MolNFT v1 · #80655 · protein
Plasmodium falciparum SIR2A preferentially hydrolyzes medium and long chain fatty acyl lysine
3U3D: “Plasmodium falciparum SIR2A preferentially hydrolyzes medium and long chain fatty acyl lysine”. X-ray diffraction. MolNFT v1 #80655 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3U3D
- Type
- protein
- Length
- 270 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q8IE47
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 263 | — | Q8IE47 |
| B | — | protein | 7 | — | — |
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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