1UW1
A Novel ADP- and Zinc-binding fold from function-directed in vitro evolution
Summary for 1UW1
Entry DOI | 10.2210/pdb1uw1/pdb |
Descriptor | ARTIFICIAL NUCLEOTIDE BINDING PROTEIN (ANBP), ADENOSINE-5'-DIPHOSPHATE, ZINC ION, ... (4 entities in total) |
Functional Keywords | artificial nucleotide binding protein, nucleotide binding protein, in vitro evolution, de novo protein |
Biological source | SYNTHETIC CONSTRUCT |
Total number of polymer chains | 1 |
Total formula weight | 10098.59 |
Authors | Lo Surdo, P.,Walsh, M.A.,Sollazzo, M. (deposition date: 2004-01-28, release date: 2004-03-26, Last modification date: 2024-05-08) |
Primary citation | Lo Surdo, P.,Walsh, M.A.,Sollazzo, M. A Novel Adp- and Zinc-Binding Fold from Function-Directed in Vitro Evolution Nat.Struct.Mol.Biol., 11:382-, 2004 Cited by PubMed Abstract: A great challenge to biologists is to create proteins with novel folds and tailored functions. As an alternative to de novo protein design, we investigated the structure of a randomly generated protein targeted to bind ATP. The crystal structure reveals a novel alpha/beta fold bound to its ligand, representing both the first protein structure derived from in vitro evolution and the first nucleotide-binding protein stabilized by a zinc ion. PubMed: 15024384DOI: 10.1038/NSMB745 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.94 Å) |
Structure validation
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