ATP-grasp
| ATP-grasp domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
Cartoon representation of the X-ray crystal structure of glycinamide ribonucleotide synthetase from Escherichia coli. , which belongs to the ATP grasp superfamily (PDB: 1gso). | |||||||||
| Identifiers | |||||||||
| Symbol | ATP-grasp | ||||||||
| Pfam | PF02222 | ||||||||
| Pfam clan | CL0179 | ||||||||
| ECOD | 206.1.3 | ||||||||
| InterPro | IPR013815 | ||||||||
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In molecular biology, the ATP-grasp fold is a unique ATP-binding protein structural motif made of two α+β subdomains that "grasp" a molecule of ATP between them. ATP-grasp proteins have ATP-dependent carboxylate-amine/thiol ligase activity.