Structure of PDB 2zo9 Chain B Binding Site BS01

Receptor Information
>2zo9 Chain B (length=271) Species: 548 (Klebsiella aerogenes) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MLLAHISDTHFRSRGEKLYGFIDVNAANADVVSQLNALRERPDAVVVSGD
IVNCGRPEEYQVARQILGSLNYPLYLIPGNHDDKALFLEYLQPLCPQLGS
DANNMRCAVDDFATRLLFIDSSRAGTSKGWLTDETISWLEAQLFEGGDKP
ATIFMHHPPLPLGNAQMDPIACENGHRLLALVERFPSLTRIFCGHNHSLT
MTQYRQALISTLPGTVHQVPYCHADTDPYYDLSPASCLMHRQVGEQWVSY
QHSLAHYAGPWLYDENISCPT
Ligand information
Ligand IDFE2
InChIInChI=1S/Fe/q+2
InChIKeyCWYNVVGOOAEACU-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Fe+2]
CACTVS 3.341[Fe++]
FormulaFe
NameFE (II) ION
ChEMBL
DrugBankDB14510
ZINC
PDB chain2zo9 Chain B Residue 275 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2zo9 Malonate-bound structure of the glycerophosphodiesterase from Enterobacter aerogenes (GpdQ) and characterization of the native Fe2+ metal-ion preference.
Resolution2.2 Å
Binding residue
(original residue number in PDB)
D8 H10 D50 H197
Binding residue
(residue number reindexed from 1)
D8 H10 D50 H197
Annotation score1
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
PDBsum2zo9
PubMed18678932
UniProtQ6XBH1|GPDQ_KLEAE Glycerophosphodiester phosphodiesterase GpdQ (Gene Name=gpdQ)

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