Structure of PDB 6vtv Chain A Binding Site BS01

Receptor Information
>6vtv Chain A (length=249) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NNPVIGVVMCRNRLKGHATQTLQEKYLNAIIHAGGLPIALPHALAEPSLL
EQLLPKLDGIYLPGSPSNVQPHLYGENGDEPDADPGRDLLSMAIINAALE
RRIPIFAICRGLQELVVATGGSLHRKLCEQPELLEHREDPELPVEQQYAP
SHEVQVEEGGLLSALLPECSNFWVNSLHGQGAKVVSPRLRVEARSPDGLV
EAVSVINHPFALGVQWHPEWNSSEYALSRILFEGFITACQHHIAEKQRL
Ligand information
Ligand IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain6vtv Chain A Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6vtv PuuD gamma-glutamyl-gamma-aminobutyrate hydrolase
Resolution2.06 Å
Binding residue
(original residue number in PDB)
H145 H161 S185 H187 E210
Binding residue
(residue number reindexed from 1)
H136 H152 S176 H178 E201
Annotation score1
Enzymatic activity
Enzyme Commision number 3.5.1.94: gamma-glutamyl-gamma-aminobutyrate hydrolase.
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0016811 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
GO:0033969 gamma-glutamyl-gamma-aminobutyrate hydrolase activity
Biological Process
GO:0006598 polyamine catabolic process
GO:0009447 putrescine catabolic process

View graph for
Molecular Function

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Biological Process
External links
PDB RCSB:6vtv, PDBe:6vtv, PDBj:6vtv
PDBsum6vtv
PubMed
UniProtP76038|PUUD_ECOLI Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (Gene Name=puuD)

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