2IOP
Crystal Structure of Full-length HtpG, the Escherichia coli Hsp90, Bound to ADP
Summary for 2IOP
Entry DOI | 10.2210/pdb2iop/pdb |
Related | 1Y4S 1Y4U 2IOQ 2IOR |
Descriptor | Chaperone protein htpG, ADENOSINE-5'-DIPHOSPHATE (2 entities in total) |
Functional Keywords | heat shock protein, chaperone, hsp90 |
Biological source | Escherichia coli |
Cellular location | Cytoplasm: P0A6Z3 |
Total number of polymer chains | 4 |
Total formula weight | 287786.49 |
Authors | Shiau, A.K.,Harris, S.F.,Agard, D.A. (deposition date: 2006-10-10, release date: 2006-11-21, Last modification date: 2024-02-21) |
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 (3.55 Å) |
Structure validation
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