› 4kag

X-ray diffraction
1.12Å resolution

Crystal structure analysis of a single amino acid deletion mutation in EGFP

Released:
DOI: 10.2210/pdb4kag/pdb
PDB entry 4kag coloured by chain, front view.
PDB entry 4kag coloured by chain, side view.
PDB entry 4kag coloured by chain, top view.
Source organism: Aequorea victoria
Primary publication:
Structural and dynamic changes associated with beneficial engineered single-amino-acid deletion mutations in enhanced green fluorescent protein.
Arpino JA, Rizkallah PJ, Jones DD
Acta Crystallogr D Biol Crystallogr 70 2152-62 (2014)
PMID: 25084334

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: 236 amino acids
Theoretical weight: 26.84 KDa
Source organism: Aequorea victoria
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P42212 (Residues: 2-238; Coverage: 99%)
Gene name: GFP
Sequence domains: Green fluorescent protein
Structure domains: Green fluorescent protein

Ligands and Environments

3 bound ligands:
Ligand EDO 16 x EDO
Ligand SO4 2 x SO4
Ligand TRS 3 x TRS
1 modified residue:
Ligand CRO 1 x CRO

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P3221
Unit cell:
a: 57.14Å b: 57.14Å c: 135.33Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.145 0.144 0.161
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Machine Learning-Guided Protein Engineering.
Kouba et al. (2023)
8 other articles

2 mentions without citation

Structural and dynamic changes associated with beneficial engineered single-amino-acid deletion mutations in enhanced green fluorescent protein.
Arpino et al. (2014)
1 more