Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1UW1

A Novel ADP- and Zinc-binding fold from function-directed in vitro evolution

Summary for 1UW1
Entry DOI10.2210/pdb1uw1/pdb
DescriptorARTIFICIAL NUCLEOTIDE BINDING PROTEIN (ANBP), ADENOSINE-5'-DIPHOSPHATE, ZINC ION, ... (4 entities in total)
Functional Keywordsartificial nucleotide binding protein, nucleotide binding protein, in vitro evolution, de novo protein
Biological sourceSYNTHETIC CONSTRUCT
Total number of polymer chains1
Total formula weight10098.59
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 citationLo 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: 15024384
DOI: 10.1038/NSMB745
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.94 Å)
Structure validation

227933

PDB entries from 2024-11-27

PDB statisticsPDBj update infoContact PDBjnumon