Structure of PDB 1umg Chain A Binding Site BS02

Receptor Information

>1umg Chain A (length=359) Species: 273063 (Sulfurisphaera tokodaii str. 7)

KTTISVIKADIGSLAGHHIVHPDTMAAANKVLASAKEQGIILDYYITHVG
DDLQLIMTHTRGELDTKVHETAWNAFKEAAKVAKDLGLYAAGQDLLSDSF
SGNVRGLGPGVAEMEIEERASEPIAIFMADKTEPGAYNLPLYKMFADPFN
TPGLVIDPTMHGGFKFEVLDVYQGEAVMLSAPQEIYDLLALIGTPARYVI
RRVYRNEDNLLAAVVSIERLNLIYVGKDDPVMIVRLQHGLPALGEALEAF
AFPHLVPGWMRGSHYGPLMPVSQRDAKATRFDGPPRLLGLGFNVKNGRLV
GPTDLFDDPAFDETRRLANIVADYMRRHGPFMPHRLEPTEMEYTTLPLIL
EKLKDRFKK

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: 1umg Chain A Residue 403

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1umg The first crystal structure of the novel class of fructose-1,6-bisphosphatase present in thermophilic archaea.
• Resolution: 1.8 Å
• Binding residue (original residue number in PDB): D53 D54 D132 D234
• Binding residue (residue number reindexed from 1): D51 D52 D130 D229
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 3.1.3.11: fructose-bisphosphatase.
  4.1.2.13: fructose-bisphosphate aldolase.

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0004332 fructose-bisphosphate aldolase activity
• GO:0016787 hydrolase activity
• GO:0016829 lyase activity
• GO:0042132 fructose 1,6-bisphosphate 1-phosphatase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006094 gluconeogenesis
• GO:0006096 glycolytic process
• GO:0006740 NADPH regeneration
• GO:0016311 dephosphorylation

External links

• PDB: RCSB:1umg, PDBe:1umg, PDBj:1umg
• PDBsum: 1umg
• PubMed: 15274916
• UniProt: F9VMT6|FBPAP_SULTO Fructose-1,6-bisphosphate aldolase/phosphatase (Gene Name=fbp)