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 | calcium/calmodulin-dependent protein kinase activity |
A | 0005516 | molecular_function | calmodulin binding |
A | 0006468 | biological_process | protein phosphorylation |
B | 0004683 | molecular_function | calcium/calmodulin-dependent protein kinase activity |
B | 0005516 | molecular_function | calmodulin binding |
B | 0006468 | biological_process | protein phosphorylation |
C | 0004683 | molecular_function | calcium/calmodulin-dependent protein kinase activity |
C | 0005516 | molecular_function | calmodulin binding |
C | 0006468 | biological_process | protein phosphorylation |
D | 0004683 | molecular_function | calcium/calmodulin-dependent protein kinase activity |
D | 0005516 | molecular_function | calmodulin binding |
D | 0006468 | biological_process | protein phosphorylation |
E | 0004683 | molecular_function | calcium/calmodulin-dependent protein kinase activity |
E | 0005516 | molecular_function | calmodulin binding |
E | 0006468 | biological_process | protein phosphorylation |
F | 0004683 | molecular_function | calcium/calmodulin-dependent protein kinase activity |
F | 0005516 | molecular_function | calmodulin binding |
F | 0006468 | biological_process | protein phosphorylation |
G | 0004683 | molecular_function | calcium/calmodulin-dependent protein kinase activity |
G | 0005516 | molecular_function | calmodulin binding |
G | 0006468 | biological_process | protein phosphorylation |
H | 0004683 | molecular_function | calcium/calmodulin-dependent protein kinase activity |
H | 0005516 | molecular_function | calmodulin binding |
H | 0006468 | biological_process | protein phosphorylation |
I | 0004683 | molecular_function | calcium/calmodulin-dependent protein kinase activity |
I | 0005516 | molecular_function | calmodulin binding |
I | 0006468 | biological_process | protein phosphorylation |
J | 0004683 | molecular_function | calcium/calmodulin-dependent protein kinase activity |
J | 0005516 | molecular_function | calmodulin binding |
J | 0006468 | biological_process | protein phosphorylation |
K | 0004683 | molecular_function | calcium/calmodulin-dependent protein kinase activity |
K | 0005516 | molecular_function | calmodulin binding |
K | 0006468 | biological_process | protein phosphorylation |
L | 0004683 | molecular_function | calcium/calmodulin-dependent protein kinase activity |
L | 0005516 | molecular_function | calmodulin binding |
L | 0006468 | biological_process | protein phosphorylation |
M | 0004683 | molecular_function | calcium/calmodulin-dependent protein kinase activity |
M | 0005516 | molecular_function | calmodulin binding |
M | 0006468 | biological_process | protein phosphorylation |
N | 0004683 | molecular_function | calcium/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 |