1BYQ
HSP90 N-TERMINAL DOMAIN BOUND TO ADP-MG
Summary for 1BYQ
Entry DOI | 10.2210/pdb1byq/pdb |
Descriptor | PROTEIN (HEAT SHOCK PROTEIN 90), MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total) |
Functional Keywords | chaperone protein, atp binding, chaperone |
Biological source | Homo sapiens (human) |
Cellular location | Cytoplasm: P07900 |
Total number of polymer chains | 1 |
Total formula weight | 26122.30 |
Authors | Russo, A.A.,Pavletich, N.P. (deposition date: 1998-10-19, release date: 1998-10-28, Last modification date: 2023-08-09) |
Primary citation | Obermann, W.M.,Sondermann, H.,Russo, A.A.,Pavletich, N.P.,Hartl, F.U. In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis. J.Cell Biol., 143:901-910, 1998 Cited by PubMed: 9817749DOI: 10.1083/jcb.143.4.901 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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