Tks-L190G mutant from cannabis sativa in complex with lauroyl-CoA

Structure

x-ray diffraction · 3 distinct chains.

Ligands and binding sites

• 8I9 · ~{S}-[2-[3-[[(2~{R})-4-[[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-3,3-dimethyl-2-oxidanyl-butanoyl]amino]propanoylamino]ethyl] tridecanethioate · ligand · 2 copies · chains C, B, D
• GOL · Glycerol · additive · 8 copies · chains A, C, D
• PEG · Di(hydroxyethyl)ether · additive · 5 copies · chains A, C, B
• PG4 · Tetraethylene glycol · additive · chains C
• 1PE · Pentaethylene glycol · additive · chains C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

• 7W6G · TKS-L190G mutant from Cannabis sativa in complex with lauroyl-CoA · the same entry in another collection · chain A against A, TM-score 1.00
• B1Q2B6 · AlphaFold monomer V2.0 prediction for 3,5,7-trioxododecanoyl-CoA synthase (B1Q2B6) · a predicted model of the same protein · chain C against A, TM-score 1.00

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt B1Q2B6
• Elsewhere: RCSB PDB 7W6G · PDBe 7W6G · UniProt B1Q2B6