3QFU
 
 | | Crystal structure of Yeast Hsp70 (Bip/kar2) complexed with ADP | | Descriptor: | 78 kDa glucose-regulated protein homolog, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... | | Authors: | Yan, M, Li, J.Z, Sha, B.D. | | Deposit date: | 2011-01-22 | | Release date: | 2011-06-29 | | Last modified: | 2023-09-13 | | Method: | X-RAY DIFFRACTION (1.8 Å) | | Cite: | Structural analysis of the Sil1-Bip complex reveals the mechanism for Sil1 to function as a nucleotide-exchange factor.
Biochem.J., 438, 2011
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3H0X
 | | Crystal structure of peptide-binding domain of Kar2 protein from Saccharomyces cerevisiae | | Descriptor: | 78 kDa glucose-regulated protein homolog | | Authors: | Osipiuk, J, Bigelow, L, Gu, M, Sahi, C, Craig, E.A, Joachimiak, A, Midwest Center for Structural Genomics (MCSG) | | Deposit date: | 2009-04-10 | | Release date: | 2009-04-21 | | Last modified: | 2023-09-06 | | Method: | X-RAY DIFFRACTION (1.92 Å) | | Cite: | X-ray crystal structure of peptide-binding domain of Kar2 protein from Saccharomyces cerevisiae.
To be Published
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3QFP
 | | Crystal structure of yeast Hsp70 (Bip/Kar2) ATPase domain | | Descriptor: | 78 kDa glucose-regulated protein homolog, PHOSPHATE ION | | Authors: | Yan, M, Li, J.Z, Sha, B.D. | | Deposit date: | 2011-01-22 | | Release date: | 2011-06-29 | | Last modified: | 2023-09-13 | | Method: | X-RAY DIFFRACTION (2.26 Å) | | Cite: | Structural analysis of the Sil1-Bip complex reveals the mechanism for Sil1 to function as a nucleotide-exchange factor.
Biochem.J., 438, 2011
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3QML
 | | The structural analysis of Sil1-Bip complex reveals the mechanism for Sil1 to function as a novel nucleotide exchange factor | | Descriptor: | 78 kDa glucose-regulated protein homolog, MAGNESIUM ION, Nucleotide exchange factor SIL1, ... | | Authors: | Yan, M, Li, J.Z, Sha, B.D. | | Deposit date: | 2011-02-04 | | Release date: | 2011-06-29 | | Last modified: | 2024-02-21 | | Method: | X-RAY DIFFRACTION (2.31 Å) | | Cite: | Structural analysis of the Sil1-Bip complex reveals the mechanism for Sil1 to function as a nucleotide-exchange factor.
Biochem.J., 438, 2011
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