› 1emk

X-ray diffraction
2.1Å resolution

GREEN FLUORESCENT PROTEIN FROM AEQUOREA VICTORIA, MUTANT

Released:
DOI: 10.2210/pdb1emk/pdb
PDB 1emk coloured by chain and viewed from the front.
PDB 1emk coloured by chain and viewed from the side.
PDB 1emk coloured by chain and viewed from the top.
Source organism: Aequorea victoria
Primary publication:
The structural basis for spectral variations in green fluorescent protein.
Palm GJ, Zdanov A, Gaitanaris GA, Stauber R, Pavlakis GN, Wlodawer A
Nat. Struct. Biol. 4 361-5 (1997)
PMID: 9145105

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Green fluorescent protein Chain: A
Molecule details ›
Chain: A
Length: 237 amino acids
Theoretical weight: 26.96 KDa
Source organism: Aequorea victoria
Expression system: Escherichia coli
UniProt:
  • Canonical: P42212 (Residues: 2-237; Coverage: 99%)
Gene name: GFP
Sequence domains: Green fluorescent protein
Structure domains: Green fluorescent protein

Ligands and Environments

No bound ligands
1 modified residue:
Ligand CCY 1 x CCY

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P6122
Unit cell:
a: 89.8Å b: 89.8Å c: 130.1Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.195 0.282
Expression system: Escherichia coli

Quick links

Citations

16 review citations

Detection of protease activity by fluorescent protein FRET sensors: from computer simulation to live cells.
Goryashchenko et al. (2018)
15 more