MolNFT v1 · #147822 · protein
DPP8 - apo, space group 19
6EOS · Dipeptidyl peptidase 8: “DPP8 - apo, space group 19”. X-ray diffraction, 20 pockets (best druggability 0.81). MolNFT v1 #147822 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6EOS
- Type
- protein
- Length
- 4,910 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dipeptidyl peptidase 8
- EC
- 3.4.14.5
- UniProt
- Q6V1X1
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 5 distinct chains · 17% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, F | Dipeptidyl peptidase 8 (EC 3.4.14.5) | protein | 815 | 17% helix, 35% strand | Q6V1X1 |
| C | Dipeptidyl peptidase 8 (EC 3.4.14.5) | protein | 829 | 17% helix, 35% strand | Q6V1X1 |
| D | Dipeptidyl peptidase 8 (EC 3.4.14.5) | protein | 815 | 16% helix, 34% strand | Q6V1X1 |
| E | Dipeptidyl peptidase 8 (EC 3.4.14.5) | protein | 825 | 17% helix, 34% strand | Q6V1X1 |
| B | Dipeptidyl peptidase 8 (EC 3.4.14.5) | protein | 811 | 18% helix, 32% strand | Q6V1X1 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 133 | 0.81 | 0.98 | 28 | empty |
| 2 | 120 | 0.80 | 0.98 | 29 | empty |
| 3 | 110 | 0.79 | 0.98 | 27 | empty |
| 4 | 138 | 0.78 | 0.96 | 33 | empty |
| 5 | 113 | 0.77 | 0.96 | 31 | empty |
Interfaces
7 interfaces between chains.
- C–D · 2307 Ų buried · 28 hydrogen bonds · protein-protein
- A–B · 2275 Ų buried · 25 hydrogen bonds · protein-protein
- E–F · 2241 Ų buried · 24 hydrogen bonds · protein-protein
- D–E · 502 Ų buried · 6 hydrogen bonds · protein-protein
- C–B · 495 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
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 Q6V1X1
- Elsewhere: RCSB PDB 6EOS · PDBe 6EOS · UniProt Q6V1X1
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