Crystal structure of human dpp-IV in complex with (1S,3S, 5S)-2-[(2S)- 2-amino-2-(3-HYDROXYTRICYCLO[3.3.1.13,7]DEC-1- YL)ACETYL]-2- AZABICYCLO[3.1.0]HEXANE-3-carbonitrile (CAS), (1S,3S,5S)-2-((2S)-2- amino-2-(3-hydroxyadamantan-1- YL)ACETYL)-2-AZABICYCLO[3.1.0]HEXANE- 3-carbonitrile (iupac), or bms-477118

Structure

x-ray diffraction · 1 distinct chain · 18% helix, 36% strand (DSSP).

Ligands and binding sites

• BJM · (2~{S})-2-azanyl-1-[(1~{S},3~{S},5~{S})-3-(iminomethyl)-2-azabicyclo[3.1.0]hexan-2-yl]-2-[(5~{R},7~{S})-3-oxidanyl-1-ad amantyl]ethanone · ligand · 2 copies · chains A, B
• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, B

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

Pockets

16 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 2285 Ų buried · 35 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide, 2 covalent (disulfide, covalent ligand).

Compared structures

• 3BJM · Crystal structure of human DPP-IV in complex with (1S,3S… · 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 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 P27487
• Elsewhere: RCSB PDB 3BJM · PDBe 3BJM · UniProt P27487