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1UHM

Solution structure of the globular domain of linker histone homolog Hho1p from S. cerevisiae

Summary for 1UHM
Entry DOI10.2210/pdb1uhm/pdb
DescriptorHistone H1 (1 entity in total)
Functional Keywordswinged helix-turn-helix, linker histone, s. cerevisiae, riken structural genomics/proteomics initiative, rsgi, structural genomics, structural protein
Biological sourceSaccharomyces cerevisiae (baker's yeast)
Cellular locationNucleus (Potential): P53551
Total number of polymer chains1
Total formula weight8516.78
Authors
Ono, K.,Kusano, O.,Shimotakahara, S.,Shimizu, M.,Yamazaki, T.,Shindo, H.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2003-07-05, release date: 2003-12-16, Last modification date: 2023-12-27)
Primary citationOno, K.,Kusano, O.,Shimotakahara, S.,Shimizu, M.,Yamazaki, T.,Shindo, H.
The linker histone homolog Hho1p from Saccharomyces cerevisiae represents a winged helix-turn-helix fold as determined by NMR spectroscopy.
Nucleic Acids Res., 31:7199-7207, 2003
Cited by
PubMed: 14654695
DOI: 10.1093/nar/gkg931
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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