2VWC

STRUCTURE OF THE HSP90 INHIBITOR MACBECIN BOUND TO THE N-TERMINUS OF YEAST HSP90.

Replaces:  2VLS

Summary for 2VWC

• Entry DOI: 10.2210/pdb2vwc/pdb
• Related: 1A4H 1AH6 1AH8 1AM1 1AMW 1BGQ 1HK7 1US7 1USU 1USV 1ZW9 1ZWH 2AKP 2BRC 2BRE 2CG9 2CGE 2CGF 2IWS 2IWU 2IWX 2VW5
• Descriptor: ATP-DEPENDENT MOLECULAR CHAPERONE HSP82, MACBECIN, GLYCEROL, ... (4 entities in total)
• Functional Keywords: chaperone, chaperone-complex, inhibitor, heat shock, atp-binding, stress response, multigene family, nucleotide-binding
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Cellular location: Cytoplasm: P02829
• Total number of polymer chains: 1
• Total formula weight: 25427.04

Authors

Roe, S.M.,Prodromou, C.,Pearl, L.H. (deposition date: 2008-06-20, release date: 2008-07-01, Last modification date: 2023-12-13)

• Primary citation: Martin, C.J.,Gaisser, S.,Challis, I.R.,Carletti, I.,Wilkinson, B.,Gregory, M.,Prodromou, C.,Roe, S.M.,Pearl, L.H.,Boyd, S.M.,Zhang, M.Q.; Molecular Characterisation of Macbecin as an Hsp90 Inhibitor; J.Med.Chem., 51:2853-, 2008; PubMed: 18357975; DOI: 10.1021/JM701558C

Experimental method

X-RAY DIFFRACTION (2.4 Å)