Structure of PDB 3lv0 Chain A

Receptor sequence
>3lv0A (length=258) Species: 38323 (Bartonella henselae) [Search protein sequence]
SAVMNVMVQAAMKAGRSLVRDYGEVQNLQVSLKGPADYVSQADRKAEKII
FNELSKARPKFGFLMEESEEIIGEDSQHRFIVDPLDGTTNFLHGIPFFAV
SIALESQGKIVAGVIYNPINDELFTAERGSGAFFNDRRCRVSARRRLEDC
VIATGMPHLPGHGTYLIELRNVMAEVSGIRRFGTAALDLAYVAAGRTDGF
WEDNLQIWDMAAGILMVREAGGFVTDKEGGNDIFRKKNIIAGNEHIRIKL
ERALKKGI
3D structure
PDB3lv0 Crystal structure of extragenic suppressor protein suhB from Bartonella henselae
ChainA
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E69 D86 L88 D89 T91 D214
Catalytic site (residue number reindexed from 1) E66 D83 L85 D86 T88 D209
Enzyme Commision number 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 MG A E69 D86 L88 E66 D83 L85
Gene Ontology
Molecular Function
GO:0008934 inositol monophosphate 1-phosphatase activity
GO:0016787 hydrolase 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:3lv0, PDBe:3lv0, PDBj:3lv0
PDBsum3lv0
PubMed
UniProtA0A0H3M6W8

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