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 PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE2 A 501 |
| Chain | Residue |
| A | HIS160 |
| A | ASP162 |
| A | HIS292 |
| A | HOH787 |
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 |
