Structure of PDB 8cdf Chain A

Receptor sequence
>8cdfA (length=299) Species: 562 (Escherichia coli) [Search protein sequence]
QYSGFTLTPSAQSPRLLELTFTEQTTKQFLEQVAEWPVQALEYKSFLRFR
VAKILDDLCANQLQPLLLKTLLNRAEGALLINAVGVDDVKQADEMVKLAT
AVAHLIGRSNFDAMSGQYYARFVVKNYLRQPHRVMELHNDGTYVEEITDY
VLMMKIDEQNMQGGNSLLLHLDDWEHLDNYFRHPLARRPMRFAAPPSKDV
FHPVFDVDQQGRPVMRYIDQFVQPKDFEEGVWLSELSDAIETSKGILSVP
VPVGKFLLINNLFWLHGRDRFTPHPDLRRELMRQRGYFAYASNHYQTHQ
3D structure
PDB8cdf 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
ChainA
Resolution1.77 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 H138 D140 H266
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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Cellular Component
External links
PDB RCSB:8cdf, PDBe:8cdf, PDBj:8cdf
PDBsum8cdf
PubMed
UniProtP76621|GLAH_ECOLI Glutarate 2-hydroxylase (Gene Name=glaH)

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