Cryo-EM structure of the human MCT1/BASIGIN-2 complex in the presence of anti-cancer drug candidate AZD3965 in the outward-open conformation.

Structure

electron microscopy · 2 distinct chains · 56% helix, 16% strand (DSSP).

Ligands and binding sites

• EY0 · 3-methyl-5-[[(4~{R})-4-methyl-4-oxidanyl-1,2-oxazolidin-2-yl]carbonyl]-6-[[5-methyl-3-(trifluoromethyl)-1~{H}-pyrazol-4-yl]methyl]-1-propan-2-yl-thieno[2,3-d]pyrimidine-2,4-dione · ligand · chains A

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

Pockets

4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 756 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

• 6LYY · Cryo-EM structure of the human MCT1/Basigin-2 complex in the presence of anti-cancer drug… · the same entry in another collection · chain A against A, TM-score 1.00
• P53985 · AlphaFold monomer V2.0 prediction for monocarboxylate transporter 1 (P53985) · a predicted model of the same protein · chain A against A, TM-score 0.81
• P35613 · AlphaFold monomer V2.0 prediction for basigin (P35613) · a predicted model of the same protein · chain B against A, TM-score 0.70

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 P53985
• Every structure of UniProt P35613
• Elsewhere: RCSB PDB 6LYY · PDBe 6LYY · UniProt P53985 · UniProt P35613