Structure of PDB 3t2b Chain A

Receptor sequence
>3t2bA (length=379) Species: 444157 (Pyrobaculum neutrophilum V24Sta) [Search protein sequence]
MRVTVSIIKADVGGFPGHAHVHPKMLEYAAAKLKEAQKRGVIIDYFVYNV
GDDISLLMTHTKGEDNKDIHGLAWETFKEVTDQIAKRFKLYGAGQDLSGN
IRGMGPQVAEMEFEERPSEPIIAFAADKTEPGAFNLPLYKMFADPFTTAG
LVIDPSMHEGFIFEVLDVVEHKVYLLKTPEDAYSLLGLIGTTGRYIIRKV
FRRADGAPAAANSVERLSYVGKDDPVLLVRAQSGLPAVGEVLEAFAHPHL
VHGWMRGSHAGPLMPARFISVDPERRIAIGPKMTRFDGPPKVGALGFQLH
EGYLEGGVDLFDDPAFDYVRQTAAQIADYIRRMGPFQPHRLPPEEMEYTA
LPKILAKVKPYPADQYEKDRKKYIEAVVK
3D structure
PDB3t2b Active-site remodelling in the bifunctional fructose-1,6-bisphosphate aldolase/phosphatase.
ChainA
Resolution1.52 Å
3D
structure
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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 D11 H18 D52 D11 H18 D52
BS02 MG A D52 D53 D132 D234 D52 D53 D127 D224
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

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Molecular Function
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Biological Process
External links
PDB RCSB:3t2b, PDBe:3t2b, PDBj:3t2b
PDBsum3t2b
PubMed21983965
UniProtB1YAL1|FBPAP_PYRNV Fructose-1,6-bisphosphate aldolase/phosphatase (Gene Name=fbp)

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