› 1rm9

X-ray diffraction
2.9Å resolution

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

Released:
DOI: 10.2210/pdb1rm9/pdb
PDB 1rm9 coloured by chain and viewed from the front.
PDB 1rm9 coloured by chain and viewed from the side.
PDB 1rm9 coloured by chain and viewed from the top.
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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Green fluorescent protein Chain: A
Molecule details ›
Chain: A
Length: 236 amino acids
Theoretical weight: 26.86 KDa
Source organism: Aequorea victoria
Expression system: Escherichia coli
UniProt:
  • Canonical: P42212 (Residues: 1-238; Coverage: 100%)
Gene name: GFP
Sequence domains: Green fluorescent protein
Structure domains: Green fluorescent protein

Ligands and Environments

No bound ligands
2 modified residues:
Ligand 4FW 1 x 4FW
Ligand 4F3 1 x 4F3

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P212121
Unit cell:
a: 51.057Å b: 62.507Å c: 69.466Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.207 0.268
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Emerging Methods for Efficient and Extensive Incorporation of Non-canonical Amino Acids Using Cell-Free Systems.
Wu et al. (2020)
6 more

1 mention without citation

Interdomain fluorescence resonance energy transfer in SERCA probed by cyan-fluorescent protein fused to the actuator domain.
Winters et al. (2008)