Research workbench
DPP8 - slrflyeg, space group 19
Analyse DPP8 - slrflyeg, space group 19 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6EOT
- Type
- protein
- Length
- 5,044 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dipeptidyl peptidase 8; Ser-leu-arg-phe-leu-tyr-glu-gly
- EC
- 3.4.14.5
- UniProt
- Q6V1X1
- Pockets
- 20 · best druggability 0.85
Structure
x-ray diffraction · 3 distinct chains · 19% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D, I, K | Dipeptidyl peptidase 8 (EC 3.4.14.5) | protein | 832 | 19% helix, 33% strand | Q6V1X1 |
| F, C, E, H, J, L | Ser-leu-arg-phe-leu-tyr-glu-gly | protein | 8 | 0% helix, 0% strand | — |
| G | Dipeptidyl peptidase 8 (EC 3.4.14.5) | protein | 836 | 19% helix, 34% 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 | 801 | 0.85 | 0.88 | 82 | empty |
| 2 | 790 | 0.84 | 0.87 | 89 | empty |
| 3 | 1111 | 0.84 | 0.85 | 113 | empty |
| 4 | 1108 | 0.84 | 0.85 | 97 | empty |
| 5 | 935 | 0.84 | 0.86 | 84 | empty |
Interfaces
13 interfaces between chains.
- A–B · 2336 Ų buried · 28 hydrogen bonds · protein-protein
- D–G · 2325 Ų buried · 26 hydrogen bonds · protein-protein
- I–K · 2316 Ų buried · 29 hydrogen bonds · protein-protein
- A–F · 890 Ų buried · 16 hydrogen bonds · protein-protein
- B–C · 879 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 6EOT · DPP8 - SLRFLYEG, space group 19 · the same entry in another collection · chain L against L, 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 Q6V1X1
- Elsewhere: RCSB PDB 6EOT · PDBe 6EOT · UniProt Q6V1X1
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