6NQK: Fluorescent protein Dronpa

Name: PDB 6NQK: Crystal structure of fast switching M159T mutant of fluorescent protein Dronpa (Dronpa2), Y63(3-FY)
Published: 2019-06-12
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: fluorescent protein

Crystal structure of fast switching M159T mutant of fluorescent protein Dronpa (Dronpa2), Y63(3-FY). Determined by X-ray diffraction at 2.0 Å resolution. Released 12 Jun 2019.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Echinophyllia sp. SC22
Chains: 8
Atoms: 15,641
Mol. weight: 231.84 kDa
Released: 12 Jun 2019

Explore 6NQK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6NQK contains 51 α-helices and 104 β-strands across 8 chains. 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.

Chains A, F and G: 7 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	8-18	11	1
β-strand	21-32	12	1
α-helix	33-35	3
β-strand	37-46	10	1
α-helix	48	1
α-helix	50	1
α-helix	55-58	4
β-strand	70	1	1
α-helix	78-81	4
β-strand	87-95	9	1
β-strand	100-110	11	1
β-strand	113-123	11	1
β-strand	136-139	4	1
α-helix	140-141	2
β-strand	142-149	8	1
β-strand	152-163	12	1
β-strand	168-179	12	1
α-helix	184-187	4
β-strand	189-200	12	1
β-strand	206-216	11	1

Chains B, C, D, E and H: 6 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	8-18	11	2
β-strand	21-32	12	2
β-strand	37-46	10	2
α-helix	48	1
α-helix	50	1
α-helix	55-58	4
β-strand	70	1	2
α-helix	78-81	4
β-strand	87-95	9	2
β-strand	100-110	11	2
β-strand	113-123	11	2
β-strand	136-139	4	2
α-helix	140-141	2
β-strand	142-149	8	2
β-strand	152-163	12	2
β-strand	168-179	12	2
α-helix	184-187	4
β-strand	189-200	12	2
β-strand	206-216	11	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Fluorescent protein Dronpa	A, B, C, D, E, F, G, H	protein	255	Echinophyllia sp. SC22	Q5TLG6 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA

>6NQK_1 Fluorescent protein Dronpa (chains A, B, C, D, E, F, G, H)
GSSHHHHHHSSGLVPGGSHMVSKGEENNMAVIKPDMKIKLRMEGAVNGHPFAIEGVGLGK
PFEGKQSMDLKVKEGGPLPFAYDILTTVFXNRVFAKYPENIVDYFKQSFPEGYSWERSMN
YEDGGICNATNDITLDGDCYIYEIRFDGVNFPANGPVMQKRTVKWEPSTEKLYVRDGVLK
GDVNTALSLEGGGHYRCDFKTTYKAKKVVQLPDYHFVDHHIEIKSHDKDYSNVNLHEHAE
AHSGLPRQAMDELYK

Primary citation

Electrostatic control of photoisomerization pathways in proteins. Romei, M.G., Lin, C.Y., Mathews, I.I. et al. Science (2020) 367:76-79. DOI 10.1126/science.aax1898 · PubMed

Other PDB entries of the same protein (UniProt Q5TLG6 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2IE2 1.7 Å, The 1.7 A crystal structure of Dronpa: a photoswitchable green fluorescent protein
7RRH 1.75 Å, Crystal structure of fast switching R66M/M159T mutant of fluorescent protein Dronpa…
2Z1O 1.75 Å, Crystal structure of a photoswitchable GFP-like protein Dronpa in the bright-state
2GX2 1.8 Å, Crystal structural and functional analysis of GFP-like fluorescent protein Dronpa
2IOV 1.8 Å, Bright-state structure of the reversibly switchable fluorescent protein Dronpa
2Z6Z 1.8 Å, Crystal structure of a photoswitchable GFP-like protein Dronpa in the bright-state
5HZU 1.89 Å, Crystal structure of Dronpa-Ni2+
6MYB 1.9 Å, Room-temperature structure of deuterated Tetdron (isomorph 1)
2GX0 1.9 Å, Crystal structural and functional analysis of GFP-like fluorescent protein
7RRK 1.93 Å, Crystal structure of fast switching M159E mutant of fluorescent protein Dronpa (Dronpa2)
2POX 1.95 Å, Dark state structure of the reversibly switchable fluorescent protein Dronpa
4EMQ 1.95 Å, Crystal structure of a single mutant of Dronpa, the green-on-state PDM1-4

Browse structure collections

About this viewer

MolViewer shows 6NQK directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.