Structure of PDB 6hl8 Chain A Binding Site BS01

Receptor Information
>6hl8 Chain A (length=291) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QDYSGFTLTPSAQSPRLLELTFTEQTTKQFLEQVAEWPVQALEYKSFLRF
RVAKILDDLCANQLQPLLLKTLLNRAEGALLINAVGVDDVKQADEMVKLA
TAVAHLIGRSNFDAMSGQYYARFVVKHRVMELHNDGTYVEEITDYVLMMK
IDEQNMQGGNSLLLHLDDWEHLDNYFRHPLARRPMRFAAKDVFHPVFDVD
QQGRPVMRYIDQFVQPKDFEEGVWLSELSDAIETSKGILSVPVPVGKFLL
INNLFWLHGRDRFTPHPDLRRELMRQRGYFAYASNHYQTHQ
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 chain6hl8 Chain A Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6hl8 Widespread bacterial lysine degradation proceeding via glutarate and L-2-hydroxyglutarate.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		H160 D162 H292
Binding residue
(residue number reindexed from 1)		H133 D135 H258
Annotation score1
Enzymatic activity
Enzyme Commision number 1.14.11.64: glutarate dioxygenase.
Gene Ontology
Molecular Function
GO:0005506 iron ion binding
GO:0008198 ferrous iron binding
GO:0042802 identical protein binding
GO:0046872 metal ion binding
GO:0050498 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, with 2-oxoglutarate as one donor, and the other dehydrogenated
GO:0051213 dioxygenase activity
GO:0106343 glutarate dioxygenase activity
Biological Process
GO:0019477 L-lysine catabolic process
GO:0090549 response to carbon starvation
Cellular Component
GO:0032991 protein-containing complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6hl8, PDBe:6hl8, PDBj:6hl8
PDBsum6hl8
PubMed30498244
UniProtP76621|GLAH_ECOLI Glutarate 2-hydroxylase (Gene Name=glaH)

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