Structure of PDB 1lbz Chain B

Receptor sequence
>1lbzB (length=252) Species: 2234 (Archaeoglobus fulgidus) [Search protein sequence]
MDERDALRISREIAGEVRKAIASMPLRERVKDVGMGKDGTPTKAADRVAE
DAALEILRKERVTVVTEESGVLGEGDVFVALDPLDGTFNATRGIPVYSVS
LCFSYSDKLKDAFFGYVYNLATGDEYYADSSGAYRNGERIEVSDAEELYC
NAIIYYPDRKFPFKRMRIFGSAATELCFFADGSFDCFLDIRPGKMLRIYD
AAAGVFIAEKAGGKVTELDGESLGNKKFDMQERLNIVAANEKLHPKLLEL
IK
3D structure
PDB1lbz Crystal structure of a dual activity IMPase/FBPase (AF2372) from Archaeoglobus fulgidus. The story of a mobile loop.
ChainB
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E367 D382 L384 D385 T387 D500
Catalytic site (residue number reindexed from 1) E67 D82 L84 D85 T87 D200
Enzyme Commision number 3.1.3.11: fructose-bisphosphatase.
3.1.3.25: inositol-phosphate phosphatase.
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 FBP B D385 G386 Y455 Y456 S471 A472 D85 G86 Y155 Y156 S171 A172
BS02 CA B D382 D385 D500 D82 D85 D200
BS03 CA B E367 D382 L384 E67 D82 L84
BS04 CA B T340 P341 E367 T40 P41 E67
Gene Ontology
Molecular Function
GO:0008934 inositol monophosphate 1-phosphatase activity
GO:0016787 hydrolase activity
GO:0042132 fructose 1,6-bisphosphate 1-phosphatase activity
GO:0046872 metal ion binding
GO:0052832 inositol monophosphate 3-phosphatase activity
GO:0052833 inositol monophosphate 4-phosphatase activity
GO:0052834 inositol monophosphate phosphatase activity
Biological Process
GO:0006020 inositol metabolic process
GO:0007165 signal transduction
GO:0046854 phosphatidylinositol phosphate biosynthetic process

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Molecular Function

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Biological Process
External links
PDB RCSB:1lbz, PDBe:1lbz, PDBj:1lbz
PDBsum1lbz
PubMed11940584
UniProtO30298|BSUHB_ARCFU Fructose-1,6-bisphosphatase/inositol-1-monophosphatase (Gene Name=suhB)

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