Histidine kinase-like ATPase domain of human cytosolic Hsp90 and its homologs including Escherichia coli HtpG, and related domains
This family includes the histidine kinase-like ATPase (HATPase) domains of 90 kilodalton heat-shock protein (Hsp90) eukaryotic homologs including cytosolic Hsp90, mitochondrial TRAP1 (tumor necrosis factor receptor-associated protein 1), GRP94 (94 kDa glucose-regulated protein) of the endoplasmic reticulum (ER), and chloroplast Hsp90C. It also includes the bacterial homologs of Hsp90, known as HtpG (High temperature protein G). Hsp90 family of chaperones assist other proteins to fold correctly, stabilizes them against heat stress, and aids in protein degradation.
Feature 1:ATP binding site [chemical binding site]
Evidence:
Comment:based on structures of the HATPase domain of human Hsp90, Escherichia coli DNA gyrase B, and other related proteins, bound with ATP, ADP or their analogs; contacts at 4A
Structure:1AM1: Saccharomyces cerevisiae Hsp90 HATPase domain binds ADP, contacts at 4A - View structure with Cn3D
Comment:in this structures of the yeast Hsp90 HATPase domain the ATP-lid is open exposing the ATP binding site
Jiyao W et al.(2023). "The conserved domain database in 2023.",