Research workbench
SAM domain of diacylglycerol kinase DELTA1 (E35G)
Analyse SAM domain of diacylglycerol kinase DELTA1 (E35G) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BQ7
- Type
- protein
- Length
- 408 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Diacylglycerol kinase delta
- EC
- 2.7.1.107
- UniProt
- Q16760
- Pockets
- 5 · best druggability 0.59
Structure
x-ray diffraction · 4 distinct chains · 69% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E | Diacylglycerol kinase delta (EC 2.7.1.107) | protein | 68 | 69% helix, 0% strand | Q16760 |
| B, F | Diacylglycerol kinase delta (EC 2.7.1.107) | protein | 67 | 70% helix, 0% strand | Q16760 |
| C | Diacylglycerol kinase delta (EC 2.7.1.107) | protein | 70 | 71% helix, 0% strand | Q16760 |
| D | Diacylglycerol kinase delta (EC 2.7.1.107) | protein | 68 | 65% helix, 0% strand | Q16760 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 448 | 0.59 | 0.75 | 43 | empty |
| 2 | 273 | 0.54 | 0.76 | 43 | empty |
| 3 | 132 | 0.38 | 0.73 | 17 | empty |
| 4 | 62 | 0.32 | 0.75 | 18 | empty |
| 5 | 67 | 0.28 | 0.73 | 16 | empty |
Interfaces
8 interfaces between chains.
- C–F · 496 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 475 Ų buried · 13 hydrogen bonds · protein-protein
- D–E · 435 Ų buried · 11 hydrogen bonds · protein-protein
- A–E · 276 Ų buried · 2 hydrogen bonds · protein-protein
- B–C · 199 Ų buried · 0 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 Q16760
- Elsewhere: RCSB PDB 3BQ7 · PDBe 3BQ7 · UniProt Q16760
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