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DPP9 - APO

Analyse DPP9 - APO in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6EOQ
Type
protein
Length
3,064 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Dipeptidyl peptidase 9
EC
3.4.14.5
UniProt
Q86TI2
Pockets
20 · best druggability 0.85

Structure

x-ray diffraction · 4 distinct chains · 18% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ADipeptidyl peptidase 9 (EC 3.4.14.5)protein76719% helix, 35% strandQ86TI2
BDipeptidyl peptidase 9 (EC 3.4.14.5)protein76617% helix, 35% strandQ86TI2
CDipeptidyl peptidase 9 (EC 3.4.14.5)protein76617% helix, 34% strandQ86TI2
DDipeptidyl peptidase 9 (EC 3.4.14.5)protein76518% helix, 34% strandQ86TI2

Pockets

20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12220.850.9733empty
22280.840.9732empty
39410.740.7789empty
48900.720.7786empty
58330.720.7794empty

Interfaces

4 interfaces between chains.

  • B–D · 2152 Ų buried · 27 hydrogen bonds · protein-protein
  • A–C · 2121 Ų buried · 26 hydrogen bonds · protein-protein
  • A–B · 617 Ų buried · 8 hydrogen bonds · protein-protein
  • C–D · 539 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 6EOQ · DPP9 - Apo · the same entry in another collection · chain D against D, TM-score 1.00
  • Q86TI2 · AlphaFold monomer V2.0 prediction for dipeptidyl peptidase 9 (Q86TI2) · a predicted model of the same protein · chain B against A, TM-score 0.99

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