ECO:0007744|PDB:1NUY, ECO:0007744|PDB:1NUZ, ECO:0007744|PDB:1NV0, ECO:0007744|PDB:1NV1, ECO:0007744|PDB:1NV2, ECO:0007744|PDB:1NV3, ECO:0007744|PDB:1NV4, ECO:0007744|PDB:1NV5, ECO:0007744|PDB:1NV7, ECO:0007744|PDB:1Q9D, ECO:0007744|PDB:1RDY, ECO:0007744|PDB:1RDZ, ECO:0007744|PDB:1YXI, ECO:0007744|PDB:1YYZ, ECO:0007744|PDB:1YZ0, ECO:0007744|PDB:2F3B, ECO:0007744|PDB:2F3D, ECO:0007744|PDB:4GBW, ECO:0007744|PDB:4GWS, ECO:0007744|PDB:4GWW, ECO:0007744|PDB:4GWX, ECO:0007744|PDB:4GWZ, ECO:0007744|PDB:4GX3, ECO:0007744|PDB:4GX4, ECO:0007744|PDB:4GX6, ECO:0007744|PDB:4H45, ECO:0007744|PDB:4H46, ECO:0007744|PDB:4KXP, ECO:0007744|PDB:5FBP

Chain	Residue	Details
A	LEU275
B	LEU275
C	LEU275
D	LEU275

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: N-acetylthreonine => ECO:0000269|PubMed:6291465, ECO:0000269|PubMed:6296821

Chain	Residue	Details
A	ASP2
B	ASP2
C	ASP2
D	ASP2

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6

Chain	Residue	Details
A	ASP151
B	ASP151
C	ASP151
D	ASP151

---

site_id	SWS_FT_FI9
Number of Residues	4
Details	MOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:6296821

Chain	Residue	Details
A	ILE208
B	ILE208
C	ILE208
D	ILE208

---

site_id	SWS_FT_FI10
Number of Residues	8
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6

Chain	Residue	Details
A	ALA216
A	VAL245
B	ALA216
B	VAL245
C	ALA216
C	VAL245
D	ALA216
D	VAL245

---

site_id	SWS_FT_FI11
Number of Residues	4
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P09467

Chain	Residue	Details
A	PRO265
B	PRO265
C	PRO265
D	PRO265

---

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

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1eyi

Chain	Residue	Details
B	GLU98
B	ASP74

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1eyi

Chain	Residue	Details
C	GLU98
C	ASP74

---

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1eyi

Chain	Residue	Details
D	GLU98
D	ASP74

---

site_id	MCSA1
Number of Residues	8
Details	M-CSA 546

Chain	Residue	Details
A	GLN69	metal ligand, proton acceptor, proton donor
A	VAL75	electrostatic stabiliser, proton acceptor, proton donor
A	GLU98	metal ligand
A	ASP99	electrostatic stabiliser
A	PRO119	metal ligand
A	ASP121	metal ligand
A	GLY122	metal ligand
A	CYS281	metal ligand

---

site_id	MCSA2
Number of Residues	8
Details	M-CSA 546

Chain	Residue	Details
B	GLN69	metal ligand, proton acceptor, proton donor
B	VAL75	electrostatic stabiliser, proton acceptor, proton donor
B	GLU98	metal ligand
B	ASP99	electrostatic stabiliser
B	PRO119	metal ligand
B	ASP121	metal ligand
B	GLY122	metal ligand
B	CYS281	metal ligand

---

site_id	MCSA3
Number of Residues	8
Details	M-CSA 546

Chain	Residue	Details
C	GLN69	metal ligand, proton acceptor, proton donor
C	VAL75	electrostatic stabiliser, proton acceptor, proton donor
C	GLU98	metal ligand
C	ASP99	electrostatic stabiliser
C	PRO119	metal ligand
C	ASP121	metal ligand
C	GLY122	metal ligand
C	CYS281	metal ligand

---

site_id	MCSA4
Number of Residues	8
Details	M-CSA 546

Chain	Residue	Details
D	GLN69	metal ligand, proton acceptor, proton donor
D	VAL75	electrostatic stabiliser, proton acceptor, proton donor
D	GLU98	metal ligand
D	ASP99	electrostatic stabiliser
D	PRO119	metal ligand
D	ASP121	metal ligand
D	GLY122	metal ligand
D	CYS281	metal ligand

---