Structure of PDB 6gpe Chain A

Receptor sequence
>6gpeA (length=291) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
QDYSGFTLTPSAQSPRLLELTFTEQTTKQFLEQVAEWPVQALEYKSFLRF
RVAKILDDLCANQLQPLLLKTLLNRAEGALLINAVGVDDVKQADEMVKLA
TAVAHLIGRSNFDAMSGQYYARFVVKHRVMELHNDGTYVEEITDYVLMMK
IDEQNMQGGNSLLLHLDDWEHLDNYFRHPLARRPMRFAAKDVFHPVFDVD
QQGRPVMRYIDQFVQPKDFEEGVWLSELSDAIETSKGILSVPVPVGKFLL
INNLFWLHGRDRFTPHPDLRRELMRQRGYFAYASNHYQTHQ
3D structure
PDB6gpe Widespread bacterial lysine degradation proceeding via glutarate and L-2-hydroxyglutarate.
ChainA
Resolution2.2 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.11.64: glutarate dioxygenase.
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 A H160 D162 H292 H133 D135 H258
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:6gpe, PDBe:6gpe, PDBj:6gpe
PDBsum6gpe
PubMed30498244
UniProtP76621|GLAH_ECOLI Glutarate 2-hydroxylase (Gene Name=glaH)

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