› 4qkr

X-ray diffraction
1.75Å resolution

Crystal Structure of 6xTyr/PV2: de novo designed beta-trefoil architecture with symmetric primary structure (L22Y/L44Y/L64Y/L85Y/L108Y/L132Y, Primitive Version 2)

Released:
DOI: 10.2210/pdb4qkr/pdb
PDB entry 4qkr coloured by chain, front view.
PDB entry 4qkr coloured by chain, side view.
PDB entry 4qkr coloured by chain, top view.
Source organism: synthetic construct
Primary publication:
A single aromatic core mutation converts a designed "primitive" protein from halophile to mesophile folding.
Longo LM, Tenorio CA, Kumru OS, Middaugh CR, Blaber M
Protein Sci 24 27-37 (2015)
PMID: 25297559

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-165099 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DE NOVO PROTEIN 6XTYR/PV2 Chain: A
Molecule details ›
Chain: A
Length: 132 amino acids
Theoretical weight: 14.62 KDa
Source organism: synthetic construct
Expression system: Escherichia coli
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)

Ligands and Environments

1 bound ligand:
Ligand IMD 1 x IMD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P212121
Unit cell:
a: 34.763Å b: 46.792Å c: 67.648Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.187 0.216
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Peptides before and during the nucleotide world: an origins story emphasizing cooperation between proteins and nucleic acids.
Fried et al. (2022)
8 other articles

1 mention without citation

A single aromatic core mutation converts a designed "primitive" protein from halophile to mesophile folding.
Longo et al. (2015)