Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004675 | molecular_function | transmembrane receptor protein serine/threonine kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
A | 0007178 | biological_process | cell surface receptor protein serine/threonine kinase signaling pathway |
A | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | binding site for residue STU A 601 |
Chain | Residue |
A | VAL250 |
A | ASN332 |
A | SER383 |
A | LEU386 |
A | CYS396 |
A | ASP397 |
A | GLY251 |
A | VAL258 |
A | ALA275 |
A | LYS277 |
A | ALA326 |
A | PHE327 |
A | HIS328 |
A | GLY331 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 28 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. VGKGRFAEVYkAklkqntseqfet......VAVK |
Chain | Residue | Details |
A | VAL250-LYS277 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDLKssNILV |
Chain | Residue | Details |
A | ILE375-VAL387 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP379 | |
Chain | Residue | Details |
A | VAL250 | |
A | LYS277 | |
Chain | Residue | Details |
A | SER409 | |
Chain | Residue | Details |
A | SER548 | |