› 1rmp

X-ray diffraction
3Å resolution

Probing the Role of Tryptophans in Aequorea Victoria Green Fluorescent Proteins with an Expanded Genetic Code

Released:
DOI: 10.2210/pdb1rmp/pdb
PDB entry 1rmp coloured by chain, front view.
PDB entry 1rmp coloured by chain, side view.
PDB entry 1rmp coloured by chain, top view.
Source organism: Aequorea victoria
Primary publication:
Probing the role of tryptophans in Aequorea victoria green fluorescent proteins with an expanded genetic code.
Budisa N, Pal PP, Alefelder S, Birle P, Krywcun T, Rubini M, Wenger W, Bae JH, Steiner T
Biol Chem 385 191-202 (2004)
PMID: 15101562

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

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: 226 amino acids
Theoretical weight: 25.73 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

No bound ligands
2 modified residues:
Ligand 23S 1 x 23S
Ligand CRO 1 x CRO

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 51.769Å b: 62.77Å c: 70.429Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.292 0.225 0.233
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Fluorinated amino acids: compatibility with native protein structures and effects on protein-protein interactions.
Salwiczek et al. (2012)
7 more