› 6qui

X-ray diffraction
1.94Å resolution

GHK tagged GFP variant at 17Kev

Released:
DOI: 10.2210/pdb6qui/pdb
PDB entry 6qui coloured by chain, front view.
PDB entry 6qui coloured by chain, side view.
PDB entry 6qui coloured by chain, top view.
Source organism: Aequorea victoria
Primary publication:
The copper(II)-binding tripeptide GHK, a valuable crystallization and phasing tag for macromolecular crystallography.
Mehr A, Henneberg F, Chari A, Görlich D, Huyton T
Acta Crystallogr D Struct Biol 76 1222-1232 (2020)
PMID: 33263328

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: B, E
Molecule details ›
Chains: B, E
Length: 229 amino acids
Theoretical weight: 26.33 KDa
Source organism: Aequorea victoria
Expression system: Escherichia coli
UniProt:
  • Canonical: P42212 (Residues: 2-3, 4-230; Coverage: 95%)
Gene name: GFP
Sequence domains: Green fluorescent protein

Ligands and Environments

3 bound ligands:
Ligand CU 2 x CU
Ligand SO4 3 x SO4
Ligand GOL 2 x GOL
1 modified residue:
Ligand CRO 2 x CRO

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P6522
Unit cell:
a: 86.252Å b: 86.252Å c: 269.535Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.202 0.201 0.224
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

Indium Kα radiation from a MetalJet X-ray source: the long way to a successful charge-density investigation.
Graw et al. (2023)
1 more

1 mention without citation

The copper(II)-binding tripeptide GHK, a valuable crystallization and phasing tag for macromolecular crystallography.
Mehr et al. (2020)