› 1hcj

X-ray diffraction
1.8Å resolution

Photoproduct of the wild-type Aequorea victoria Green Fluorescent Protein

Released:
DOI: 10.2210/pdb1hcj/pdb
PDB entry 1hcj coloured by chain, front view.
PDB entry 1hcj coloured by chain, side view.
PDB entry 1hcj coloured by chain, top view.
Source organism: Aequorea victoria
Primary publication:
Phototransformation of green fluorescent protein with UV and visible light leads to decarboxylation of glutamate 222.
van Thor JJ, Gensch T, Hellingwerf KJ, Johnson LN
Nat Struct Biol 9 37-41 (2002)
PMID: 11740505

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154560 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Green fluorescent protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 236 amino acids
Theoretical weight: 26.89 KDa
Source organism: Aequorea victoria
Expression system: Escherichia coli M15
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 GYS 4 x GYS
Ligand ABA 4 x ABA

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P2
Unit cell:
a: 71.77Å b: 65.67Å c: 110.5Å
α: 90° β: 103.88° γ: 90°
R-values:
R R work R free
0.209 0.209 0.267
Expression system: Escherichia coli M15

Quick links

Citations

32 review citations

Fluorescent proteins and their applications in imaging living cells and tissues.
Chudakov et al. (2010)
31 more

1 mention without citation

The Role of the Tight-Turn, Broken Hydrogen Bonding, Glu222 and Arg96 in the Post-translational Green Fluorescent Protein Chromophore Formation.
Lemay et al. (2008)