› 2q6p

X-ray diffraction
2.1Å resolution

The Chemical Control of Protein Folding: Engineering a Superfolder Green Fluorescent Protein

Released:
DOI: 10.2210/pdb2q6p/pdb
PDB entry 2q6p coloured by chain, front view.
PDB entry 2q6p coloured by chain, side view.
PDB entry 2q6p coloured by chain, top view.
Source organism: Aequorea victoria
Primary publication:
Synthetic biology of proteins: tuning GFPs folding and stability with fluoroproline.
Steiner T, Hess P, Bae JH, Wiltschi B, Moroder L, Budisa N
PLoS One 3 e1680 (2008)
PMID: 18301757

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154537 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Green fluorescent protein Chain: A
Molecule details ›
Chain: A
Length: 236 amino acids
Theoretical weight: 27.09 KDa
Source organism: Aequorea victoria
Expression system: Escherichia coli
UniProt:
  • Canonical: P42212 (Residues: 1-238; Coverage: 100%)
Gene name: GFP
Sequence domains: Green fluorescent protein
Structure domains: Green fluorescent protein

Ligands and Environments

No bound ligands
2 modified residues:
Ligand 4FB 10 x 4FB
Ligand CRO 1 x CRO

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 51.168Å b: 62.556Å c: 69.215Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.227 0.26
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Residue-specific incorporation of non-canonical amino acids into proteins: recent developments and applications.
Johnson et al. (2010)
7 more

3 mentions without citation

Biochemistry of fluoroprolines: the prospect of making fluorine a bioelement.
Kubyshkin et al. (2021)
2 more