Structure of PDB 8cdf Chain A Binding Site BS01

Receptor Information

>8cdf Chain A (length=299) Species: 562 (Escherichia coli)

QYSGFTLTPSAQSPRLLELTFTEQTTKQFLEQVAEWPVQALEYKSFLRFR
VAKILDDLCANQLQPLLLKTLLNRAEGALLINAVGVDDVKQADEMVKLAT
AVAHLIGRSNFDAMSGQYYARFVVKNYLRQPHRVMELHNDGTYVEEITDY
VLMMKIDEQNMQGGNSLLLHLDDWEHLDNYFRHPLARRPMRFAAPPSKDV
FHPVFDVDQQGRPVMRYIDQFVQPKDFEEGVWLSELSDAIETSKGILSVP
VPVGKFLLINNLFWLHGRDRFTPHPDLRRELMRQRGYFAYASNHYQTHQ

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: 8cdf Chain A Residue 401

Receptor-Ligand Complex Structure

Structure summary

• PDB: 8cdf Structure of glutarate hydroxylase (GlaH) from Escherichia coli at a resolution of 1.8 angstrom obtained as a contaminant during routine use of E. coli as an expression host
• Resolution: 1.77 Å
• Binding residue (original residue number in PDB): H160 D162 H292
• Binding residue (residue number reindexed from 1): H138 D140 H266
• 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:8cdf, PDBe:8cdf, PDBj:8cdf
• PDBsum: 8cdf
• UniProt: P76621|GLAH_ECOLI Glutarate 2-hydroxylase (Gene Name=glaH)