EC Number   |
Subunits |
Reference |
|---|
    2.7.4.8 | monomer |
1 * 20548, calculated from amino acid sequence |
642691 |
| 2.7.4.8 | monomer |
1 * 23000, SDS-PAGE |
642561 |
| 2.7.4.8 | homodimer |
2 * 24000, SDS-PAGE, gel filtration and glutaraldehyde cross-linking |
739240 |
| 2.7.4.8 | hexamer |
crystallography |
662657 |
| 2.7.4.8 | More |
GMPKs share a highly conserved structure comprising a GMP-binding domain, a central CORE domain that carries the ATP beta-phosphate binding loop (P-loop) and a LID domain which binds the adenine base of ATP and provides catalytic residues to the phosphoryl transfer reaction. |
672440 |
| 2.7.4.8 | dimer |
One of the two SaGMK dimers within the crystal asymmetric unit has two monomers in different conformations: an open form with a bound sulfate ion (mimicking the beta-phosphate of ATP) and a closed form with bound GMP and sulfate ion. Each monomer is bound through its P-loop to a sulfate ion. |
671155 |
| 2.7.4.8 | More |
structural model of microtubule-associated protein-1a. Domain organization of neuronal MAGUKs, overview |
676138 |
| 2.7.4.8 | More |
synaptic scaffolding molecule, S-SCAM, is a synaptic protein, which harbors five or six PSD-95/Discs large/ZO-1, a guanylate kinase, and two WW domains |
675510 |
| 2.7.4.8 | monomer or dimer |
the recombinant and refolded CaVbeta1b-GK is a mixture of dimers and monomers |
700950 |
| 2.7.4.8 | dimer |
the recombinant refolded CaVbeta2a-GK is essentially a dimer |
700950 |
