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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | binding site for residue G8B A 401 |
Chain | Residue |
A | ALA83 |
A | ASP200 |
A | GOL404 |
A | HOH522 |
A | HOH533 |
A | HOH540 |
A | LYS85 |
A | VAL110 |
A | ASP133 |
A | TYR134 |
A | VAL135 |
A | PRO136 |
A | ARG141 |
A | LEU188 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue MLI A 402 |
Chain | Residue |
A | ARG96 |
A | ARG180 |
A | LYS205 |
A | ASN213 |
A | VAL214 |
A | HOH546 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue GOL A 403 |
Chain | Residue |
A | TYR56 |
A | THR59 |
A | TYR71 |
A | LYS86 |
A | ASN129 |
B | GLU290 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue GOL A 404 |
Chain | Residue |
A | TYR140 |
A | ARG141 |
A | GLN185 |
A | G8B401 |
A | HOH530 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue GOL A 405 |
Chain | Residue |
A | PTR216 |
A | SER219 |
A | ARG220 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue CL A 406 |
Chain | Residue |
A | ARG167 |
A | GLU366 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue DMS A 407 |
Chain | Residue |
A | TYR146 |
A | TYR157 |
A | TYR161 |
site_id | AC8 |
Number of Residues | 12 |
Details | binding site for residue G8B B 401 |
Chain | Residue |
B | ALA83 |
B | LYS85 |
B | VAL110 |
B | ASP133 |
B | TYR134 |
B | VAL135 |
B | PRO136 |
B | ARG141 |
B | LEU188 |
B | ASP200 |
B | HOH537 |
B | HOH559 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue MLI B 402 |
Chain | Residue |
B | ARG96 |
B | ARG180 |
B | LYS205 |
B | ASN213 |
B | VAL214 |
B | HOH536 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue GOL B 403 |
Chain | Residue |
B | TYR56 |
B | LYS86 |
B | ASN129 |
site_id | AD2 |
Number of Residues | 2 |
Details | binding site for residue CL B 404 |
Chain | Residue |
B | HIS106 |
B | GLU366 |
site_id | AD3 |
Number of Residues | 3 |
Details | binding site for residue DMS B 405 |
Chain | Residue |
A | PRO51 |
B | TYR157 |
B | TYR161 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 25 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGNGSFGVVYqAklcdsgelv.........AIKK |
Chain | Residue | Details |
A | ILE62-LYS86 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IcHrDIKpqNLLL |
Chain | Residue | Details |
A | ILE177-LEU189 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | ASP181 | |
B | ASP181 | |
Chain | Residue | Details |
A | ILE62 | |
B | ILE62 | |
Chain | Residue | Details |
A | LYS85 | |
B | LYS85 | |
Chain | Residue | Details |
A | PTR216 | |
B | PTR216 | |