X-ray diffraction
3.52Å resolution

Structure of the Fluorescence Recovery Protein from Synechocystis sp PCC 6803, R60K mutant


Function and Biology Details

Biochemical function:
Biological process:
  • not assigned

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Entry contents:
1 distinct polypeptide molecule
Fluorescence recovery protein Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 115 amino acids
Theoretical weight: 13.19 KDa
Source organism: Synechocystis sp. PCC 6803 substr. Kazusa
Expression system: Escherichia coli
  • Canonical: P74103 (Residues: 2-109; Coverage: 99%)
Gene names: frp, slr1964
Sequence domains: Photoprotection regulator fluorescence recovery protein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P41212
Unit cell:
a: 87.406Å b: 87.406Å c: 229.481Å
α: 90° β: 90° γ: 90°
R R work R free
0.237 0.233 0.273
Expression system: Escherichia coli