Structure of PDB 2zoa Chain B

Receptor sequence
>2zoaB (length=271) Species: 548 (Klebsiella aerogenes) [Search protein sequence]
MLLAHISDTHFRSRGEKLYGFIDVNAANADVVSQLNALRERPDAVVVSGD
IVNCGRPEEYQVARQILGSLNYPLYLIPGNHDDKALFLEYLQPLCPQLGS
DANNMRCAVDDFATRLLFIDSSRAGTSKGWLTDETISWLEAQLFEGGDKP
ATIFMHHPPLPLGNAQMDPIACENGHRLLALVERFPSLTRIFCGHNHSLT
MTQYRQALISTLPGTVHQVPYCHADTDPYYDLSPASCLMHRQVGEQWVSY
QHSLAHYAGPWLYDENISCPT
3D structure
PDB2zoa Malonate-bound structure of the glycerophosphodiesterase from Enterobacter aerogenes (GpdQ) and characterization of the native Fe2+ metal-ion preference.
ChainB
Resolution2.4 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.1.4.46: glycerophosphodiester phosphodiesterase.
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 FE2 B D8 H10 D50 H197 D8 H10 D50 H197
BS02 FE2 B D50 N80 H156 H195 D50 N80 H156 H195
BS03 MLI B H10 N80 H81 H195 H10 N80 H81 H195
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:2zoa, PDBe:2zoa, PDBj:2zoa
PDBsum2zoa
PubMed18678932
UniProtQ6XBH1|GPDQ_KLEAE Glycerophosphodiester phosphodiesterase GpdQ (Gene Name=gpdQ)

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