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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005506	molecular_function	iron ion binding
A	0008198	molecular_function	ferrous iron binding
A	0016491	molecular_function	oxidoreductase activity
A	0016706	molecular_function	2-oxoglutarate-dependent dioxygenase activity
A	0019477	biological_process	L-lysine catabolic process
A	0032991	cellular_component	protein-containing complex
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	0050498	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, with 2-oxoglutarate as one donor, and the other dehydrogenated
A	0051213	molecular_function	dioxygenase activity
A	0090549	biological_process	response to carbon starvation
A	0106343	molecular_function	glutarate dioxygenase activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11910018","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30498244","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1JR7","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"6GPE","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

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