› 1uw1

X-ray diffraction
1.94Å resolution

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

Released:
DOI: 10.2210/pdb1uw1/pdb
PDB entry 1uw1 coloured by chain, front view.
PDB entry 1uw1 coloured by chain, side view.
PDB entry 1uw1 coloured by chain, top view.
Source organism: synthetic construct
Primary publication:
A novel ADP- and zinc-binding fold from function-directed in vitro evolution.
Lo Surdo P, Walsh MA, Sollazzo M
Nat Struct Mol Biol 11 382-3 (2004)
PMID: 15024384

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162506 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ARTIFICIAL NUCLEOTIDE BINDING PROTEIN (ANBP) Chain: A
Molecule details ›
Chain: A
Length: 80 amino acids
Theoretical weight: 9.61 KDa
Source organism: synthetic construct
Expression system: Escherichia coli BL21(DE3)
Structure domains: Nuclear Transport Factor 2; Chain: A,

Ligands and Environments

2 bound ligands:
Ligand ADP 1 x ADP
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P3221
Unit cell:
a: 71.077Å b: 71.077Å c: 54.883Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.2 0.2 0.228
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Protein design by directed evolution.
Jäckel et al. (2008)
5 more

1 mention without citation

De novo proteins from random sequences through in vitro evolution.
Tong et al. (2021)