1VQA
GENE V PROTEIN MUTANT WITH VAL 35 REPLACED BY ALA 35 AND ILE 47 REPLACED BY LEU 47 (V35A, I47L)
Summary for 1VQA
| Entry DOI | 10.2210/pdb1vqa/pdb |
| Descriptor | GENE V PROTEIN (2 entities in total) |
| Functional Keywords | dna-binding protein, mutant, gene v, dna binding protein |
| Biological source | Enterobacteria phage f1 |
| Total number of polymer chains | 1 |
| Total formula weight | 9671.16 |
| Authors | Skinner, M.M.,Terwilliger, T.C. (deposition date: 1996-08-14, release date: 1997-02-12, Last modification date: 2024-02-14) |
| Primary citation | Skinner, M.M.,Terwilliger, T.C. Potential use of additivity of mutational effects in simplifying protein engineering. Proc.Natl.Acad.Sci.USA, 93:10753-10757, 1996 Cited by PubMed Abstract: The problem of rationally engineering protein molecules can be simplified where effects of mutations on protein function are additive. Crystal structures of single and double mutants in the hydrophobic core of gene V protein indicate that structural and functional effects of core mutations are additive when the regions structurally influenced by the mutations do not substantially overlap. These regions of influence can provide a simple basis for identifying sets of mutations that will show additive effects. PubMed: 8855252DOI: 10.1073/pnas.93.20.10753 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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