Structure of PDB 1cnq Chain A

Receptor sequence

>1cnqA (length=332) Species: 9823 (Sus scrofa) [Search protein sequence]

FDTNIVTLTRFVMEEGRKARGTGEMTQLLNSLCTAVKAISTAVRKAGIAH
LYGIAGSTNVTGDQVKKLDVLSNDLVINVLKSSFATCVLVSEEDKNAIIV
EPEKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKNSTDEPSEKDALQP
GRNLVAAGYALYGSATMLVLAMVNGVNCFMLDPAIGEFILVDRDVKIKKK
GSIYSINEGYAKEFDPAITEYIQRKKFPPDNSAPYGARYVGSMVADVHRT
LVYGGIFMYPANKKSPKGKLRLLYECNPMAYVMEKAGGLATTGKEAVLDI
VPTDIHQRAPIILGSPEDVTELLEIYQKHAAK

3D structure

PDB

1cnq Role of a dynamic loop in cation activation and allosteric regulation of recombinant porcine fructose-1,6-bisphosphatase.

Chain

Resolution

2.27 Å

3D
structure

Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]

Enzymatic activity

Catalytic site (original residue number in PDB)	D68 D74 E97 E98 D118 L120 D121 E280
Catalytic site (residue number reindexed from 1)	D63 D69 E92 E93 D113 L115 D116 E275
Enzyme Commision number	3.1.3.11: fructose-bisphosphatase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)
BS01	F6P	A	G26 T27 G28 E29 M30 K112 Y113 V160 M177	G21 T22 G23 E24 M25 K107 Y108 V155 M172
BS02	F6P	A	D121 G122 N212 Y215 Y244 G246 M248 Y264 K274 R276	D116 G117 N207 Y210 Y239 G241 M243 Y259 K269 R271
BS03	ZN	A	E97 D118 L120	E92 D113 L115
BS04	ZN	A	D118 D121 E280	D113 D116 E275
BS05	ZN	A	D68 E97	D63 E92
BS06	PO4	A	E97 D118 L120 D121 G122 S123 R276	E92 D113 L115 D116 G117 S118 R271

Gene Ontology

	Molecular Function
GO:0016208	AMP binding
GO:0016787	hydrolase activity
GO:0016791	phosphatase activity
GO:0042132	fructose 1,6-bisphosphate 1-phosphatase activity
GO:0042578	phosphoric ester hydrolase activity
GO:0042802	identical protein binding
GO:0046872	metal ion binding
GO:0048029	monosaccharide binding

	Biological Process
GO:0005975	carbohydrate metabolic process
GO:0005986	sucrose biosynthetic process
GO:0006000	fructose metabolic process
GO:0006002	fructose 6-phosphate metabolic process
GO:0006094	gluconeogenesis
GO:0006111	regulation of gluconeogenesis
GO:0016311	dephosphorylation
GO:0030308	negative regulation of cell growth
GO:0030388	fructose 1,6-bisphosphate metabolic process
GO:0045820	negative regulation of glycolytic process
GO:0046580	negative regulation of Ras protein signal transduction
GO:0071286	cellular response to magnesium ion
GO:0071466	cellular response to xenobiotic stimulus

	Cellular Component
GO:0005737	cytoplasm
GO:0005829	cytosol

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:1cnq, PDBe:1cnq, PDBj:1cnq
PDBsum	1cnq
PubMed	9708979
UniProt	P00636\|F16P1_PIG Fructose-1,6-bisphosphatase 1 (Gene Name=FBP1)

[Back to BioLiP]