Structure of PDB 2zo9 Chain B Binding Site BS01
Receptor Information
>2zo9 Chain B (length=271) Species:
548
(Klebsiella aerogenes) [
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MLLAHISDTHFRSRGEKLYGFIDVNAANADVVSQLNALRERPDAVVVSGD
IVNCGRPEEYQVARQILGSLNYPLYLIPGNHDDKALFLEYLQPLCPQLGS
DANNMRCAVDDFATRLLFIDSSRAGTSKGWLTDETISWLEAQLFEGGDKP
ATIFMHHPPLPLGNAQMDPIACENGHRLLALVERFPSLTRIFCGHNHSLT
MTQYRQALISTLPGTVHQVPYCHADTDPYYDLSPASCLMHRQVGEQWVSY
QHSLAHYAGPWLYDENISCPT
Ligand information
Ligand ID
FE2
InChI
InChI=1S/Fe/q+2
InChIKey
CWYNVVGOOAEACU-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Fe+2]
CACTVS 3.341
[Fe++]
Formula
Fe
Name
FE (II) ION
ChEMBL
DrugBank
DB14510
ZINC
PDB chain
2zo9 Chain B Residue 275 [
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Receptor-Ligand Complex Structure
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PDB
2zo9
Malonate-bound structure of the glycerophosphodiesterase from Enterobacter aerogenes (GpdQ) and characterization of the native Fe2+ metal-ion preference.
Resolution
2.2 Å
Binding residue
(original residue number in PDB)
D8 H10 D50 H197
Binding residue
(residue number reindexed from 1)
D8 H10 D50 H197
Annotation score
1
Enzymatic activity
Enzyme Commision number
3.1.4.46
: glycerophosphodiester phosphodiesterase.
Gene Ontology
Molecular Function
GO:0004112
cyclic-nucleotide phosphodiesterase activity
GO:0004115
3',5'-cyclic-AMP phosphodiesterase activity
GO:0008889
glycerophosphodiester phosphodiesterase activity
GO:0016787
hydrolase activity
GO:0046872
metal ion binding
Biological Process
GO:0006071
glycerol metabolic process
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Molecular Function
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Biological Process
External links
PDB
RCSB:2zo9
,
PDBe:2zo9
,
PDBj:2zo9
PDBsum
2zo9
PubMed
18678932
UniProt
Q6XBH1
|GPDQ_KLEAE Glycerophosphodiester phosphodiesterase GpdQ (Gene Name=gpdQ)
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