Structure of PDB 3lv0 Chain B Binding Site BS01

Receptor Information
>3lv0 Chain B (length=254) Species: 38323 (Bartonella henselae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SAVMNVMVQAAMKAGRSLVRDYGLQVSLKGPADYVSQADRKAEKIIFNEL
SKARPKFGFLMEESEEIIGEDSQHRFIVDPLDGTTNFLHGIPFFAVSIAL
ESQGKIVAGVIYNPINDELFTAERGSGAFFNDRRCRVSARRRLEDCVIAT
GMPHLPGHGTYLIELRNVMAEVSGIRRFGTAALDLAYVAAGRTDGFWEDN
LQIWDMAAGILMVREAGGFVTDKEGGNDIFRKKNIIAGNEHIRIKLERAL
KKGI
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain3lv0 Chain B Residue 264 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3lv0 Crystal structure of extragenic suppressor protein suhB from Bartonella henselae
Resolution1.85 Å
Binding residue
(original residue number in PDB)
E69 D86 L88
Binding residue
(residue number reindexed from 1)
E62 D79 L81
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) E69 D86 L88 D89 T91 D214
Catalytic site (residue number reindexed from 1) E62 D79 L81 D82 T84 D205
Enzyme Commision number 3.1.3.25: inositol-phosphate phosphatase.
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

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:3lv0, PDBe:3lv0, PDBj:3lv0
PDBsum3lv0
PubMed
UniProtA0A0H3M6W8

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