1PV2
Native Form 2 E.coli Chaperone Hsp31
Summary for 1PV2
Entry DOI | 10.2210/pdb1pv2/pdb |
Related | 1n57 |
Descriptor | Chaperone protein hchA (2 entities in total) |
Functional Keywords | chaperone, heat shock protein, putative catalytic triad, flexibility, monoclinic |
Biological source | Escherichia coli |
Cellular location | Cytoplasm: P31658 |
Total number of polymer chains | 8 |
Total formula weight | 249811.33 |
Authors | Quigley, P.M.,Korotkov, K.,Baneyx, F.,Hol, W.G.J. (deposition date: 2003-06-26, release date: 2004-01-13, Last modification date: 2023-09-20) |
Primary citation | Quigley, P.M.,Korotkov, K.,Baneyx, F.,Hol, W.G.J. A new native EcHsp31 structure suggests a key role of structural flexibility for chaperone function. Protein Sci., 13:269-277, 2004 Cited by PubMed: 14691241DOI: 10.1110/ps.03399604 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.71 Å) |
Structure validation
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