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 | 5 |
Details | BINDING SITE FOR RESIDUE CA A 601 |
Chain | Residue |
A | ASP515 |
A | ASN517 |
A | ASP519 |
A | GLU521 |
A | GLU526 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 602 |
Chain | Residue |
A | GLU404 |
A | HOH547 |
A | ASP393 |
A | ASN395 |
A | ASP397 |
A | MET399 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 603 |
Chain | Residue |
A | ASP443 |
A | ASP445 |
A | SER447 |
A | SER449 |
A | GLU451 |
A | GLU454 |
site_id | AC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE ANP A 610 |
Chain | Residue |
A | HOH37 |
A | HOH47 |
A | GLY83 |
A | GLY85 |
A | SER86 |
A | PHE87 |
A | GLY88 |
A | VAL90 |
A | LYS105 |
A | GLU153 |
A | TYR155 |
A | ASP219 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 1 |
Chain | Residue |
A | GLU101 |
A | TYR102 |
A | GLU153 |
A | LEU154 |
A | THR377 |
A | THR378 |
A | LEU379 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 539 |
Chain | Residue |
A | TYR76 |
A | ASP95 |
A | PHE139 |
A | GLU140 |
A | LYS375 |
A | MET477 |
A | HOH611 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 540 |
Chain | Residue |
A | GLN325 |
A | ARG468 |
A | VAL528 |
A | GOL546 |
A | HOH579 |
A | HOH589 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CA A 541 |
Chain | Residue |
A | ASP481 |
A | GLY484 |
A | ILE486 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 542 |
Chain | Residue |
A | HIS316 |
A | PRO317 |
A | SER318 |
A | LYS476 |
A | GLY482 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SRT A 543 |
Chain | Residue |
A | TYR291 |
A | PHE293 |
A | ARG310 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 544 |
Chain | Residue |
A | HIS196 |
A | ARG197 |
A | ASP198 |
A | ASP219 |
A | GLY221 |
A | SER223 |
site_id | BC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PO4 A 545 |
Chain | Residue |
A | LYS166 |
A | LYS209 |
site_id | BC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 546 |
Chain | Residue |
A | LYS254 |
A | SER318 |
A | ARG320 |
A | THR322 |
A | GLN325 |
A | ASN525 |
A | GOL540 |
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 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASP198 | |
A | GLU202 | |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASP198 | |
A | LYS200 | |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | THR238 | |
A | ASP198 | |
A | LYS200 | |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASP198 | |
A | LYS200 | |
A | ASN203 | |