4NHX
Crystal structure of human OGFOD1, 2-oxoglutarate and iron-dependent oxygenase domain containing 1, in complex with N-oxalylglycine (NOG)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006449 | biological_process | regulation of translational termination |
| A | 0008283 | biological_process | cell population proliferation |
| A | 0010494 | cellular_component | cytoplasmic stress granule |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016705 | molecular_function | oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen |
| A | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| A | 0018126 | biological_process | protein hydroxylation |
| A | 0019511 | biological_process | peptidyl-proline hydroxylation |
| A | 0031418 | molecular_function | L-ascorbic acid binding |
| A | 0031543 | molecular_function | peptidyl-proline dioxygenase activity |
| A | 0031544 | molecular_function | peptidyl-proline 3-dioxygenase activity |
| A | 0034063 | biological_process | stress granule assembly |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051213 | molecular_function | dioxygenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 601 |
| Chain | Residue |
| A | HIS155 |
| A | ASP157 |
| A | HIS218 |
| A | OGA603 |
| A | HOH841 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 602 |
| Chain | Residue |
| A | ARG108 |
| A | ASP506 |
| A | THR509 |
| A | HOH944 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE OGA A 603 |
| Chain | Residue |
| A | LEU152 |
| A | HIS155 |
| A | ASP157 |
| A | TYR169 |
| A | HIS218 |
| A | VAL220 |
| A | ARG230 |
| A | MN601 |
| A | GOL604 |
| A | HOH838 |
| A | HOH841 |
| A | HOH843 |
| A | HOH844 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 604 |
| Chain | Residue |
| A | HIS155 |
| A | ARG162 |
| A | TRP236 |
| A | OGA603 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 105 |
| Details | Domain: {"description":"Fe2OG dioxygenase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00805","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00805","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"25728928","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25728928","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00805","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"25728928","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
