Research workbench
Plasmodium falciparum SIR2A preferentially hydrolyzes medium and long chain fatty acyl lysine
Analyse Plasmodium falciparum SIR2A preferentially hydrolyzes medium and long chain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3U3D
- Type
- protein
- Length
- 270 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional regulatory protein SIR2 homologue; Histone 3 myristoyl lysine 9 peptide
- EC
- 3.5.1.17
- UniProt
- Q8IE47
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional regulatory protein SIR2 homologue (EC 3.5.1.17) | protein | 263 | 37% helix, 20% strand | Q8IE47 |
| B | Histone 3 myristoyl lysine 9 peptide | protein | 7 | 0% helix, 29% strand | — |
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 | 303 | 0.70 | 0.83 | 40 | GOL |
Interfaces
1 interface between chains.
- A–B · 733 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
- 3U3D · Plasmodium falciparum Sir2A preferentially hydrolyzes medium and long chain fatty acyl… · the same entry in another collection · chain A against A, TM-score 1.00
- Q8IE47 · AlphaFold monomer V2.0 prediction for NAD-dependent protein deacylase SIR2A (Q8IE47) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q8IE47
- Elsewhere: RCSB PDB 3U3D · PDBe 3U3D · UniProt Q8IE47
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