Protein family
Protein sequence
Protein function
Catalytic activity
EC number
EC number description
1.14.11.73
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor;
[protein]-arginine 3-hydroxylase
3.4.-.-
Hydrolases;
Acting on peptide bonds (peptidases);
;
| PDB | Resolution (Å) | PDB name |
|---|---|---|
| 3UYJ | 2.351 | Crystal structure of JMJD5 catalytic core domain in complex with nickle and alpha-KG |
| 4AAP | 2.6 | Crystal structure of JMJD5 domain of human Lysine-specific demethylase 8 (KDM8) in complex with N-oxalylglycine (NOG) |
| 4GAZ | 2.81 | Crystal Structure of a Jumonji Domain-containing Protein JMJD5 |
| 4GJY | 1.2492 | JMJD5 in complex with N-Oxalylglycine |
| 4GJZ | 1.0481 | JMJD5 in complex with 2-oxoglutarate |
| 4QU1 | 1.57 | Crystal structure of human JMJD5 jmj-c domain |
| 5FBJ | 2.42 | Complex structure of JMJD5 and substrate |
| 6AVS | 2.02 | Complex structure of JMJD5 and Symmetric Monomethyl-Arginine (MMA) |
| 6AX3 | 2.25 | Complex structure of JMJD5 and Symmetric Dimethyl-Arginine (SDMA) |
| 6F4M | 1.705 | Human JMJD5 in its apo form. |
| 6F4N | 2.541 | Human JMJD5 in complex with MN and 2OG. |
| 6F4O | 1.28 | Human JMJD5 in complex with Mn(II) and Succinate. |
| 6F4P | 1.45 | Human JMJD5 in complex with MN, NOG and RPS6 (129-144) (complex-1) |
| 6F4Q | 1.12 | Human JMJD5 (Q275C) in complex with Mn(II), NOG and RPS6-A138C (129-144) (complex-2) |
| 6F4R | 1.3 | Human JMJD5 (N308C) in complex with Mn(II), NOG and RCCD1 (139-143) (complex-3) |
| 6F4S | 1.461 | Human JMJD5 (N308C) in complex with Mn(II), 2OG and RCCD1 (139-143) (complex-4) |
| 6F4T | 1.22 | Human JMJD5 (W414C) in complex with Mn(II), NOG and RCCD1 (139-143) (complex-5) |
| 6I9L | 1.53 | JmjC domain-containing protein 5 (JMJD5) in complex with Mn and pyridine-2,4-dicarboxylic acid (2,4-PDCA) |
| 6I9M | 1.65 | JmjC domain-containing protein 5 (JMJD5) in complex with Mn and R-2-hydroxyglutarate |
| 6I9N | 1.361 | JmjC domain-containing protein 5 (JMJD5) in complex with Mn and L-2-hydroxyglutarate |
| 7DYT | 1.62 | Human JMJD5 in complex with MN and 5-((4-methoxybenzyl)amino)pyridine-2,4-dicarboxylic acid. |
| 7DYU | 1.72 | Human JMJD5 in complex with MN and 5-((4-phenylbutyl)amino)pyridine-2,4-dicarboxylic acid. |
| 7DYV | 1.92 | Human JMJD5 in complex with MN and 5-(benzylamino)pyridine-2,4-dicarboxylic acid. |
| 7DYW | 2.13 | Human JMJD5 in complex with MN and 5-((2-methoxybenzyl)amino)pyridine-2,4-dicarboxylic acid. |
| 7DYX | 2.27 | Human JMJD5 in complex with MN and 5-((2-cyclopropylbenzyl)amino)pyridine-2,4-dicarboxylic acid. |
| 7UQ3 | 1.49 | JmjC domain-containing protein 5 (JMJD5) in complex with Mn and (S)-2-(1-hydroxy-2,5-dioxopyrrolidin-3-yl)acetic acid |
| GO ontology
|
GO term | GO description |
|---|---|---|
| Biological Process | GO:0000086 | G2/M transition of mitotic cell cycle |
| Biological Process | GO:0032922 | circadian regulation of gene expression |
| Biological Process | GO:0045892 | negative regulation of DNA-templated transcription |
| Biological Process | GO:0045893 | positive regulation of DNA-templated transcription |
| Biological Process | GO:0031648 | protein destabilization |
| Biological Process | GO:0006508 | proteolysis |
| Molecular Function | GO:0004177 | aminopeptidase activity |
| Molecular Function | GO:0003682 | chromatin binding |
| Molecular Function | GO:0004175 | endopeptidase activity |
| Molecular Function | GO:0051864 | histone H3K36 demethylase activity |
| Molecular Function | GO:0046872 | metal ion binding |
| Molecular Function | GO:0035064 | methylated histone binding |
| Molecular Function | GO:0106157 | peptidyl-arginine 3-dioxygenase activity |
| Cellular Component | GO:0005694 | chromosome |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Location
|
ECO term
|
Pubmed |
|---|---|---|
| Chromosome | ECO:0000269 | PubMed:24981860 |
| Nucleus | ECO:0000269 | PubMed:20457893 |
| Nucleus | ECO:0000269 | PubMed:28982940 |