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 551 |
Chain | Residue |
A | ASP393 |
A | ASN395 |
A | ASP397 |
A | MET399 |
A | GLU404 |
A | HOH609 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 552 |
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 553 |
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 554 |
Chain | Residue |
A | ASP515 |
A | ASN517 |
A | ASP519 |
A | GLU521 |
A | GLU526 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE BK3 A 561 |
Chain | Residue |
A | LYS105 |
A | MET136 |
A | ILE150 |
A | GLU153 |
A | TYR155 |
A | GLU159 |
A | ASP219 |
A | HOH610 |
A | HOH630 |
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 | |