1HKX
Crystal structure of calcium/calmodulin-dependent protein kinase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004683 | molecular_function | calmodulin-dependent protein kinase activity |
| A | 0005516 | molecular_function | calmodulin binding |
| A | 0006468 | biological_process | protein phosphorylation |
| B | 0004683 | molecular_function | calmodulin-dependent protein kinase activity |
| B | 0005516 | molecular_function | calmodulin binding |
| B | 0006468 | biological_process | protein phosphorylation |
| C | 0004683 | molecular_function | calmodulin-dependent protein kinase activity |
| C | 0005516 | molecular_function | calmodulin binding |
| C | 0006468 | biological_process | protein phosphorylation |
| D | 0004683 | molecular_function | calmodulin-dependent protein kinase activity |
| D | 0005516 | molecular_function | calmodulin binding |
| D | 0006468 | biological_process | protein phosphorylation |
| E | 0004683 | molecular_function | calmodulin-dependent protein kinase activity |
| E | 0005516 | molecular_function | calmodulin binding |
| E | 0006468 | biological_process | protein phosphorylation |
| F | 0004683 | molecular_function | calmodulin-dependent protein kinase activity |
| F | 0005516 | molecular_function | calmodulin binding |
| F | 0006468 | biological_process | protein phosphorylation |
| G | 0004683 | molecular_function | calmodulin-dependent protein kinase activity |
| G | 0005516 | molecular_function | calmodulin binding |
| G | 0006468 | biological_process | protein phosphorylation |
| H | 0004683 | molecular_function | calmodulin-dependent protein kinase activity |
| H | 0005516 | molecular_function | calmodulin binding |
| H | 0006468 | biological_process | protein phosphorylation |
| I | 0004683 | molecular_function | calmodulin-dependent protein kinase activity |
| I | 0005516 | molecular_function | calmodulin binding |
| I | 0006468 | biological_process | protein phosphorylation |
| J | 0004683 | molecular_function | calmodulin-dependent protein kinase activity |
| J | 0005516 | molecular_function | calmodulin binding |
| J | 0006468 | biological_process | protein phosphorylation |
| K | 0004683 | molecular_function | calmodulin-dependent protein kinase activity |
| K | 0005516 | molecular_function | calmodulin binding |
| K | 0006468 | biological_process | protein phosphorylation |
| L | 0004683 | molecular_function | calmodulin-dependent protein kinase activity |
| L | 0005516 | molecular_function | calmodulin binding |
| L | 0006468 | biological_process | protein phosphorylation |
| M | 0004683 | molecular_function | calmodulin-dependent protein kinase activity |
| M | 0005516 | molecular_function | calmodulin binding |
| M | 0006468 | biological_process | protein phosphorylation |
| N | 0004683 | molecular_function | calmodulin-dependent protein kinase activity |
| N | 0005516 | molecular_function | calmodulin binding |
| N | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A1476 |
| Chain | Residue |
| A | ILE361 |
| A | TYR369 |
| A | ARG453 |
| A | PHE467 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B1475 |
| Chain | Residue |
| B | ILE361 |
| B | TYR369 |
| B | ARG453 |
| B | PHE467 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL C1475 |
| Chain | Residue |
| C | TYR369 |
| C | ARG453 |
| C | PHE467 |
| C | ILE361 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL D1475 |
| Chain | Residue |
| D | ILE361 |
| D | TYR369 |
| D | ARG453 |
| D | PHE467 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL E1475 |
| Chain | Residue |
| E | ILE361 |
| E | TYR369 |
| E | ARG453 |
| E | PHE467 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL F1475 |
| Chain | Residue |
| F | ILE361 |
| F | TYR369 |
| F | PHE467 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL G1475 |
| Chain | Residue |
| G | ILE361 |
| G | TYR369 |
| G | ARG453 |
| G | PHE467 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL H1475 |
| Chain | Residue |
| H | ILE361 |
| H | TYR369 |
| H | ARG453 |
| H | PHE467 |
| H | ARG469 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL I1475 |
| Chain | Residue |
| I | ILE361 |
| I | PHE467 |
| I | ARG469 |
| I | VAL475 |
| I | HOH2002 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL J1475 |
| Chain | Residue |
| J | ILE361 |
| J | TYR369 |
| J | ARG453 |
| J | PHE467 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL K1475 |
| Chain | Residue |
| K | TYR369 |
| K | ARG453 |
| K | PHE467 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL L1475 |
| Chain | Residue |
| L | ILE361 |
| L | ARG453 |
| L | PHE467 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL M1475 |
| Chain | Residue |
| M | ILE361 |
| M | TYR369 |
| M | ARG453 |
| M | PHE467 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL N1475 |
| Chain | Residue |
| N | ILE361 |
| N | TYR369 |
| N | ARG453 |
| N | PHE467 |
| N | VAL475 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE DTT A1475 |
| Chain | Residue |
| A | GLU339 |
| A | ASP342 |
| A | ARG346 |
| A | ASP424 |
| A | TBR2000 |
| G | HIS456 |
| G | ARG458 |
| site_id | BC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE TBR A2000 |
| Chain | Residue |
| A | THR343 |
| A | ARG346 |
| A | LEU421 |
| A | GLY423 |
| A | DTT1475 |
| B | HIS456 |
| G | HIS456 |
| H | THR343 |
| H | ARG346 |
| H | LEU421 |
| H | GLY423 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 28 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:21183079 |
| Chain | Residue | Details |
| A | THR336 | |
| E | THR337 | |
| F | THR336 | |
| F | THR337 | |
| G | THR336 | |
| G | THR337 | |
| H | THR336 | |
| H | THR337 | |
| I | THR336 | |
| I | THR337 | |
| J | THR336 | |
| A | THR337 | |
| J | THR337 | |
| K | THR336 | |
| K | THR337 | |
| L | THR336 | |
| L | THR337 | |
| M | THR336 | |
| M | THR337 | |
| N | THR336 | |
| N | THR337 | |
| B | THR336 | |
| B | THR337 | |
| C | THR336 | |
| C | THR337 | |
| D | THR336 | |
| D | THR337 | |
| E | THR336 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079 |
| Chain | Residue | Details |
| A | SER404 | |
| J | SER404 | |
| K | SER404 | |
| L | SER404 | |
| M | SER404 | |
| N | SER404 | |
| B | SER404 | |
| C | SER404 | |
| D | SER404 | |
| E | SER404 | |
| F | SER404 | |
| G | SER404 | |
| H | SER404 | |
| I | SER404 |
