Structure of PDB 6hl9 Chain A Binding Site BS01
Receptor Information
>6hl9 Chain A (length=299) Species:
83333
(Escherichia coli K-12) [
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QDYSGFTLTPSAQSPRLLELTFTEQTTKQFLEQVAEWPVQALEYKSFLRF
RVAKILDDLCANQLQPLLLKTLLNRAEGALLINAVGVDDVKQADEMVKLA
TAVAHLIGRSNFDAMSGQYYARFVVKNYLRQPHRVMELHNDGTYVEEITD
YVLMMKIDEQNMQGGNSLLLHLDDWEHLDNYFRHPLARRPMRFAAPPSKD
VFHPVFDVDQQGRPVMRYIDQFVQPKDFEEGVWLSELSDAIETSKGILSV
PVPVGKFLLINNLFWLHGRDRFTPHPDLRRELMRQRGYFAYASNHYQTH
Ligand information
Ligand ID
FE2
InChI
InChI=1S/Fe/q+2
InChIKey
CWYNVVGOOAEACU-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Fe+2]
CACTVS 3.341
[Fe++]
Formula
Fe
Name
FE (II) ION
ChEMBL
DrugBank
DB14510
ZINC
PDB chain
6hl9 Chain A Residue 401 [
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Receptor-Ligand Complex Structure
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PDB
6hl9
Widespread bacterial lysine degradation proceeding via glutarate and L-2-hydroxyglutarate.
Resolution
2.3 Å
Binding residue
(original residue number in PDB)
H160 D162 H292
Binding residue
(residue number reindexed from 1)
H139 D141 H267
Annotation score
1
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
View graph for
Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:6hl9
,
PDBe:6hl9
,
PDBj:6hl9
PDBsum
6hl9
PubMed
30498244
UniProt
P76621
|GLAH_ECOLI Glutarate 2-hydroxylase (Gene Name=glaH)
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