Structure of PDB 5a5l Chain A Binding Site BS03

Receptor Information

>5a5l Chain A (length=338) Species: 146786 (Thermosynechococcus vestitus)

SMDNVIGLEIIEVVEQAAIASARWMGKGDKNMADQAAVDAMRNRMNQIHM
RGRIVIGEGERDEAPMLYIGEEVGICTRPDAAQYCNPEELIEIDIAVDPC
EGTNLCAYGQPGSMAVLAISEKGGLFAAPDFYMKKLAAPPAAKGKVDIRN
SATENLKILSECLDRAIDELVVVVMKRDRHNDLIQEIRDAGARVQLISDG
DVSAALACAFSGTNIHALMGIGAAPEGVISAAAMRALGGHFQGQLVYDPA
VVMTKEWANRTREGNLEELKKAGITDPDKVYEAEELASGETVLFAACGIT
PGMLMKGVRFFKGGARTQSLVISTQSKTARFVDTIHMF

Ligand information

• Ligand ID: MG
• InChI: InChI=1S/Mg/q+2
• InChIKey: JLVVSXFLKOJNIY-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mg+2]
  CACTVS 3.341: [Mg++]
• Formula: Mg
• Name: MAGNESIUM ION
• DrugBank: DB01378
• PDB chain: 5a5l Chain A Residue 1342

Receptor-Ligand Complex Structure

Structure summary

• PDB: 5a5l Structure of the Dual-Function Fructose-1,6/Sedoheptulose-1, 7-Bisphosphatase from Thermosynechococcus Elongatus Bound with Sedoheptulose-7-Phosphate.
• Resolution: 2.34 Å
• Binding residue (original residue number in PDB): D97 E225
• Binding residue (residue number reindexed from 1): D98 E226
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 3.1.3.11: fructose-bisphosphatase.
  3.1.3.37: sedoheptulose-bisphosphatase.

Gene Ontology

Molecular Function

• GO:0016787 hydrolase activity
• GO:0042132 fructose 1,6-bisphosphate 1-phosphatase activity
• GO:0046872 metal ion binding
• GO:0050278 sedoheptulose-bisphosphatase activity

Biological Process

• GO:0006071 glycerol metabolic process
• GO:0006094 gluconeogenesis
• GO:0019253 reductive pentose-phosphate cycle
• GO:0030388 fructose 1,6-bisphosphate metabolic process

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:5a5l, PDBe:5a5l, PDBj:5a5l
• PDBsum: 5a5l
• PubMed: 26457528
• UniProt: Q8DJE9|FBSB_THEVB D-fructose 1,6-bisphosphatase class 2/sedoheptulose 1,7-bisphosphatase (Gene Name=tll1276)