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 |
| 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 |
| C | 0010506 | biological_process | regulation of autophagy |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue 1FV A 301 |
| Chain | Residue |
| A | VAL15 |
| A | ASN89 |
| A | GLN135 |
| A | LEU138 |
| A | ASP158 |
| A | HOH403 |
| A | HOH406 |
| A | HIS17 |
| A | VAL23 |
| A | ALA37 |
| A | LYS39 |
| A | MET85 |
| A | GLU86 |
| A | TYR87 |
| A | CYS88 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 302 |
| Chain | Residue |
| A | SER10 |
| A | ASP13 |
| A | ARG25 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 303 |
| Chain | Residue |
| A | ASP6 |
| A | HIS28 |
| A | GLN30 |
| B | TYR72 |
| B | ASP73 |
| B | HOH415 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 304 |
| Chain | Residue |
| A | ARG238 |
| A | THR240 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 305 |
| Chain | Residue |
| A | ASP158 |
| A | GOL306 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 306 |
| Chain | Residue |
| A | LYS39 |
| A | ILE41 |
| A | GLU56 |
| A | ASP158 |
| A | EDO305 |
| A | HOH421 |
| A | HOH440 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 307 |
| site_id | AC8 |
| Number of Residues | 16 |
| Details | binding site for residue 1FV B 301 |
| Chain | Residue |
| B | VAL15 |
| B | HIS17 |
| B | GLY18 |
| B | VAL23 |
| B | ALA37 |
| B | MET85 |
| B | GLU86 |
| B | TYR87 |
| B | CYS88 |
| B | ASN89 |
| B | GLY90 |
| B | GLY91 |
| B | GLN135 |
| B | LEU138 |
| B | ASP158 |
| B | HOH427 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | binding site for residue EDO B 302 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 303 |
| Chain | Residue |
| B | GLN256 |
| B | EDO304 |
| C | GLU184 |
| C | MET187 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 304 |
| Chain | Residue |
| B | SER188 |
| B | TYR191 |
| B | EDO303 |
| C | SER188 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 305 |
| Chain | Residue |
| B | LYS55 |
| B | ARG163 |
| C | LYS55 |
| site_id | AD4 |
| Number of Residues | 13 |
| Details | binding site for residue 1FV C 301 |
| Chain | Residue |
| C | VAL15 |
| C | HIS17 |
| C | GLY18 |
| C | VAL23 |
| C | ALA37 |
| C | MET85 |
| C | GLU86 |
| C | TYR87 |
| C | CYS88 |
| C | ASN89 |
| C | GLY91 |
| C | LEU138 |
| C | ASP158 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO C 302 |
| Chain | Residue |
| B | PRO237 |
| B | GLU239 |
| C | SER241 |
| C | PRO242 |
| C | TYR243 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 25 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGHGAFAVVFrGrhrqktdwe.........VAIK |
| Chain | Residue | Details |
| A | VAL15-LYS39 | |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKpqNILL |
| Chain | Residue | Details |
| A | ILE127-LEU139 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 262 |
| Details | Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
