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PDBe Entry: 1qqm view

D199S MUTANT OF BOVINE 70 KILODALTON HEAT SHOCK PROTEIN
Summary
Header HYDROLASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 1.9 Å, R-factor: 19.3%, Free R-factor: 23.4%, Spacegroup: P 21 21 21
Released 15/09/1999, deposition: 07/06/1999, last revision: 24/02/2009
Authors Johnson, E.R.search; Mckay, D.B.search
Primary citation Mapping the role of active site residues for transducing an ATP-induced conformational change in the bovine 70-kDa heat shock cognate protein.
BIOCHEMISTRYsearch vol:38, pag:10823-10930 (1999) [PubMed ID 10451379 ]search
Keywords HYDROLASE (ACTING ON ACID ANHYDRIDES)search, MOLECULAR CHAPERONEsearch, ATPASEsearch
Organism Bos taurus(cattle) 9913search(A)
UniProt Heat shock cognate 71 kDa protein (Heat shock 70 kDa protein 8) P19120search (A)
Solvent A
Related entries 1hpm
Polymers
Id Name Type UniProt Residues Observed
A D199S MUTANT OF BOVINE 70 KILODALTON HEAT SHOCK PROTEIN Protein P19120 (HSP7C_BOVIN)search
378 100%
Heterogens
Id Name Ligands
A MAGNESIUM ION MG search
A POTASSIUM ION K search
A CHLORIDE ION CL search
A PHOSPHATE ION PO4 search
A ADENOSINE-5'-DIPHOSPHATE ADP search
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