Research workbench
Crystal structure of the RIF1 C-terminal domain (RIF1-ctd) from saccharomyces cerevisiae
Analyse Crystal structure of the RIF1 C-terminal domain (RIF1-ctd) from saccharomyces… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BJS
- Type
- protein
- Length
- 209 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Telomere length regulator protein RIF1
- UniProt
- P29539
- Pockets
- 2 · best druggability 0.34
Structure
x-ray diffraction · 4 distinct chains · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Telomere length regulator protein RIF1 | protein | 53 | 75% helix, 0% strand | P29539 |
| B | Telomere length regulator protein RIF1 | protein | 55 | 75% helix, 0% strand | P29539 |
| C | Telomere length regulator protein RIF1 | protein | 52 | 69% helix, 0% strand | P29539 |
| D | Telomere length regulator protein RIF1 | protein | 49 | 78% helix, 0% strand | P29539 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 84 | 0.34 | 0.75 | 18 | empty |
| 2 | 50 | 0.25 | 0.73 | 16 | empty |
Interfaces
6 interfaces between chains.
- B–D · 2038 Ų buried · 24 hydrogen bonds · protein-protein
- A–C · 2019 Ų buried · 24 hydrogen bonds · protein-protein
- A–D · 531 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 435 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 103 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 4BJS · Crystal structure of the Rif1 C-terminal domain (Rif1-CTD) from Saccharomyces cerevisiae · the same entry in another collection · chain D against D, TM-score 1.00
- P29539 · AlphaFold monomer V2.0 prediction for telomere length regulator protein RIF1 (P29539) · a predicted model of the same protein · chain C against A, TM-score 0.69
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 P29539
- Elsewhere: RCSB PDB 4BJS · PDBe 4BJS · UniProt P29539
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