Research workbench
SIR2 homologues (D102G/F159A/R170A) mutant-2'-O-acetyl ADP ribose complex
Analyse SIR2 homologues (D102G/F159A/R170A) mutant-2'-O-acetyl ADP ribose complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1M2N
- Type
- protein
- Length
- 498 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Silent information regulator 2
- UniProt
- O28597
- Ligands
- OAD, ZN
- Pockets
- 4 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Silent information regulator 2 | protein | 249 | 38% helix, 18% strand | O28597 |
Ligands and binding sites
- OAD · 2'-O-acetyl adenosine-5-diphosphoribose · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · 2 copies · chains A, B
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 | 413 | 0.76 | 0.85 | 54 | OAD |
| 2 | 454 | 0.74 | 0.83 | 61 | OAD |
| 3 | 127 | 0.42 | 0.76 | 20 | empty |
| 4 | 123 | 0.38 | 0.74 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 609 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 1M2N · Sir2 homologues (D102G/F159A/R170A) mutant-2'-O-acetyl ADP ribose complex · the same entry in another collection · chain A against A, TM-score 1.00
- O28597 · AlphaFold monomer V2.0 prediction for NAD-dependent protein deacylase 1 (O28597) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 O28597
- Elsewhere: RCSB PDB 1M2N · PDBe 1M2N · UniProt O28597
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