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Crystal structure of a SIR2 homolog-NAD complex
Analyse Crystal structure of a SIR2 homolog-NAD complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ICI
- Type
- protein
- Length
- 500 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional regulatory protein, SIR2 family
- UniProt
- O28597
- Ligands
- NAD, ZN
- Pockets
- 4 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional regulatory protein, SIR2 family | protein | 256 | 38% helix, 18% strand | O28597 |
| B | Transcriptional regulatory protein, SIR2 family | protein | 244 | 39% helix, 19% strand | O28597 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · 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, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 539 | 0.72 | 0.80 | 56 | NAD |
| 2 | 524 | 0.71 | 0.80 | 54 | NAD |
| 3 | 387 | 0.64 | 0.79 | 42 | empty |
| 4 | 317 | 0.60 | 0.78 | 38 | empty |
Interfaces
1 interface between chains.
- A–B · 448 Ų buried · 6 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 O28597
- Elsewhere: RCSB PDB 1ICI · PDBe 1ICI · UniProt O28597
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