› 2fwq

X-ray diffraction
1.4Å resolution

Reduced enolate chromophore intermediate for Y66H GFP variant

Released:
DOI: 10.2210/pdb2fwq/pdb
PDB 2fwq coloured by chain and viewed from the front.
PDB 2fwq coloured by chain and viewed from the side.
PDB 2fwq coloured by chain and viewed from the top.
Source organism: Aequorea victoria
Primary publication:
Structural evidence for an enolate intermediate in GFP fluorophore biosynthesis.
Barondeau DP, Tainer JA, Getzoff ED
J. Am. Chem. Soc. 128 3166-8 (2006)
PMID: 16522096

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Green fluorescent protein Chain: A
Molecule details ›
Chain: A
Length: 237 amino acids
Theoretical weight: 26.73 KDa
Source organism: Aequorea victoria
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P42212 (Residues: 2-238; Coverage: 100%)
Gene name: GFP
Sequence domains: Green fluorescent protein
Structure domains: Green fluorescent protein

Ligands and Environments

1 bound ligand:
Ligand MG 1 x MG
1 modified residue:
Ligand XXY 1 x XXY

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P212121
Unit cell:
a: 51.135Å b: 62.451Å c: 71.453Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.136 not available 0.198
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Excited state reactions in fluorescent proteins.
Meech SR. (2009)
4 more

2 mentions without citation

Kinetic isotope effect studies on the de novo rate of chromophore formation in fast- and slow-maturing GFP variants.
Pouwels et al. (2008)
1 more