Research workbench
Human star-related lipid transfer protein 5
Analyse Human star-related lipid transfer protein 5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2R55
- Type
- protein
- Length
- 416 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Star-related lipid transfer protein 5
- UniProt
- Q9NSY2
- Pockets
- 3 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Star-related lipid transfer protein 5 | protein | 208 | 28% helix, 36% strand | Q9NSY2 |
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 222 | 0.84 | 0.96 | 39 | empty |
| 2 | 223 | 0.83 | 0.96 | 35 | empty |
| 3 | 591 | 0.75 | 0.82 | 65 | empty |
Interfaces
1 interface between chains.
- A–B · 622 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
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 Q9NSY2
- Elsewhere: RCSB PDB 2R55 · PDBe 2R55 · UniProt Q9NSY2
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