8K62
Crystal structure of ALKBH1 and 13h complex.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000049 | molecular_function | tRNA binding |
| A | 0000791 | cellular_component | euchromatin |
| A | 0002101 | biological_process | tRNA wobble cytosine modification |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006281 | biological_process | DNA repair |
| A | 0006446 | biological_process | regulation of translational initiation |
| A | 0006448 | biological_process | regulation of translational elongation |
| A | 0008198 | molecular_function | ferrous iron binding |
| A | 0035513 | biological_process | oxidative RNA demethylation |
| A | 0035515 | molecular_function | oxidative RNA demethylase activity |
| A | 0035516 | molecular_function | broad specificity oxidative DNA demethylase activity |
| A | 0042056 | molecular_function | chemoattractant activity |
| A | 0050918 | biological_process | positive chemotaxis |
| A | 0070129 | biological_process | regulation of mitochondrial translation |
| A | 0140078 | molecular_function | class I DNA-(apurinic or apyrimidinic site) endonuclease activity |
| A | 0141131 | molecular_function | DNA N6-methyladenine demethylase activity |
| A | 0141137 | biological_process | positive regulation of gene expression, epigenetic |
| A | 0160290 | molecular_function | 2-oxoglutarate-dependent tRNA 5-methylcytidine formyltransferase activity |
| A | 1990983 | biological_process | regulation of translational initiation by tRNA modification |
| A | 1990984 | molecular_function | tRNA demethylase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 139 |
| 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 | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q6NS38","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q96Q83","evidenceCode":"ECO:0000250"}]} |
| 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":"19959401","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"27745969","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00805","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Site: {"description":"Secondary catalytic residue forming the imine linkage with DNA","evidences":[{"source":"PubMed","id":"23577621","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
