Structure of PDB 6hl8 Chain A Binding Site BS02

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 IDGUA
InChIInChI=1S/C5H8O4/c6-4(7)2-1-3-5(8)9/h1-3H2,(H,6,7)(H,8,9)
InChIKeyJFCQEDHGNNZCLN-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(CC(=O)O)CC(=O)O
ACDLabs 10.04O=C(O)CCCC(=O)O
CACTVS 3.341OC(=O)CCCC(O)=O
FormulaC5 H8 O4
NameGLUTARIC ACID
ChEMBLCHEMBL1162495
DrugBankDB03553
ZINCZINC000000388706
PDB chain6hl8 Chain A Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB6hl8 Widespread bacterial lysine degradation proceeding via glutarate and L-2-hydroxyglutarate.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		D162 G163 Y165 R311
Binding residue
(residue number reindexed from 1)		D135 G136 Y138 R277
Annotation score5
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
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6hl8, PDBe:6hl8, PDBj:6hl8
PDBsum6hl8
PubMed30498244
UniProtP76621|GLAH_ECOLI Glutarate 2-hydroxylase (Gene Name=glaH)

[Back to BioLiP]