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Structure of DPP2

Analyse Structure of DPP2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4EBB
Type
protein
Length
899 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Dipeptidyl peptidase 2
EC
3.4.14.2
UniProt
Q9UHL4
Ligands
NAG, ZN
Pockets
6 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 44% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ADipeptidyl peptidase 2 (EC 3.4.14.2)protein45044% helix, 13% strandQ9UHL4
BDipeptidyl peptidase 2 (EC 3.4.14.2)protein44944% helix, 13% strandQ9UHL4

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A, B
  • ZN · Zinc ion · metal · 3 copies · chains A

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

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15800.760.8352empty
25070.740.8248empty
31730.550.8021empty
41110.420.7618empty
51030.380.7517empty

Interfaces

1 interface between chains.

  • A–B · 23 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified, 8 disulfide, 3 glycan (engineered, disulfide, N-glycosylation).

Compared structures

  • 4EBB · Structure of DPP2 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9UHL4 · AlphaFold monomer V2.0 prediction for dipeptidyl peptidase 2 (Q9UHL4) · a predicted model of the same protein · chain A against A, TM-score 1.00

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