2GQ0
Crystal Structure of the Middle Domain of HtpG, the E. coli Hsp90
Summary for 2GQ0
Entry DOI | 10.2210/pdb2gq0/pdb |
Related | 1SF8 |
Descriptor | Chaperone protein htpG (2 entities in total) |
Functional Keywords | molecular chaperone, hsp90, htpg, e. coli, chaperone, hydrolase |
Biological source | Escherichia coli |
Total number of polymer chains | 2 |
Total formula weight | 70116.84 |
Authors | Harris, S.F.,Shiau, A.K.,Agard, D.A. (deposition date: 2006-04-19, release date: 2006-10-31, Last modification date: 2023-08-30) |
Primary citation | Shiau, A.K.,Harris, S.F.,Southworth, D.R.,Agard, D.A. Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements. Cell(Cambridge,Mass.), 127:329-340, 2006 Cited by PubMed: 17055434DOI: 10.1016/j.cell.2006.09.027 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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