7OPO
RSK2 N-terminal kinase domain in complex with ORF45
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0004674 | molecular_function | protein serine/threonine kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006468 | biological_process | protein phosphorylation |
| E | 0004672 | molecular_function | protein kinase activity |
| E | 0004674 | molecular_function | protein serine/threonine kinase activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0006468 | biological_process | protein phosphorylation |
| G | 0004672 | molecular_function | protein kinase activity |
| G | 0004674 | molecular_function | protein serine/threonine kinase activity |
| G | 0005524 | molecular_function | ATP binding |
| G | 0006468 | biological_process | protein phosphorylation |
| I | 0004672 | molecular_function | protein kinase activity |
| I | 0004674 | molecular_function | protein serine/threonine kinase activity |
| I | 0005524 | molecular_function | ATP binding |
| I | 0006468 | biological_process | protein phosphorylation |
| K | 0004672 | molecular_function | protein kinase activity |
| K | 0004674 | molecular_function | protein serine/threonine kinase activity |
| K | 0005524 | molecular_function | ATP binding |
| K | 0006468 | biological_process | protein phosphorylation |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 27 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGSFGKVFlVkkisgsdarql.......YAMK |
| Chain | Residue | Details |
| A | LEU74-LYS100 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiYrDLKpeNILL |
| Chain | Residue | Details |
| A | ILE189-LEU201 |
| site_id | PS00284 |
| Number of Residues | 11 |
| Details | SERPIN Serpins signature. VEVNHPFIVkL |
| Chain | Residue | Details |
| A | VAL123-LEU133 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 54 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphoserine; by PDPK1","evidences":[{"source":"UniProtKB","id":"P18654","evidenceCode":"ECO:0000250"},{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphoserine; by host TBK1 and IKKE","evidences":[{"source":"PubMed","id":"11943871","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22787218","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
