Structure of PDB 1umg Chain A

Receptor sequence

>1umgA (length=359) Species: 273063 (Sulfurisphaera tokodaii str. 7)

KTTISVIKADIGSLAGHHIVHPDTMAAANKVLASAKEQGIILDYYITHVG
DDLQLIMTHTRGELDTKVHETAWNAFKEAAKVAKDLGLYAAGQDLLSDSF
SGNVRGLGPGVAEMEIEERASEPIAIFMADKTEPGAYNLPLYKMFADPFN
TPGLVIDPTMHGGFKFEVLDVYQGEAVMLSAPQEIYDLLALIGTPARYVI
RRVYRNEDNLLAAVVSIERLNLIYVGKDDPVMIVRLQHGLPALGEALEAF
AFPHLVPGWMRGSHYGPLMPVSQRDAKATRFDGPPRLLGLGFNVKNGRLV
GPTDLFDDPAFDETRRLANIVADYMRRHGPFMPHRLEPTEMEYTTLPLIL
EKLKDRFKK

3D structure

• PDB: 1umg The first crystal structure of the novel class of fructose-1,6-bisphosphatase present in thermophilic archaea.
• Chain: A
• Resolution: 1.8 Å

Enzymatic activity

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

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	MG	A	D233 D234	D228 D229
BS02	MG	A	D53 D54 D132 D234	D51 D52 D130 D229
BS03	MG	A	D12 H19 D53 Q95	D10 H17 D51 Q93
BS04	2FP	A	H19 D53 Y91 Q95 S103 G104 N105 K133 D233 D234 M265 R266 D287 Y348	H17 D51 Y89 Q93 S101 G102 N103 K131 D228 D229 M260 R261 D282 Y343

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)