Crystal structure of human dpp-IV in complex with sa-(+)-3- (aminomethyl)-4-(2,4-dichlorophenyl)-6-(2-methoxyphenyl)- 2-methyl- 5H-PYRROLO[3,4-B]PYRIDIN-7(6H)-one

Structure

x-ray diffraction · 2 distinct chains · 18% helix, 36% strand (DSSP).

Ligands and binding sites

• KXA · 3-(aminomethyl)-4-(2,4-dichlorophenyl)-6-(2-methoxyphenyl)-2-methyl-5,6-dihydro-7H-pyrrolo[3,4-b]pyridin-7-one · ligand · 2 copies · chains A, B
• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 15 copies · chains A, B

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

Pockets

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

Interfaces

1 interface between chains.

• A–B · 2213 Ų buried · 42 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 glycan, 10 disulfide (N-glycosylation, disulfide).

Compared structures

• 3SX4 · Crystal structure of human dpp-iv in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
• P27487 · AlphaFold monomer V2.0 prediction for dipeptidyl peptidase 4 (P27487) · a predicted model of the same protein · chain B 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 P27487
• Elsewhere: RCSB PDB 3SX4 · PDBe 3SX4 · UniProt P27487