Structure of PDB 2qvv Chain A Binding Site BS03

Receptor Information
>2qvv Chain A (length=329) Species: 9823 (Sus scrofa) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NIVTLTRFVMEEGRKARGTGEMTQLLNSLCTAVKAISTAVRKAGIAHLYG
IAGSTNVTGDQVKKLDVLSNDLVINVLKSSFATCVLVSEEDKNAIIVEPE
KRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKNSTDEPSEKDALQPGRN
LVAAGYALYGSATMLVLAMVNGVNCFMLDPAIGEFILVDRDVKIKKKGSI
YSINEGYAKEFDPAITEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVY
GGIFMYPANKKSPKGKLRLLYECNPMAYVMEKAGGLATTGKEAVLDIVPT
DIHQRAPIILGSPEDVTELLEIYQKHAAK
Ligand information
Ligand IDPO4
InChIInChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
InChIKeyNBIIXXVUZAFLBC-UHFFFAOYSA-K
SMILES
SoftwareSMILES
CACTVS 3.341[O-][P]([O-])([O-])=O
ACDLabs 10.04[O-]P([O-])([O-])=O
OpenEye OEToolkits 1.5.0[O-]P(=O)([O-])[O-]
FormulaO4 P
NamePHOSPHATE ION
ChEMBL
DrugBankDB14523
ZINC
PDB chain2qvv Chain A Residue 400 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB2qvv Structures of mammalian and bacterial fructose-1,6-bisphosphatase reveal the basis for synergism in AMP/fructose 2,6-bisphosphate inhibition
Resolution2.03 Å
Binding residue
(original residue number in PDB)		G26 T27 G28 E29 M30 Y113
Binding residue
(residue number reindexed from 1)		G18 T19 G20 E21 M22 Y105
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) D68 D74 E97 E98 D118 L120 D121 E280
Catalytic site (residue number reindexed from 1) D60 D66 E89 E90 D110 L112 D113 E272
Enzyme Commision number 3.1.3.11: fructose-bisphosphatase.
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:2qvv, PDBe:2qvv, PDBj:2qvv
PDBsum2qvv
PubMed17933867
UniProtP00636|F16P1_PIG Fructose-1,6-bisphosphatase 1 (Gene Name=FBP1)

[Back to BioLiP]