Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004692 | molecular_function | cGMP-dependent protein kinase activity |
A | 0005524 | molecular_function | ATP binding |
B | 0004692 | molecular_function | cGMP-dependent protein kinase activity |
B | 0005524 | molecular_function | ATP binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | binding site for residue EDO A 401 |
Chain | Residue |
A | HIS256 |
A | GLU261 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue EDO A 402 |
Chain | Residue |
A | ASP303 |
A | TRP304 |
A | 6FW404 |
A | HOH539 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue EDO A 403 |
Chain | Residue |
A | NA406 |
B | 6FW405 |
B | CA406 |
A | GLN311 |
A | GLU313 |
A | EDO405 |
site_id | AC4 |
Number of Residues | 17 |
Details | binding site for residue 6FW A 404 |
Chain | Residue |
A | ILE264 |
A | LEU296 |
A | ARG297 |
A | LEU299 |
A | TRP304 |
A | PHE305 |
A | GLY306 |
A | GLU307 |
A | LYS308 |
A | ALA309 |
A | ARG316 |
A | THR317 |
A | ALA318 |
A | TYR351 |
A | EDO402 |
B | ASP287 |
B | HOH505 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue EDO A 405 |
Chain | Residue |
A | LYS308 |
A | THR317 |
A | EDO403 |
A | HOH533 |
B | ARG285 |
B | ASP287 |
B | LEU296 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue NA A 406 |
Chain | Residue |
A | LYS308 |
A | GLN311 |
A | GLU313 |
A | EDO403 |
A | HOH573 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue EDO B 401 |
Chain | Residue |
B | HIS338 |
B | HOH529 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue EDO B 402 |
Chain | Residue |
B | GLU226 |
B | TYR227 |
B | SER277 |
B | HOH507 |
B | HOH543 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue EDO B 403 |
Chain | Residue |
B | GLY220 |
B | TYR227 |
B | ALA249 |
B | HOH508 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue EDO B 404 |
Chain | Residue |
B | ASP303 |
B | TRP304 |
B | 6FW405 |
B | HOH535 |
site_id | AD2 |
Number of Residues | 16 |
Details | binding site for residue 6FW B 405 |
Chain | Residue |
A | EDO403 |
B | ILE264 |
B | LEU296 |
B | ARG297 |
B | LEU299 |
B | TRP304 |
B | PHE305 |
B | GLY306 |
B | GLU307 |
B | LYS308 |
B | ALA309 |
B | ARG316 |
B | THR317 |
B | ALA318 |
B | EDO404 |
B | CA406 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue CA B 406 |
Chain | Residue |
A | LYS308 |
A | EDO403 |
B | ARG285 |
B | 6FW405 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue NA B 407 |
Chain | Residue |
A | ASN348 |
B | LYS308 |
B | GLN311 |
B | GLU313 |
B | HOH571 |
Functional Information from PROSITE/UniProt
site_id | PS00888 |
Number of Residues | 17 |
Details | CNMP_BINDING_1 Cyclic nucleotide-binding domain signature 1. IIrQGArGDtFFIIskG |
Chain | Residue | Details |
A | ILE263-GLY279 | |
site_id | PS00889 |
Number of Residues | 18 |
Details | CNMP_BINDING_2 Cyclic nucleotide-binding domain signature 2. FGEkALqgedv......RTAnViA |
Chain | Residue | Details |
A | PHE305-ALA322 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ARG297 | |
A | GLY306 | |
A | ARG316 | |
A | TYR351 | |
B | ARG297 | |
B | GLY306 | |
B | ARG316 | |
B | TYR351 | |