Research workbench
The structural basis of sirtuin substrate affinity
Analyse The structural basis of sirtuin substrate affinity in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2H2I
- Type
- protein
- Length
- 244 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NAD-dependent deacetylase
- EC
- 3.5.1.-
- UniProt
- Q9WYW0
- Ligands
- ZPG, ZN
- Pockets
- 1 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD-dependent deacetylase (EC 3.5.1.-) | protein | 244 | 39% helix, 18% strand | Q9WYW0 |
Ligands and binding sites
- ZPG · (2S,5R,8R,11S,14S,17S,21R)-5,8,11,14,17-pentamethyl-4,7,10,13,16,19-hexaoxadocosane-2,21-diol · ligand · chains A
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 300 | 0.76 | 0.87 | 28 | ZPG |
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 Q9WYW0
- Elsewhere: RCSB PDB 2H2I · PDBe 2H2I · UniProt Q9WYW0
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