4KAG: Green fluorescent protein

Crystal structure analysis of a single amino acid deletion mutation in EGFP. Determined by X-ray diffraction at 1.12 Å resolution. Released 6 Aug 2014.

Method
X-ray diffraction
Resolution
1.12 Å
Organism
Aequorea victoria
Chains
1
Atoms
2,444
Mol. weight
28.39 kDa
Released
6 Aug 2014

Explore 4KAG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4KAG contains 6 α-helices and 14 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 6 helices, 14 β-strands

ElementResiduesLengthSheet
α-helix4-85
β-strand12-22111
β-strand25-36121
β-strand41-4881
α-helix57-604
α-helix69-713
β-strand7311
α-helix76-816
α-helix83-864
β-strand92-10091
β-strand105-115111
β-strand118-128111
β-strand14112
β-strand148-15471
β-strand161-170101
β-strand17112
β-strand176-187121
α-helix194-1974
β-strand199-208101
β-strand217-228121

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Green fluorescent proteinAprotein236Aequorea victoriaP42212 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4KAG_1 Green fluorescent protein (chains A)
MVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPT
LVTTLTYGVQCFSRYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTL
VNRIELKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLA
DHYQQNTPIGGPVLLPDNHYLSTQSALSKDPNEKRDHMVLLEFVTAAGITLGMDELYK

Primary citation

Structural and dynamic changes associated with beneficial engineered single-amino-acid deletion mutations in enhanced green fluorescent protein. Arpino, J.A., Rizkallah, P.J., Jones, D.D. Acta Crystallogr D Biol Crystallogr (2014) 70:2152-2162. DOI 10.1107/S139900471401267X · PubMed

Other PDB entries of the same protein (UniProt P42212 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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