5NFN
JMJD7 IN COMPLEX WITH MN AND 2OG IN THE H32 FORM
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 | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| A | 0018126 | biological_process | protein hydroxylation |
| A | 0035064 | molecular_function | methylated histone binding |
| 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 | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| B | 0018126 | biological_process | protein hydroxylation |
| B | 0035064 | molecular_function | methylated histone binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0106155 | molecular_function | peptidyl-lysine 3-dioxygenase activity |
| C | 0004175 | molecular_function | endopeptidase activity |
| C | 0004177 | molecular_function | aminopeptidase activity |
| C | 0004497 | molecular_function | monooxygenase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006508 | biological_process | proteolysis |
| C | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| C | 0018126 | biological_process | protein hydroxylation |
| C | 0035064 | molecular_function | methylated histone binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0106155 | molecular_function | peptidyl-lysine 3-dioxygenase activity |
| D | 0004175 | molecular_function | endopeptidase activity |
| D | 0004177 | molecular_function | aminopeptidase activity |
| D | 0004497 | molecular_function | monooxygenase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005634 | cellular_component | nucleus |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0006508 | biological_process | proteolysis |
| D | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| D | 0018126 | biological_process | protein hydroxylation |
| D | 0035064 | molecular_function | methylated histone binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 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 | HOH632 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue AKG A 502 |
| Chain | Residue |
| A | ASP180 |
| A | ASN184 |
| A | TYR186 |
| A | LYS193 |
| A | HIS277 |
| A | VAL279 |
| A | TRP291 |
| A | MN501 |
| A | HOH601 |
| A | HOH632 |
| A | TYR127 |
| A | TRP167 |
| A | THR175 |
| A | HIS178 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue NO3 A 503 |
| Chain | Residue |
| A | ASP162 |
| A | ASP293 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue NO3 A 504 |
| Chain | Residue |
| A | GLU12 |
| A | GLU15 |
| B | SER308 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue MN B 501 |
| Chain | Residue |
| B | HIS178 |
| B | ASP180 |
| B | HIS277 |
| B | AKG502 |
| B | HOH637 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | binding site for residue AKG B 502 |
| Chain | Residue |
| B | TYR127 |
| B | TRP167 |
| B | THR175 |
| B | HIS178 |
| B | ASP180 |
| B | ASN184 |
| B | TYR186 |
| B | LYS193 |
| B | HIS277 |
| B | VAL279 |
| B | ASN289 |
| B | TRP291 |
| B | MN501 |
| B | HOH637 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| B | ASP162 |
| B | ASP293 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue GOL B 504 |
| Chain | Residue |
| B | MET232 |
| B | GLU233 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 505 |
| Chain | Residue |
| B | SER254 |
| B | ALA256 |
| B | GLN257 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue MN C 501 |
| Chain | Residue |
| C | HIS178 |
| C | ASP180 |
| C | HIS277 |
| C | HOH622 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue NO3 C 502 |
| Chain | Residue |
| C | THR37 |
| C | PRO38 |
| C | LEU39 |
| C | HOH635 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue MN D 501 |
| Chain | Residue |
| D | HIS178 |
| D | ASP180 |
| D | HIS277 |
| D | AKG502 |
| D | HOH625 |
| site_id | AD4 |
| Number of Residues | 13 |
| Details | binding site for residue AKG D 502 |
| Chain | Residue |
| D | TYR127 |
| D | TRP167 |
| D | THR175 |
| D | HIS178 |
| D | ASP180 |
| D | ASN184 |
| D | TYR186 |
| D | LYS193 |
| D | HIS277 |
| D | VAL279 |
| D | ASN289 |
| D | MN501 |
| D | HOH625 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue GOL D 503 |
| Chain | Residue |
| D | GLU183 |
| D | ASP293 |
| D | MET294 |
| D | GLU295 |
| D | ASP297 |
| D | LYS299 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue NO3 D 504 |
| Chain | Residue |
| B | ASP88 |
| D | GLN121 |
| D | HIS122 |
| D | GLY124 |
| D | HOH610 |
| site_id | AD7 |
| Number of Residues | 2 |
| Details | binding site for residue NO3 D 505 |
| Chain | Residue |
| D | LEU143 |
| D | SER148 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue NO3 D 506 |
| Chain | Residue |
| D | SER254 |
| D | ALA256 |
| D | HOH607 |
| D | HOH644 |
| site_id | AD9 |
| Number of Residues | 3 |
| Details | binding site for residue NO3 D 507 |
| Chain | Residue |
| D | ARG203 |
| D | ASP307 |
| D | HOH641 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:29915238 |
| Chain | Residue | Details |
| A | HIS178 | |
| D | HIS178 | |
| D | ASP180 | |
| D | HIS277 | |
| A | ASP180 | |
| A | HIS277 | |
| B | HIS178 | |
| B | ASP180 | |
| B | HIS277 | |
| C | HIS178 | |
| C | ASP180 | |
| C | HIS277 |
