Research workbench
Structure of the phosphatidylcholine binding mutant of yeast SEC14 homolog SFH1 (S175I,T177I) in complex with phosphatidylinositol
Analyse Structure of the phosphatidylcholine binding mutant of yeast SEC14 homolog SFH1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SLD
- Type
- protein
- Length
- 307 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cral-trio domain-containing protein YKL091C
- UniProt
- P33324
- Ligands
- B7N
- Pockets
- 4 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cral-trio domain-containing protein YKL091C | protein | 307 | 52% helix, 11% strand | P33324 |
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
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 672 | 0.87 | 0.90 | 72 | B7N |
| 2 | 264 | 0.63 | 0.81 | 35 | empty |
| 3 | 178 | 0.57 | 0.81 | 24 | empty |
| 4 | 64 | 0.38 | 0.79 | 19 | empty |
Compared structures
- 6SLD · Structure of the Phosphatidylcholine Binding Mutant of Yeast Sec14 Homolog Sfh1… · the same entry in another collection · chain A against A, TM-score 1.00
- P33324 · AlphaFold monomer V2.0 prediction for cral-trio domain-containing protein YKL091C (P33324) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 P33324
- Elsewhere: RCSB PDB 6SLD · PDBe 6SLD · UniProt P33324
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