Research workbench
Crystal structure of LSP1 from saccharomyces cerevisiae
Analyse Crystal structure of LSP1 from saccharomyces cerevisiae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PLT
- Type
- protein
- Length
- 634 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sphingolipid long chain base-responsive protein LSP1
- UniProt
- Q12230
- Pockets
- 2 · best druggability 0.77
Structure
x-ray diffraction · 3 distinct chains · 84% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sphingolipid long chain base-responsive protein LSP1 | protein | 214 | 85% helix, 0% strand | Q12230 |
| B | Sphingolipid long chain base-responsive protein LSP1 | protein | 207 | 85% helix, 0% strand | Q12230 |
| C | Sphingolipid long chain base-responsive protein LSP1 | protein | 213 | 84% helix, 0% strand | Q12230 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 83 | 0.77 | 0.98 | 18 | empty |
| 2 | 143 | 0.43 | 0.75 | 26 | empty |
Interfaces
2 interfaces between chains.
- A–B · 2981 Ų buried · 20 hydrogen bonds · protein-protein
- A–C · 70 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 3PLT · Crystal structure of Lsp1 from Saccharomyces cerevisiae · the same entry in another collection · chain A against A, TM-score 1.00
- Q12230 · AlphaFold monomer V2.0 prediction for sphingolipid long chain base- responsive protein… · a predicted model of the same protein · chain A 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 Q12230
- Elsewhere: RCSB PDB 3PLT · PDBe 3PLT · UniProt Q12230
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