8SV9
Crystal structure of ULK1 kinase domain with inhibitor MR-2088
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 |
| A | 0010506 | biological_process | regulation of autophagy |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004674 | molecular_function | protein serine/threonine kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0010506 | biological_process | regulation of autophagy |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 25 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGHGAFAVVFkGrhraahdle.........VAVK |
| Chain | Residue | Details |
| A | ILE22-LYS46 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKpqNILL |
| Chain | Residue | Details |
| A | ILE134-LEU146 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
| Chain | Residue | Details |
| A | ASP138 | |
| B | ASP138 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | ILE22 | |
| B | ILE22 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000305|PubMed:20921139 |
| Chain | Residue | Details |
| A | LYS46 | |
| B | LYS46 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:O70405 |
| Chain | Residue | Details |
| A | LYS162 | |
| B | LYS162 |
