2W2C
STRUCTURE OF THE TETRADECAMERIC OLIGOMERISATION DOMAIN OF CALCIUM- CALMODULIN DEPENDENT PROTEIN KINASE II DELTA
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 | 6 |
| Details | BINDING SITE FOR RESIDUE ACT A 632 |
| Chain | Residue |
| A | ILE361 |
| A | TYR369 |
| A | ARG433 |
| A | ARG453 |
| A | PHE467 |
| A | ARG469 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT B 632 |
| Chain | Residue |
| B | ARG453 |
| B | PHE467 |
| B | ARG469 |
| B | ILE361 |
| B | TYR369 |
| B | ARG433 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT C 632 |
| Chain | Residue |
| C | ILE361 |
| C | TYR369 |
| C | ARG433 |
| C | ARG453 |
| C | PHE467 |
| C | ARG469 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT D 632 |
| Chain | Residue |
| D | ILE361 |
| D | TYR369 |
| D | ARG433 |
| D | ARG453 |
| D | PHE467 |
| D | ARG469 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT E 632 |
| Chain | Residue |
| E | ILE361 |
| E | TYR369 |
| E | ARG453 |
| E | PHE467 |
| E | ARG469 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT F 632 |
| Chain | Residue |
| F | ILE361 |
| F | TYR369 |
| F | ARG453 |
| F | PHE467 |
| F | ARG469 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT G 632 |
| Chain | Residue |
| G | ILE361 |
| G | TYR369 |
| G | ARG433 |
| G | ARG453 |
| G | PHE467 |
| G | ARG469 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT H 632 |
| Chain | Residue |
| H | ILE361 |
| H | TYR369 |
| H | ARG453 |
| H | PHE467 |
| H | ARG469 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT I 632 |
| Chain | Residue |
| I | ILE361 |
| I | TYR369 |
| I | ARG433 |
| I | ARG453 |
| I | PHE467 |
| I | ARG469 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT J 632 |
| Chain | Residue |
| J | ILE361 |
| J | TYR369 |
| J | ARG433 |
| J | ARG453 |
| J | PHE467 |
| J | ARG469 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT K 632 |
| Chain | Residue |
| K | ILE361 |
| K | TYR369 |
| K | ARG453 |
| K | PHE467 |
| K | ARG469 |
| K | HOH2001 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT L 632 |
| Chain | Residue |
| L | ILE361 |
| L | TYR369 |
| L | ARG433 |
| L | ARG453 |
| L | PHE467 |
| L | ARG469 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT M 632 |
| Chain | Residue |
| M | ILE361 |
| M | TYR369 |
| M | ARG433 |
| M | ARG453 |
| M | PHE467 |
| M | ARG469 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT N 632 |
| Chain | Residue |
| N | ILE361 |
| N | TYR369 |
| N | ARG433 |
| N | ARG453 |
| N | PHE467 |
| N | ARG469 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD B 1472 |
| Chain | Residue |
| B | ASP425 |
| B | HOH2006 |
| B | HOH2009 |
| L | ASP425 |
| site_id | BC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CD H 1472 |
| Chain | Residue |
| H | ASP424 |
| N | ASP425 |
| N | ARG457 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CD F 1472 |
| Chain | Residue |
| F | ASP425 |
| G | ASP425 |
| G | HOH2005 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CD J 1472 |
| Chain | Residue |
| J | ASP425 |
| J | CD1474 |
| M | ASP425 |
| site_id | CC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CD J 1473 |
| Chain | Residue |
| G | ASP424 |
| J | ASP424 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD J 1474 |
| Chain | Residue |
| M | ASP425 |
| J | ASP424 |
| J | ASP425 |
| J | CD1472 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q6PHZ2 |
| Chain | Residue | Details |
| A | THR336 | |
| J | THR336 | |
| K | THR336 | |
| L | THR336 | |
| M | THR336 | |
| N | THR336 | |
| B | THR336 | |
| C | THR336 | |
| D | THR336 | |
| E | THR336 | |
| F | THR336 | |
| G | THR336 | |
| H | THR336 | |
| I | THR336 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| A | THR337 | |
| J | THR337 | |
| K | THR337 | |
| L | THR337 | |
| M | THR337 | |
| N | THR337 | |
| B | THR337 | |
| C | THR337 | |
| D | THR337 | |
| E | THR337 | |
| F | THR337 | |
| G | THR337 | |
| H | THR337 | |
| I | THR337 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195 |
| 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 |
