› 2whu

X-ray diffraction
2.65Å resolution

Fluorescent Protein mKeima at pH 8.0

Released:
DOI: 10.2210/pdb2whu/pdb
PDB entry 2whu coloured by chain, front view.
PDB entry 2whu coloured by chain, side view.
PDB entry 2whu coloured by chain, top view.
Source organism: Montipora sp. 20
Primary publication:
Reverse pH-dependence of chromophore protonation explains the large Stokes shift of the red fluorescent protein mKeima.
Violot S, Carpentier P, Blanchoin L, Bourgeois D
J Am Chem Soc 131 10356-7 (2009)
PMID: 19722611

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172910 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Large stokes shift fluorescent protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 240 amino acids
Theoretical weight: 27.23 KDa
Source organism: Montipora sp. 20
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q1JV70 (Residues: 1-222; Coverage: 100%)
Gene name: m-keima
Sequence domains: Green fluorescent protein
Structure domains: Green fluorescent protein

Ligands and Environments

No bound ligands
1 modified residue:
Ligand CRQ 4 x CRQ

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: C2
Unit cell:
a: 225.11Å b: 57.75Å c: 93.07Å
α: 90° β: 108.99° γ: 90°
R-values:
R R work R free
0.239 0.235 0.307
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

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

1 mention without citation

Chromophore transformations in red fluorescent proteins.
Subach et al. (2012)