Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3IFA

Human muscle fructose-1,6-bisphosphatase E69Q mutant in complex with AMP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005975	biological_process	carbohydrate metabolic process
A	0006000	biological_process	fructose metabolic process
A	0006094	biological_process	gluconeogenesis
A	0016787	molecular_function	hydrolase activity
A	0016791	molecular_function	phosphatase activity
A	0030018	cellular_component	Z disc
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	0046872	molecular_function	metal ion binding
A	0070062	cellular_component	extracellular exosome
A	0070161	cellular_component	anchoring junction
B	0003824	molecular_function	catalytic activity
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005975	biological_process	carbohydrate metabolic process
B	0006000	biological_process	fructose metabolic process
B	0006094	biological_process	gluconeogenesis
B	0016787	molecular_function	hydrolase activity
B	0016791	molecular_function	phosphatase activity
B	0030018	cellular_component	Z disc
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	0046872	molecular_function	metal ion binding
B	0070062	cellular_component	extracellular exosome
B	0070161	cellular_component	anchoring junction
C	0003824	molecular_function	catalytic activity
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0005975	biological_process	carbohydrate metabolic process
C	0006000	biological_process	fructose metabolic process
C	0006094	biological_process	gluconeogenesis
C	0016787	molecular_function	hydrolase activity
C	0016791	molecular_function	phosphatase activity
C	0030018	cellular_component	Z disc
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	0046872	molecular_function	metal ion binding
C	0070062	cellular_component	extracellular exosome
C	0070161	cellular_component	anchoring junction
D	0003824	molecular_function	catalytic activity
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0005975	biological_process	carbohydrate metabolic process
D	0006000	biological_process	fructose metabolic process
D	0006094	biological_process	gluconeogenesis
D	0016787	molecular_function	hydrolase activity
D	0016791	molecular_function	phosphatase activity
D	0030018	cellular_component	Z disc
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	0046872	molecular_function	metal ion binding
D	0070062	cellular_component	extracellular exosome
D	0070161	cellular_component	anchoring junction

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE AMP A 339

Chain	Residue
A	VAL17
A	LYS112
A	TYR113
A	ARG140
A	THR177
A	HOH363
A	HOH390
A	HOH415
A	HOH515
A	HOH538
A	LYS20
A	GLY21
A	ALA24
A	THR27
A	GLY28
A	GLU29
A	LEU30
A	THR31

site_id	AC2
Number of Residues	19
Details	BINDING SITE FOR RESIDUE AMP B 339

Chain	Residue
B	VAL17
B	LYS20
B	GLY21
B	ALA24
B	GLY26
B	THR27
B	GLY28
B	GLU29
B	LEU30
B	THR31
B	LYS112
B	TYR113
B	THR177
B	HOH344
B	HOH345
B	HOH417
B	HOH423
B	HOH424
B	HOH447

site_id	AC3
Number of Residues	20
Details	BINDING SITE FOR RESIDUE AMP C 339

Chain	Residue
C	VAL17
C	LYS20
C	GLY21
C	ALA24
C	GLY26
C	THR27
C	GLY28
C	GLU29
C	LEU30
C	THR31
C	LYS112
C	TYR113
C	VAL160
C	THR177
C	HOH373
C	HOH405
C	HOH462
C	HOH568
C	HOH569
C	HOH587

site_id	AC4
Number of Residues	18
Details	BINDING SITE FOR RESIDUE AMP D 339

Chain	Residue
D	VAL17
D	LYS20
D	GLY21
D	ALA24
D	GLY26
D	THR27
D	GLY28
D	GLU29
D	LEU30
D	THR31
D	LYS112
D	TYR113
D	ARG140
D	THR177
D	HOH357
D	HOH358
D	HOH375
D	HOH521

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 A 340

Chain	Residue
A	ASN212
A	TYR215
A	ARG243
A	TYR244
A	TYR264
A	LYS274
A	HOH397
A	HOH549

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 341

Chain	Residue
A	LYS274
A	ARG276
A	ARG313
A	HOH452

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 342

Chain	Residue
A	GLY122
A	SER123
A	SER124

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 343

Chain	Residue
A	LYS207
A	SER237
A	ALA238
A	HOH431

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 B 340

Chain	Residue
B	LYS274
B	HOH362
B	ASN212
B	TYR215
B	ARG243
B	TYR244
B	TYR264

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 341

Chain	Residue
B	GLY122
B	SER123
B	SER124

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 342

Chain	Residue
B	LYS274
B	ARG276
B	ARG313
B	HOH405

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 340

Chain	Residue
C	ASP121
C	GLY122
C	SER123
C	SER124

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 341

Chain	Residue
C	ASN212
C	TYR215
C	ARG243
C	TYR244
C	TYR264
C	HOH571

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 342

Chain	Residue
C	LYS274
C	ARG276
C	ARG313

site_id	BC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 D 340

Chain	Residue
D	ASN212
D	TYR215
D	ARG243
D	TYR244
D	TYR264
D	LYS274
D	HOH364

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 D 341

Chain	Residue
D	LYS274
D	ARG276
D	ARG313
D	HOH371

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 D 342

Chain	Residue
D	ASP121
D	GLY122
D	SER123
D	SER124

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 344

Chain	Residue
A	ASN99
A	LYS100
A	ASP101
A	HOH641

site_id	CC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 345

Chain	Residue
A	LYS217
A	TYR218
A	LYS269
A	HOH430
A	HOH445

site_id	CC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 346

Chain	Residue
A	LYS203
A	LYS204
A	LYS205
A	HOH401

site_id	CC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 343

Chain	Residue
B	ASN99
B	LYS100
B	ASP101

site_id	CC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL C 343

Chain	Residue
C	ASN99
C	LYS100
C	ASP101
C	HOH431

site_id	CC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL D 343

Chain	Residue
D	GLU98
D	ASN99
D	LYS100
D	ASP101
D	GLU146

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLY273-ALA285

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	Motif: {"description":"Nuclear localization signal","evidences":[{"source":"PubMed","id":"19626708","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"PubMed","id":"22120740","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	57
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Site: {"description":"Important for the conversion from active R-state to inactive T-state in the presence of AMP"}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	8
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q9Z1N1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)