Structure of trypanosoma brucei brucei tim with the salt-bridge- forming residue ARG191 mutated to ser

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 17% strand (DSSP).

Ligands and binding sites

• PGA · 2-phosphoglycolic acid · ligand · 2 copies · chains A, B
• SO4 · Sulfate ion · ion · chains B
• GOL · Glycerol · additive · 4 copies · chains A, B
• DTT · 2,3-dihydroxy-1,4-dithiobutane · additive · chains A

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 1552 Ų buried · 34 hydrogen bonds · protein-protein

Compared structures

• 1KV5 · Structure of Trypanosoma brucei brucei TIM with the salt-bridge-forming residue Arg191… · the same entry in another collection · chain A against A, TM-score 1.00
• P04789 · AlphaFold monomer V2.0 prediction for triosephosphate isomerase, glycosomal (P04789) · a predicted model of the same protein · chain A against A, TM-score 1.00
• 4TIM · Crystallographic and molecular modeling studies on trypanosomal triosephosphate… · a predicted model of the same protein · chain A against A, TM-score 0.98
• 4TIM · Crystallographic and molecular modeling studies on trypanosomal triosephosphate… · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P04789
• Elsewhere: RCSB PDB 1KV5 · PDBe 1KV5 · UniProt P04789