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Literature summary for 3.4.21.6 extracted from
- The Na+ binding channel of human coagulation proteases: Novel insights on the structure and allosteric modulation revealed by molecular surface analysis (2006), Biophys. Chem., 119, 282-294.
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | ion binding site structure, overview | Homo sapiens |  |
| Na+ | binding channel structure, topography and lipophilicity, and allosteric modulation of the enzyme activity, no aperture on the enzyme surface opposite to the S1 subsite entrance and lack of the three-residue insertion in loop 1, residues 183-189, as found in thrombin, modeling, overview | Homo sapiens | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | structural basis for Na+ specificity of enzymes involved in the coagulation cascade, overview | Homo sapiens | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| factor Xa | - |
Homo sapiens |
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