Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue CA A 601 |
Chain | Residue |
A | ASP393 |
A | ASN395 |
A | ASP397 |
A | MET399 |
A | GLU404 |
A | HOH796 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue CA A 602 |
Chain | Residue |
A | SER449 |
A | GLU451 |
A | GLU454 |
A | ASP443 |
A | ASP445 |
A | SER447 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue CA A 603 |
Chain | Residue |
A | ASP479 |
A | ASP481 |
A | SER483 |
A | LYS485 |
A | GLU490 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue CA A 604 |
Chain | Residue |
A | ASP515 |
A | ASN517 |
A | ASP519 |
A | GLU521 |
A | GLU526 |
site_id | AC5 |
Number of Residues | 14 |
Details | binding site for residue AMP A 605 |
Chain | Residue |
A | GLY85 |
A | VAL90 |
A | ALA103 |
A | LYS105 |
A | GLU153 |
A | TYR155 |
A | LEU205 |
A | ASP219 |
A | HOH719 |
A | HOH729 |
A | HOH764 |
A | HOH775 |
A | HOH787 |
A | HOH797 |
Functional Information from PROSITE/UniProt
site_id | PS00018 |
Number of Residues | 13 |
Details | EF_HAND_1 EF-hand calcium-binding domain. DTNNDGMLDrdEL |
Chain | Residue | Details |
A | ASP393-LEU405 | |
A | ASP443-PHE455 | |
A | ASP479-LEU491 | |
A | ASP515-PHE527 | |
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGSFGEVLkCkdritqqe..........YAVK |
Chain | Residue | Details |
A | LEU82-LYS105 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDLKpeNILL |
Chain | Residue | Details |
A | ILE194-LEU206 | |