› 1kp5

X-ray diffraction
2.6Å resolution

Cyclic Green Fluorescent Protein

Released:
DOI: 10.2210/pdb1kp5/pdb
PDB entry 1kp5 coloured by chain, front view.
PDB entry 1kp5 coloured by chain, side view.
PDB entry 1kp5 coloured by chain, top view.
Source organism: Aequorea victoria
Primary publication:
Structure of cyclized green fluorescent protein.
Hofmann A, Iwai H, Hess S, Plückthun A, Wlodawer A
Acta Crystallogr D Biol Crystallogr 58 1400-6 (2002)
PMID: 12198295

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo tetramer
homo dimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Green fluorescent protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 246 amino acids
Theoretical weight: 27.97 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

1 bound ligand:
Ligand SO4 8 x SO4
1 modified residue:
Ligand GYS 2 x GYS

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9B
Spacegroup: P6522
Unit cell:
a: 142.447Å b: 142.447Å c: 183.809Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.208 0.208 0.256
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

A flow cytometric method to detect protein-protein interaction in living cells by directly visualizing donor fluorophore quenching during CFP-->YFP fluorescence resonance energy transfer (FRET).
He et al. (2003)
3 more

1 mention without citation

GFP-complementation assay to detect functional CPP and protein delivery into living cells.
Milech et al. (2015)