Crystallization (Comment) | Organism |
---|---|
structures of N-terminally truncated (aa 153-416 and aa 183-416) constructs and in complex with substrate RPS6. The JMJD5 active site contains a metal centre, which is octahedrally coordinated by an HXD..H motif, the 2-oxoglutarate oxalyl group and a water molecule, which is likely replaced by a dioxygen during catalysis | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
H321A | substitution of Fe2+-binding residue, significantly reduces 2-oxoglutarate turnover | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
N-oxalylglycine | - |
Homo sapiens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | - |
Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q8N371 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | JMJD5 catalyses stereoselective C-3 hydroxylation of arginine residues in sequences from human regulator of chromosome condensation domain-containing protein 1 (RCCD1) and ribosomal protein S6 (RPS6) | Homo sapiens | ? | - |
- |
|
[RCCD1]-L-arginine + 2-oxoglutarate + O2 | substrate i.e. regulator of chromosome condensation domain-containing protein 1 | Homo sapiens | [RCCD1]-(3R)-3-hydroxy-L-arginine + succinate + CO2 | - |
? | |
[RPS6]-L-arginine + 2-oxoglutarate + O2 | substrate i.e. ribosomal protein S6 | Homo sapiens | [RPS6]-(3R)-3-hydroxy-L-arginine + succinate + CO2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
JMJD5 | - |
Homo sapiens |
KDM8 | - |
Homo sapiens |