1BAM
STRUCTURE OF RESTRICTION ENDONUCLEASE BAMHI PHASED AT 1.95 ANGSTROMS RESOLUTION BY MAD ANALYSIS
Summary for 1BAM
Entry DOI | 10.2210/pdb1bam/pdb |
Descriptor | ENDONUCLEASE BamH I (2 entities in total) |
Functional Keywords | endonuclease |
Biological source | Bacillus amyloliquefaciens |
Total number of polymer chains | 1 |
Total formula weight | 24602.30 |
Authors | Aggarwal, A.K.,Newman, M. (deposition date: 1994-12-28, release date: 1995-02-27, Last modification date: 2024-02-07) |
Primary citation | Newman, M.,Strzelecka, T.,Dorner, L.F.,Schildkraut, I.,Aggarwal, A.K. Structure of restriction endonuclease bamhi phased at 1.95 A resolution by MAD analysis. Structure, 2:439-452, 1994 Cited by PubMed Abstract: Type II restriction endonucleases recognize DNA sequences that vary between four to eight base pairs, and require only Mg2+ as a cofactor to catalyze the hydrolysis of DNA. Their protein sequences display a surprising lack of similarity, and no recurring structural motif analogous to the helix-turn-helix or the zinc finger of transcription factors, has yet been discovered. PubMed: 8081758DOI: 10.1016/S0969-2126(00)00045-9 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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