Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004175 | molecular_function | endopeptidase activity |
| A | 0004177 | molecular_function | aminopeptidase activity |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006508 | biological_process | proteolysis |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0017185 | biological_process | peptidyl-lysine hydroxylation |
| A | 0018126 | biological_process | protein hydroxylation |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0106155 | molecular_function | peptidyl-lysine 3-dioxygenase activity |
| B | 0004175 | molecular_function | endopeptidase activity |
| B | 0004177 | molecular_function | aminopeptidase activity |
| B | 0004497 | molecular_function | monooxygenase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006508 | biological_process | proteolysis |
| B | 0008233 | molecular_function | peptidase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0017185 | biological_process | peptidyl-lysine hydroxylation |
| B | 0018126 | biological_process | protein hydroxylation |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0106155 | molecular_function | peptidyl-lysine 3-dioxygenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue MN A 501 |
| Chain | Residue |
| A | HIS178 |
| A | ASP180 |
| A | HIS277 |
| A | AKG502 |
| A | HOH680 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue AKG A 502 |
| Chain | Residue |
| A | ASN184 |
| A | TYR186 |
| A | LYS193 |
| A | HIS277 |
| A | VAL279 |
| A | ASN289 |
| A | TRP291 |
| A | MN501 |
| A | HOH656 |
| A | HOH680 |
| A | TYR127 |
| A | THR175 |
| A | HIS178 |
| A | ASP180 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | ALA93 |
| A | VAL94 |
| A | ARG95 |
| A | GLY118 |
| A | SER176 |
| A | ILE238 |
| A | PRO239 |
| A | HOH661 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | LYS179 |
| A | ARG203 |
| A | TYR208 |
| A | PRO236 |
| A | ASP307 |
| A | LYS311 |
| A | HOH718 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 505 |
| Chain | Residue |
| A | TYR300 |
| A | HOH666 |
| B | SER-1 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue NO3 A 506 |
| Chain | Residue |
| A | SER254 |
| A | GLN255 |
| A | ALA256 |
| A | GLN257 |
| A | HOH606 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue MN B 501 |
| Chain | Residue |
| B | HIS178 |
| B | ASP180 |
| B | HIS277 |
| B | AKG502 |
| B | HOH680 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | binding site for residue AKG B 502 |
| Chain | Residue |
| B | TYR127 |
| B | THR175 |
| B | HIS178 |
| B | ASP180 |
| B | ASN184 |
| B | TYR186 |
| B | LYS193 |
| B | HIS277 |
| B | VAL279 |
| B | ASN289 |
| B | TRP291 |
| B | MN501 |
| B | HOH645 |
| B | HOH680 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| A | CYS47 |
| B | TYR42 |
| B | GLU183 |
| B | MET294 |
| B | GLU295 |
| B | ASP297 |
| B | LYS299 |
| B | HOH618 |
| B | HOH632 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 504 |
| Chain | Residue |
| B | ARG203 |
| B | TYR208 |
| B | PRO236 |
| B | ASP307 |
| B | LYS311 |
| site_id | AD2 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 505 |
| Chain | Residue |
| B | ALA93 |
| B | VAL94 |
| B | ARG95 |
| B | SER176 |
| B | ILE238 |
| B | PRO239 |
| B | ASP241 |
| B | HOH656 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue NO3 B 506 |
| Chain | Residue |
| B | GLU104 |
| B | ARG105 |
| B | GLN217 |
| B | LEU218 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 358 |
| Details | Domain: {"description":"JmjC","evidences":[{"source":"PROSITE-ProRule","id":"PRU00538","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29915238","evidenceCode":"ECO:0000269"}]} |
