Structure of PDB 3lv0 Chain B Binding Site BS01
Receptor Information
>3lv0 Chain B (length=254) Species:
38323
(Bartonella henselae) [
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SAVMNVMVQAAMKAGRSLVRDYGLQVSLKGPADYVSQADRKAEKIIFNEL
SKARPKFGFLMEESEEIIGEDSQHRFIVDPLDGTTNFLHGIPFFAVSIAL
ESQGKIVAGVIYNPINDELFTAERGSGAFFNDRRCRVSARRRLEDCVIAT
GMPHLPGHGTYLIELRNVMAEVSGIRRFGTAALDLAYVAAGRTDGFWEDN
LQIWDMAAGILMVREAGGFVTDKEGGNDIFRKKNIIAGNEHIRIKLERAL
KKGI
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
3lv0 Chain B Residue 264 [
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Receptor-Ligand Complex Structure
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PDB
3lv0
Crystal structure of extragenic suppressor protein suhB from Bartonella henselae
Resolution
1.85 Å
Binding residue
(original residue number in PDB)
E69 D86 L88
Binding residue
(residue number reindexed from 1)
E62 D79 L81
Annotation score
1
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
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Biological Process
External links
PDB
RCSB:3lv0
,
PDBe:3lv0
,
PDBj:3lv0
PDBsum
3lv0
PubMed
UniProt
A0A0H3M6W8
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