4ELT
Snapshot of the large fragment of DNA polymerase I from Thermus Aquaticus processing modified pyrimidines
Summary for 4ELT
Entry DOI | 10.2210/pdb4elt/pdb |
Related | 3OJS 3OJU 4ELU 4ELV |
Descriptor | DNA polymerase I, thermostable, DNA (5'-D(*GP*AP*CP*CP*AP*CP*GP*GP*CP*GP*CP*(DOC))-3'), DNA (5'-D(*AP*AP*AP*AP*GP*GP*CP*GP*CP*CP*GP*TP*GP*GP*TP*C)-3'), ... (9 entities in total) |
Functional Keywords | dna polymerase, modified nucleotides, a family, dna synthesis, rigid linker, non-natural nucleotide, transferase-dna complex, transferase/dna |
Biological source | Thermus aquaticus More |
Total number of polymer chains | 3 |
Total formula weight | 71235.79 |
Authors | Marx, A.,Diederichs, K.,Obeid, S. (deposition date: 2012-04-11, release date: 2013-03-27, Last modification date: 2023-09-13) |
Primary citation | Obeid, S.,Busskamp, H.,Welte, W.,Diederichs, K.,Marx, A. Interactions of non-polar and "Click-able" nucleotides in the confines of a DNA polymerase active site. Chem.Commun.(Camb.), 48:8320-8322, 2012 Cited by PubMed Abstract: Modified nucleotides play a paramount role in many cutting-edge biomolecular techniques. The present structural study highlights the plasticity and flexibility of the active site of a DNA polymerase while incorporating non-polar "Click-able" nucleotide analogs and emphasizes new insights into rational design guidelines for modified nucleotides. PubMed: 22766607DOI: 10.1039/c2cc34181f PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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