6HL8

Crystal Structure of the CsiD Glutarate Hydroxylase in complex with Glutarate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005506	molecular_function	iron ion binding
A	0008198	molecular_function	ferrous iron binding
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
B	0005506	molecular_function	iron ion binding
B	0008198	molecular_function	ferrous iron binding
B	0019477	biological_process	L-lysine catabolic process
B	0032991	cellular_component	protein-containing complex
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
B	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
B	0051213	molecular_function	dioxygenase activity
B	0090549	biological_process	response to carbon starvation
B	0106343	molecular_function	glutarate dioxygenase activity

Functional Information from PDB Data

site_id	AC2
Number of Residues	8
Details	binding site for residue GUA A 402

site_id	AC4
Number of Residues	8
Details	binding site for residue GUA B 402

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:11910018, ECO:0000269\|PubMed:30498244, ECO:0000312\|PDB:1JR7, ECO:0000312\|PDB:6GPE