› 1yhg

X-ray diffraction
2.5Å resolution

Uncyclized precursor structure of S65G Y66S V68G GFP variant

Released:
DOI: 10.2210/pdb1yhg/pdb
PDB entry 1yhg coloured by chain, front view.
PDB entry 1yhg coloured by chain, side view.
PDB entry 1yhg coloured by chain, top view.
Source organism: Aequorea victoria
Primary publication:
Understanding GFP chromophore biosynthesis: controlling backbone cyclization and modifying post-translational chemistry.
Barondeau DP, Kassmann CJ, Tainer JA, Getzoff ED
Biochemistry 44 1960-70 (2005)
PMID: 15697221

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 239 amino acids
Theoretical weight: 26.69 KDa
Source organism: Aequorea victoria
Expression system: Escherichia coli
UniProt:
  • Canonical: P42212 (Residues: 2-238; Coverage: 100%)
Gene name: GFP
Sequence domains: Green fluorescent protein
Structure domains: Green fluorescent protein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P21
Unit cell:
a: 45.301Å b: 71.098Å c: 60.94Å
α: 90° β: 94.765° γ: 90°
R-values:
R R work R free
0.213 0.213 0.28
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Fluorescent proteins and their applications in imaging living cells and tissues.
Chudakov et al. (2010)
9 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)