Research workbench
Structure of a SIR2 enzyme bound to an acetylated P53 peptide
Analyse Structure of a SIR2 enzyme bound to an acetylated P53 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MA3
- Type
- protein
- Length
- 251 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional regulatory protein, SIR2 family; Cellular tumor antigen P53
- UniProt
- O30124, P04637
- Ligands
- ZN
- Pockets
- 2 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional regulatory protein, SIR2 family | protein | 242 | 43% helix, 21% strand | O30124 |
| B | Cellular tumor antigen P53 | protein | 9 | 0% helix, 33% strand | P04637 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 519 | 0.74 | 0.82 | 49 | empty |
| 2 | 53 | 0.23 | 0.72 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 662 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (acetylation).
Compared structures
- 1MA3 · Structure of a Sir2 enzyme bound to an acetylated p53 peptide · the same entry in another collection · chain A against A, TM-score 1.00
- O30124 · AlphaFold monomer V2.0 prediction for NAD-dependent protein deacylase 2 (O30124) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 O30124
- Every structure of UniProt P04637
- Elsewhere: RCSB PDB 1MA3 · PDBe 1MA3 · UniProt O30124 · UniProt P04637
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