Structure of PDB 1fta Chain C Binding Site BS01

Receptor Information

>1fta Chain C (length=317) Species: 9606 (Homo sapiens)

DVVTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAVRKAGIAHLYG
IAGKLDVLSNDLVMNMLKSSFATCVLVSEEDKHAIIVEPEKRGKYVVCFD
PLDGSSNIDCLVSVGTIFGIYRKKSTDEPSEKDALQPGRNLVAAGYALYG
SATMLVLAMDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEAYAKD
FDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFLYPANK
KSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPTDIHQRAPIIL
GSPDDVLEFLKVYEKHS

Ligand information

• Ligand ID: AMP
• InChI: InChI=1S/C10H14N5O7P/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(22-10)1-21-23(18,19)20/h2-4,6-7,10,16-17H,1H2,(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
• InChIKey: UDMBCSSLTHHNCD-KQYNXXCUSA-N
• SMILES:
  CACTVS 3.370: Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(O)=O)[CH](O)[CH]3O
  CACTVS 3.370: Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P](O)(O)=O)[C@@H](O)[C@H]3O
  OpenEye OEToolkits 1.7.6: c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=O)(O)O)O)O)N
  ACDLabs 12.01: O=P(O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
  OpenEye OEToolkits 1.7.6: c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)O)O)O)N
• Formula: C10 H14 N5 O7 P
• Name: ADENOSINE MONOPHOSPHATE
• ChEMBL: CHEMBL752
• DrugBank: DB00131
• ZINC: ZINC000003860156
• PDB chain: 1fta Chain C Residue 338

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1fta The allosteric site of human liver fructose-1,6-bisphosphatase. Analysis of six AMP site mutants based on the crystal structure.
• Resolution: 2.3 Å
• Binding residue (original residue number in PDB): V17 E20 G21 A24 G26 T27 G28 E29 L30 K112 Y113 R140 M177
• Binding residue (residue number reindexed from 1): V9 E12 G13 A16 G18 T19 G20 E21 L22 K94 Y95 R122 M159
• Annotation score: 1
• Binding affinity: PDBbind-CN: -logKd/Ki=6.36,IC50=0.44uM
  BindingDB: IC50=3200nM

Enzymatic activity

• Catalytic site (original residue number in PDB): D74 E97 E98 D118 L120 D121 E280
• Catalytic site (residue number reindexed from 1): D56 E79 E80 D100 L102 D103 E262
• Enzyme Commision number: 3.1.3.11: fructose-bisphosphatase.

Gene Ontology

Molecular Function

• GO:0005515 protein binding
• 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
• GO:0061629 RNA polymerase II-specific DNA-binding transcription factor binding

Biological Process

• GO:0000122 negative regulation of transcription by RNA polymerase II
• 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:0031667 response to nutrient levels
• GO:0032869 cellular response to insulin stimulus
• GO:0045820 negative regulation of glycolytic process
• GO:0046580 negative regulation of Ras protein signal transduction
• GO:0071286 cellular response to magnesium ion
• GO:0071320 cellular response to cAMP
• GO:0071466 cellular response to xenobiotic stimulus
• GO:0071475 cellular hyperosmotic salinity response
• GO:0071477 cellular hypotonic salinity response
• GO:0097403 cellular response to raffinose
• GO:1904628 cellular response to phorbol 13-acetate 12-myristate

Cellular Component

• GO:0005615 extracellular space
• GO:0005634 nucleus
• GO:0005737 cytoplasm
• GO:0005829 cytosol
• GO:0070062 extracellular exosome

External links

• PDB: RCSB:1fta, PDBe:1fta, PDBj:1fta
• PDBsum: 1fta
• PubMed: 7961695
• UniProt: P09467|F16P1_HUMAN Fructose-1,6-bisphosphatase 1 (Gene Name=FBP1)