This domain is found in several ATP-binding proteins, including: histidine kinase, DNA gyrase B, topoisomerases [1], heat shock protein HSP90 [2, 3, 4], phytochrome-like ATPases and DNA mismatch repair proteins. The fold of this domain consists of two layers, alpha/beta, which contains an 8-stranded mixed beta-sheet.

1. Crystal structures of Escherichia coli topoisomerase IV ParE subunit (24 and 43 kilodaltons): a single residue dictates differences in novobiocin potency against topoisomerase IV and DNA gyrase. Antimicrob. Agents Chemother. 48, 1856-64
2. Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone. J. Biol. Chem. 279, 46162-71
3. The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37). Cell 116, 87-98
4. Structure-activity relationships in purine-based inhibitor binding to HSP90 isoforms. Chem. Biol. 11, 775-85

This domain is found in several ATP-binding proteins, including: histidine kinase, DNA gyrase B,
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