Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
B | 0004672 | molecular_function | protein kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006468 | biological_process | protein phosphorylation |
C | 0004672 | molecular_function | protein kinase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0006468 | biological_process | protein phosphorylation |
D | 0004672 | molecular_function | protein kinase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | binding site for residue EJP A 1100 |
Chain | Residue |
A | PHE28 |
A | LEU157 |
A | LEU159 |
A | SER161 |
A | MET67 |
A | LEU70 |
A | VAL75 |
A | VAL76 |
A | LEU90 |
A | MET92 |
A | VAL134 |
A | ASP156 |
site_id | AC2 |
Number of Residues | 11 |
Details | binding site for residue EJP B 1100 |
Chain | Residue |
B | VAL31 |
B | LYS45 |
B | VAL75 |
B | VAL76 |
B | LEU90 |
B | MET92 |
B | ILE154 |
B | ALA155 |
B | ASP156 |
B | LEU157 |
B | LEU159 |
site_id | AC3 |
Number of Residues | 14 |
Details | binding site for residue EJP C 1100 |
Chain | Residue |
C | VAL31 |
C | ILE43 |
C | LYS45 |
C | MET67 |
C | LEU70 |
C | VAL75 |
C | VAL76 |
C | LEU78 |
C | LEU90 |
C | MET92 |
C | ALA155 |
C | ASP156 |
C | LEU157 |
C | PHE162 |
site_id | AC4 |
Number of Residues | 12 |
Details | binding site for residue EJP D 1100 |
Chain | Residue |
D | VAL31 |
D | ILE43 |
D | LYS45 |
D | MET67 |
D | VAL76 |
D | LEU90 |
D | MET92 |
D | ALA155 |
D | ASP156 |
D | LEU157 |
D | SER161 |
D | PHE162 |
Functional Information from PROSITE/UniProt
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHkDLKpeNILV |
Chain | Residue | Details |
A | VAL134-VAL146 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP138 | |
B | ASP138 | |
C | ASP138 | |
D | ASP138 | |
Chain | Residue | Details |
A | LEU23 | |
A | LYS45 | |
B | LEU23 | |
B | LYS45 | |
C | LEU23 | |
C | LYS45 | |
D | LEU23 | |
D | LYS45 | |
Chain | Residue | Details |
A | SER6 | |
B | SER6 | |
C | SER6 | |
D | SER6 | |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000255 |
Chain | Residue | Details |
A | SER20 | |
B | SER20 | |
C | SER20 | |
D | SER20 | |
Chain | Residue | Details |
A | SER25 | |
B | SER25 | |
C | SER25 | |
D | SER25 | |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine; by RIPK3 and autocatalysis => ECO:0000255 |
Chain | Residue | Details |
A | SER161 | |
B | SER161 | |
C | SER161 | |
D | SER161 | |
Chain | Residue | Details |
A | SER166 | |
B | SER166 | |
C | SER166 | |
D | SER166 | |