Research workbench
Crystal structure of SIR2 C543S mutant in complex with sid domain of SIR4
Analyse Crystal structure of SIR2 C543S mutant in complex with sid domain of SIR4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4IAO
- Type
- protein
- Length
- 1,049 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P06700, P11978
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 425 | — | P06700 |
| B | — | protein | 429 | — | P06700 |
| C | — | protein | 97 | — | P11978 |
| D | — | protein | 98 | — | P11978 |
Compared structures
- 4IAO · Crystal structure of Sir2 C543S mutant in complex with SID domain of Sir4 · the same entry in another collection · chain D against D, TM-score 1.00
- P06700 · AlphaFold monomer V2.0 prediction for NAD-dependent histone deacetylase SIR2 (P06700) · a predicted model of the same protein · chain B against A, TM-score 0.99
- P11978 · AlphaFold monomer V2.0 prediction for regulatory protein SIR4 (P11978) · a predicted model of the same protein · chain C 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 P06700
- Every structure of UniProt P11978
- Elsewhere: RCSB PDB 4IAO · PDBe 4IAO · UniProt P06700 · UniProt P11978
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