Crystal structure of transketolase complexed with thiamine diphosphate from bacillus anthracis

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 13% strand (DSSP).

Ligands and binding sites

• TPP · Thiamine diphosphate · ligand · 2 copies · chains A, B
• MG · Magnesium ion · metal · chains A
• SO4 · Sulfate ion · ion · 9 copies · chains A, B
• FMT · Formic acid · additive · 12 copies · chains A, B
• GOL · Glycerol · additive · 8 copies · chains A, B
• PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A
• ACY · Acetic acid · additive · chains A
• PG5 · 1-methoxy-2-[2-(2-methoxy-ethoxy]-ethane · additive · chains A
• TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
• BTB · 2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diol · additive · chains B

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

Pockets

15 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 4270 Ų buried · 70 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 42 modified (engineered).

Compared structures

• 3M49 · Crystal Structure of Transketolase Complexed with Thiamine Diphosphate from Bacillus… · the same entry in another collection · chain A 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 Q81Y15
• Elsewhere: RCSB PDB 3M49 · PDBe 3M49 · UniProt Q81Y15