Structure of PDB 6gpe Chain A Binding Site BS01

Receptor Information

>6gpe Chain A (length=291) Species: 83333 (Escherichia coli K-12)

QDYSGFTLTPSAQSPRLLELTFTEQTTKQFLEQVAEWPVQALEYKSFLRF
RVAKILDDLCANQLQPLLLKTLLNRAEGALLINAVGVDDVKQADEMVKLA
TAVAHLIGRSNFDAMSGQYYARFVVKHRVMELHNDGTYVEEITDYVLMMK
IDEQNMQGGNSLLLHLDDWEHLDNYFRHPLARRPMRFAAKDVFHPVFDVD
QQGRPVMRYIDQFVQPKDFEEGVWLSELSDAIETSKGILSVPVPVGKFLL
INNLFWLHGRDRFTPHPDLRRELMRQRGYFAYASNHYQTHQ

Ligand information

• Ligand ID: FE2
• InChI: InChI=1S/Fe/q+2
• InChIKey: CWYNVVGOOAEACU-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Fe+2]
  CACTVS 3.341: [Fe++]
• Formula: Fe
• Name: FE (II) ION
• DrugBank: DB14510
• PDB chain: 6gpe Chain A Residue 401

Receptor-Ligand Complex Structure

Structure summary

• PDB: 6gpe Widespread bacterial lysine degradation proceeding via glutarate and L-2-hydroxyglutarate.
• Resolution: 2.2 Å
• Binding residue (original residue number in PDB): H160 D162 H292
• Binding residue (residue number reindexed from 1): H133 D135 H258
• 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

External links

• PDB: RCSB:6gpe, PDBe:6gpe, PDBj:6gpe
• PDBsum: 6gpe
• PubMed: 30498244
• UniProt: P76621|GLAH_ECOLI Glutarate 2-hydroxylase (Gene Name=glaH)