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 |
D | 0004672 | molecular_function | protein kinase activity |
D | 0004674 | molecular_function | protein serine/threonine kinase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0006468 | biological_process | protein phosphorylation |
D | 0010506 | biological_process | regulation of autophagy |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue GOL A 301 |
Chain | Residue |
A | HIS130 |
A | ILE134 |
A | ILE135 |
A | LEU172 |
A | PHE269 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue GOL A 302 |
Chain | Residue |
A | HOH462 |
B | SER131 |
B | GLY133 |
A | HIS130 |
A | SER131 |
A | GLY133 |
A | LEU172 |
site_id | AC3 |
Number of Residues | 13 |
Details | binding site for residue 3RJ A 303 |
Chain | Residue |
A | ILE22 |
A | ALA44 |
A | GLU93 |
A | TYR94 |
A | CYS95 |
A | ASN96 |
A | GLY98 |
A | ASP102 |
A | GLN142 |
A | ASN143 |
A | LEU145 |
A | HOH425 |
A | HOH460 |
site_id | AC4 |
Number of Residues | 10 |
Details | binding site for residue 3RJ B 401 |
Chain | Residue |
B | ILE22 |
B | ALA44 |
B | GLU93 |
B | TYR94 |
B | CYS95 |
B | GLY98 |
B | ASP99 |
B | GLN142 |
B | ASN143 |
B | LEU145 |
site_id | AC5 |
Number of Residues | 11 |
Details | binding site for residue 3RJ C 401 |
Chain | Residue |
C | ILE22 |
C | ALA44 |
C | GLU93 |
C | TYR94 |
C | CYS95 |
C | ASN96 |
C | GLY98 |
C | ASP102 |
C | GLN142 |
C | ASN143 |
C | LEU145 |
site_id | AC6 |
Number of Residues | 12 |
Details | binding site for residue 3RJ D 401 |
Chain | Residue |
D | ILE22 |
D | ALA44 |
D | LYS46 |
D | GLU93 |
D | TYR94 |
D | CYS95 |
D | GLY98 |
D | ASP99 |
D | GLN142 |
D | ASN143 |
D | LEU145 |
D | HOH539 |
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
Chain | Residue | Details |
A | ASP138 | |
B | ASP138 | |
C | ASP138 | |
D | ASP138 | |
Chain | Residue | Details |
A | ILE22 | |
B | ILE22 | |
C | ILE22 | |
D | ILE22 | |
Chain | Residue | Details |
A | LYS46 | |
B | LYS46 | |
C | LYS46 | |
D | LYS46 | |
Chain | Residue | Details |
A | LYS162 | |
B | LYS162 | |
C | LYS162 | |
D | LYS162 | |