Research workbench
Crystal structure of S. cerevisiae RAP1-SIR3 complex
Analyse Crystal structure of S. cerevisiae RAP1-SIR3 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OWT
- Type
- protein
- Length
- 316 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA-binding protein RAP1; Regulatory protein SIR3
- UniProt
- P11938, P06701
- Pockets
- 1 · best druggability 0.73
Structure
x-ray diffraction · 3 distinct chains · 59% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-binding protein RAP1 | protein | 148 | 61% helix, 2% strand | P11938 |
| B | DNA-binding protein RAP1 | protein | 148 | 59% helix, 1% strand | P11938 |
| C | Regulatory protein SIR3 | protein | 20 | 55% helix, 5% strand | P06701 |
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 | 1054 | 0.73 | 0.76 | 77 | empty |
Interfaces
3 interfaces between chains.
- A–C · 871 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 419 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 128 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3OWT · Crystal structure of S. cerevisiae RAP1-Sir3 complex · the same entry in another collection · chain A against A, TM-score 1.00
- P11938 · AlphaFold monomer V2.0 prediction for DNA-binding protein RAP1 (P11938) · a predicted model of the same protein · chain B against A, TM-score 0.97
- P06701 · AlphaFold monomer V2.0 prediction for regulatory protein SIR3 (P06701) · a predicted model of the same protein · chain C against A, TM-score 0.47
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 P11938
- Every structure of UniProt P06701
- Elsewhere: RCSB PDB 3OWT · PDBe 3OWT · UniProt P11938 · UniProt P06701
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