Research workbench
Crystal structure of saccharomyces cerevisiae SFH2 complexed with phosphatidylinositol
Analyse Crystal structure of saccharomyces cerevisiae SFH2 complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7WVT
- Type
- protein
- Length
- 364 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphatidylinositol transfer protein CSR1
- UniProt
- Q06705
- Ligands
- B7N
- Pockets
- 5 · best druggability 0.88
Structure
x-ray diffraction · 1 distinct chain · 57% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylinositol transfer protein CSR1 | protein | 364 | 57% helix, 8% strand | Q06705 |
Ligands and binding sites
- B7N · (1R)-2-{[(S)-hydroxy{[(1S,2R,3R,4S,5S,6R)-2,3,4,5,6-pentahydroxycyclohexyl]oxy}phosphoryl]oxy}-1-[(octadecanoyloxy)methyl]ethyl (9Z)-octadec-9-enoate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 597 | 0.88 | 0.92 | 51 | B7N |
| 2 | 133 | 0.77 | 0.95 | 26 | empty |
| 3 | 333 | 0.53 | 0.74 | 41 | empty |
| 4 | 97 | 0.51 | 0.83 | 24 | empty |
| 5 | 80 | 0.44 | 0.80 | 17 | empty |
Compared structures
- 7WVT · Crystal structure of Saccharomyces cerevisiae Sfh2 complexed with phosphatidylinositol · the same entry in another collection · chain A against A, TM-score 1.00
- Q06705 · AlphaFold monomer V2.0 prediction for phosphatidylinositol transfer protein CSR1 (Q06705) · 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 Q06705
- Elsewhere: RCSB PDB 7WVT · PDBe 7WVT · UniProt Q06705
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