Research workbench
Structure of a SIR2 substrate, alba, reveals a mechanism for deactylation-induced enhancement of DNA-binding
Analyse Structure of a SIR2 substrate, alba, reveals a mechanism for… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NFJ
- Type
- protein
- Length
- 87 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Conserved hypothetical protein AF1956
- UniProt
- O28323
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Conserved hypothetical protein AF1956 | protein | 87 | 33% helix, 39% strand | O28323 |
Compared structures
- 1NFJ · Structure of a Sir2 substrate, alba, reveals a mechanism for deactylation-induced… · the same entry in another collection · chain A against A, TM-score 1.00
- O28323 · AlphaFold monomer V2.0 prediction for DNA/RNA-binding protein alba 2 (O28323) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 O28323
- Elsewhere: RCSB PDB 1NFJ · PDBe 1NFJ · UniProt O28323
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