6OF8
Structure of Thr354Asn, Glu355Gln, Thr412Asn, Ile414Met, Ile464His, and Phe467Met mutant human CamKII-alpha hub domain
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue K F 501 |
Chain | Residue |
D | GLN348 |
F | THR370 |
F | LYS371 |
F | CYS373 |
F | GLN463 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue K F 502 |
Chain | Residue |
F | MET377 |
F | ALA379 |
F | VAL389 |
F | GLY391 |
site_id | AC3 |
Number of Residues | 8 |
Details | binding site for residue GOL C 501 |
Chain | Residue |
C | GLN448 |
D | LEU385 |
D | GLY386 |
D | ASN387 |
E | LEU385 |
E | GLY386 |
E | ASN387 |
F | GLN448 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue GOL E 501 |
Chain | Residue |
E | GLN448 |
F | LEU385 |
F | ASN387 |
G | GLN448 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue K E 502 |
Chain | Residue |
E | THR370 |
E | LYS371 |
E | CYS373 |
E | GLN463 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue GOL A 501 |
Chain | Residue |
A | LEU385 |
A | GLY386 |
A | ASN387 |
B | ILE432 |
B | GLN448 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue K A 502 |
Chain | Residue |
A | THR370 |
A | LYS371 |
A | CYS373 |
A | GLN463 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue K D 501 |
Chain | Residue |
D | THR370 |
D | LYS371 |
D | CYS373 |
D | GLN463 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
F | SER404 | |
B | SER404 | |
C | SER404 | |
G | SER404 | |
E | SER404 | |
A | SER404 | |
D | SER404 | |