Research workbench
Crystal structure of scheffersomyces stipitis RAI1
Analyse Crystal structure of scheffersomyces stipitis RAI1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5BTO
- Type
- protein
- Length
- 754 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SSRAI1
- UniProt
- A3LNL5
- Pockets
- 7 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SSRAI1 | protein | 377 | 41% helix, 25% strand | A3LNL5 |
| B | SSRAI1 | protein | 377 | 42% helix, 25% strand | A3LNL5 |
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1178 | 0.78 | 0.80 | 75 | empty |
| 2 | 939 | 0.76 | 0.79 | 72 | empty |
| 3 | 263 | 0.63 | 0.81 | 40 | empty |
| 4 | 368 | 0.60 | 0.77 | 40 | empty |
| 5 | 89 | 0.38 | 0.76 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 612 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- A3LNL5 · AlphaFold monomer V2.0 prediction for decapping nuclease RAI1 (A3LNL5) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 A3LNL5
- Elsewhere: RCSB PDB 5BTO · PDBe 5BTO · UniProt A3LNL5
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