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Crystal structure of an Hsp90-Sba1 closed chaperone complex[CHAPERONE]
View in iCn3D Similar StructuresPubMedProteinsConserved DomainsPubChem Compound
Crystal Structure of the Unliganded Form of GRP94, the ER Hsp90: Basis for Nucleotide-Induced Conformational Change, GRP94N APO CRYSTAL[CHAPERONE]
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Crystal Structure of the N-domain of the ER Hsp90 chaperone GRP94 in complex with 2-chlorodideoxyadenosine[CHAPERONE]
Crystal Structure of the N-domain of the ER Hsp90 chaperone GRP94 in complex with Radicicol[CHAPERONE]
Structure of the N-domain of GRP94 bound to the HSP90 inhibitor PU-H54[chaperone/inhibitor]
N-Domain Of Grp94 In Complex With the Novel Ligand N-(2-hydroxyl)ethyl Carboxyamido Adenosine[CHAPERONE]
View in iCn3D Similar StructuresProteinsConserved DomainsPubChem Compound
N-Domain Of Grp94 In Complex With the 2-Iodo-NECA[CHAPERONE]
N-Domain Of Grp94 In Complex With the Novel Ligand N-(2-amino)ethyl Carboxyamido Adenosine[CHAPERONE]
N-Domain Of Grp94 In Complex With the Novel Ligand N-Propyl Carboxyamido Adenosine[CHAPERONE]
GRP94 in complex with the novel HSP90 Inhibitor Radamide[CHAPERONE]
GRP94 in complex with the novel HSP90 Inhibitor Radester amine[CHAPERONE]
GRP94 N-terminal Domain bound to geldanamycin[CHAPERONE]
Crystal Structure of the Unliganded Form of GRP94, the ER Hsp90: Basis for Nucleotide-Induced Conformational Change, GRP94N(DELTA)41 APO CRYSTAL[CHAPERONE]
Crystal Structure of the Unliganded Form of GRP94, the ER Hsp90: Basis for Nucleotide-Induced Conformational Change, GRP94N(DELTA)41 APO CRYSTAL SOAKED WITH ADP[CHAPERONE]
Crystal Structure of the Unliganded Form of GRP94, the ER Hsp90: Basis for Nucleotide-Induced Conformational Change, GRP94N(DELTA)41 APO CRYSTAL SOAKED WITH NECA[CHAPERONE]
N-Domain Of Grp94 Lacking The Charged Domain In Complex With Radicicol[CHAPERONE]
Ligand Induced Conformational Shift in the N-terminal Domain of GRP94, Open Conformation ADP-Complex[CHAPERONE]
Ligand Induced Conformational Shifts in the N-terminal Domain of GRP94, Open Conformation Complexed with the physiological partner ATP[CHAPERONE]
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