Structure of PDB 1q9d Chain B Binding Site BS02

Receptor Information
>1q9d Chain B (length=328) Species: 9823 (Sus scrofa) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TNIVTLTRFVMEEGRKARGTGEMTQLLNSLCTAVKAISTAVRKAGIAHLY
GIAGSTNVTGDQVKKLDVLSNDLVINVLKSSFATCVLVSEEDKNAIIVEP
EKRGKYVVCFDPLDGSSNIDCLVSIGTIFGIYRKNSTDEPSEKDALQPGR
NLVAAGYALYGSATMLVLAMVNGVNCFMLDPAIGEFILVDRDVKIKKKGS
IYSINEGYAKEFDPAITEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLV
YGGIFMYPANKKSPKGKLRLLYECNPMAYVMEKAGGLATTGKEAVLDIVP
TDIHQRAPIILGSPEDVTELLEIYQKHA
Ligand information
Ligand IDF6P
InChIInChI=1S/C6H13O9P/c7-2-6(10)5(9)4(8)3(15-6)1-14-16(11,12)13/h3-5,7-10H,1-2H2,(H2,11,12,13)/t3-,4-,5+,6-/m1/s1
InChIKeyBGWGXPAPYGQALX-ARQDHWQXSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=P(O)(O)OCC1OC(O)(CO)C(O)C1O
OpenEye OEToolkits 1.5.0C(C1C(C(C(O1)(CO)O)O)O)OP(=O)(O)O
OpenEye OEToolkits 1.5.0C([C@@H]1[C@H]([C@@H]([C@](O1)(CO)O)O)O)OP(=O)(O)O
CACTVS 3.341OC[C]1(O)O[CH](CO[P](O)(O)=O)[CH](O)[CH]1O
CACTVS 3.341OC[C@@]1(O)O[C@H](CO[P](O)(O)=O)[C@@H](O)[C@@H]1O
FormulaC6 H13 O9 P
Name6-O-phosphono-beta-D-fructofuranose;
FRUCTOSE-6-PHOSPHATE;
6-O-phosphono-beta-D-fructose;
6-O-phosphono-D-fructose;
6-O-phosphono-fructose
ChEMBLCHEMBL604196
DrugBank
ZINCZINC000004096690
PDB chain1q9d Chain B Residue 411 [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]
PDB1q9d Inhibition of fructose-1,6-bisphosphatase by a new class of allosteric effectors
Resolution2.35 Å
Binding residue
(original residue number in PDB)		D121 G122 Y215 Y244 G246 S247 M248 Y264 K274
Binding residue
(residue number reindexed from 1)		D114 G115 Y208 Y237 G239 S240 M241 Y257 K267
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) D68 D74 E97 E98 D118 L120 D121 E280
Catalytic site (residue number reindexed from 1) D61 D67 E90 E91 D111 L113 D114 E273
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:1q9d, PDBe:1q9d, PDBj:1q9d
PDBsum1q9d
PubMed14530289
UniProtP00636|F16P1_PIG Fructose-1,6-bisphosphatase 1 (Gene Name=FBP1)

[Back to BioLiP]