Research workbench
The novel de-long chain fatty acid function of human SIRT6
Analyse The novel de-long chain fatty acid function of human SIRT6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZG6
- Type
- protein
- Length
- 306 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NAD-dependent protein deacetylase sirtuin-6; Peptide
- EC
- 3.5.1.-, 2.4.2.31
- UniProt
- Q8N6T7
- Ligands
- APR, ZN
- Pockets
- 4 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD-dependent protein deacetylase sirtuin-6 (EC 3.5.1.-, 2.4.2.31) | protein | 294 | 28% helix, 15% strand | Q8N6T7 |
| F | Peptide | protein | 12 | 0% helix, 17% strand | — |
Ligands and binding sites
- APR · Adenosine-5-diphosphoribose · ligand · chains A, F
- ZN · Zinc ion · metal · chains A
- GOL · Glycerol · additive · 2 copies · chains A, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 298 | 0.77 | 0.89 | 50 | APR, GOL |
| 2 | 181 | 0.52 | 0.78 | 27 | empty |
| 3 | 173 | 0.49 | 0.77 | 19 | empty |
| 4 | 57 | 0.25 | 0.71 | 15 | empty |
Interfaces
1 interface between chains.
- A–F · 1037 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
- 3ZG6 · The novel de-long chain fatty acid function of human sirt6 · the same entry in another collection · chain A against A, 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 Q8N6T7
- Elsewhere: RCSB PDB 3ZG6 · PDBe 3ZG6 · UniProt Q8N6T7
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