› 2awm

X-ray diffraction
1.7Å resolution

GFP R96A chromophore maturation recovery mutant R96A Q183R

Released:
DOI: 10.2210/pdb2awm/pdb
PDB entry 2awm coloured by chain, front view.
PDB entry 2awm coloured by chain, side view.
PDB entry 2awm coloured by chain, top view.
Source organism: Aequorea victoria
Primary publication:
Defining the role of arginine 96 in green fluorescent protein fluorophore biosynthesis.
Wood TI, Barondeau DP, Hitomi C, Kassmann CJ, Tainer JA, Getzoff ED
Biochemistry 44 16211-20 (2005)
PMID: 16331981

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 Chain: A
Molecule details ›
Chain: A
Length: 228 amino acids
Theoretical weight: 25.7 KDa
Source organism: Aequorea victoria
Expression system: Escherichia coli
UniProt:
  • Canonical: P42212 (Residues: 2-229; Coverage: 96%)
Gene name: GFP
Sequence domains: Green fluorescent protein
Structure domains: Green fluorescent protein

Ligands and Environments

1 bound ligand:
Ligand MG 2 x MG
1 modified residue:
Ligand CRO 1 x CRO

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P212121
Unit cell:
a: 51.51Å b: 62.34Å c: 71.26Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.223 0.164 0.223
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Fluorescent proteins: maturation, photochemistry and photophysics.
Remington SJ. (2006)
6 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)