2WKQ: PDB entry 2WKQ

Structure of a photoactivatable Rac1 containing the Lov2 C450A Mutant. Determined by X-ray diffraction at 1.6 Å resolution. Released 18 Aug 2009.

Method: X-ray diffraction
Resolution: 1.6 Å
Organisms: AVENA SATIVA, HOMO SAPIENS
Chains: 1
Atoms: 3,078
Mol. weight: 38.81 kDa
Ligands: MG, FMN, GTP
Released: 18 Aug 2009

Explore 2WKQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2WKQ contains 18 α-helices and 11 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: 18 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	408-410	3
β-strand	414-418	5	1
β-strand	427-430	4	1
α-helix	432-438	7
α-helix	442-445	4
α-helix	450-453	4
α-helix	460-471	12
β-strand	476-483	8	1
β-strand	489-500	12	1
β-strand	506-516	11	1
α-helix	522-543	22
α-helix	546	1
β-strand	547-553	7	2
α-helix	559-568	10
β-strand	580-589	10	2
β-strand	592-601	10	2
α-helix	605-607	3
α-helix	611-614	4
β-strand	620-626	7	2
α-helix	630-635	6
α-helix	636-640	5
α-helix	641-647	7
β-strand	653-658	6	2
α-helix	660-663	4
α-helix	666-674	9
α-helix	679-681	3
α-helix	682-691	10
β-strand	696-699	4	2
α-helix	708-720	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
NPH1-1, ras-related C3 botulinum toxin substrate 1	A	protein	332	AVENA SATIVA, HOMO SAPIENS	O49003 (AlphaFold model), P63000 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2WKQ_1 NPH1-1, RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1 (chains A)
MRGSHHHHHHGSLATTLERIEKNFVITDPRLPDNPIIFASDSFLQLTEYSREEILGRNAR
FLQGPETDRATVRKIRDAIDNQTEVTVQLINYTKSGKKFWNLFHLQPMRDQKGDVQYFIG
VQLDGTEHVRDAAEREGVMLIKKTAENIDEAAKELIKCVVVGDGAVGKTCLLISYTTNAF
PGEYIPTVFDNYSANVMVDGKPVNLGLWDTAGLEDYDRLRPLSYPQTDVFLICFSLVSPA
SFHHVRAKWYPEVRHHCPNTPIILVGTKLDLRDDKDTIEKLKEKKLTPITYPQGLAMAKE
IGAVKYLECSALTQRGLKTVFDEAIRAVLCPP

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	1
FMN	Flavin mononucleotide	C17 H21 N4 O9 P	1
GTP	Guanosine-5'-triphosphate	C10 H16 N5 O14 P3	1

Water and common crystallization additives (EDO, CL) are not listed.

Primary citation

A Genetically Encoded Photoactivatable Rac Controls the Motility of Living Cells. Wu, Y.I., Frey, D., Lungu, O.I. et al. Nature (2009) 461:104. DOI 10.1038/NATURE08241 · PubMed

Other PDB entries of the same protein (UniProt O49003 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7PGZ 0.9 Å, Structure of dark-adapted AsLOV2 Q513L
7PH0 0.98 Å, Structure of light-adapted AsLOV2 Q513L
7PGX 1.0 Å, Structure of dark-adapted AsLOV2 wild type
7PGY 1.09 Å, Structure of light-adapted AsLOV2 wild type
2V0U 1.4 Å, n- and c-terminal helices of oat lov2 (404-546) are involved in light-induced signal…
2V1B 1.55 Å, N- and C-terminal helices of oat LOV2 (404-546) are involved in light-induced signal…
2V1A 1.65 Å, N- and C-terminal helices of oat LOV2 (404-546) are involved in light-induced signal…
2V0W 1.7 Å, N- and C-terminal helices of oat LOV2 (404-546) are involved in light- induced signal…
6NTP 1.89 Å, PTP1B Domain of PTP1B-LOV2 Chimera
2WKP 1.9 Å, Structure of a photoactivatable Rac1 containing Lov2 Wildtype
4WF0 1.95 Å, Crystal Structure of iLID - an Improved Light-Inducible Dimer
5EFW 2.1 Å, Crystal structure of LOV2-Zdk1 - the complex of oat LOV2 and the affibody protein Zdark1

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