Research workbench
SIR2 H116Y mutant-P53 peptide-NAD
Analyse SIR2 H116Y mutant-P53 peptide-NAD in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2H4H
- Type
- protein
- Length
- 245 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NAD-dependent deacetylase; Cellular tumor antigen P53
- EC
- 3.5.1.-
- UniProt
- Q9WYW0, Q9NP68
- Ligands
- NAD, ZN
- Pockets
- 1 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD-dependent deacetylase (EC 3.5.1.-) | protein | 237 | 42% helix, 20% strand | Q9WYW0 |
| B | Cellular tumor antigen P53 | protein | 8 | 0% helix, 38% strand | Q9NP68 |
Ligands and binding sites
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 | 205 | 0.72 | 0.88 | 40 | NAD |
Interfaces
1 interface between chains.
- A–B · 630 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (acetylation).
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
- Every structure of UniProt Q9NP68
- Elsewhere: RCSB PDB 2H4H · PDBe 2H4H · UniProt Q9WYW0 · UniProt Q9NP68
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