Research workbench
Structure of pathogen-related yeast protein, PRY1 in complex with a competitive inhibitor of cholesterol binding
Analyse Structure of pathogen-related yeast protein, PRY1 in complex with a competitive… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ETE
- Type
- protein
- Length
- 142 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- PRY1P
- UniProt
- A0A0C6AG41
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | PRY1P | protein | 142 | 36% helix, 18% strand | A0A0C6AG41 |
Ligands and binding sites
- DIO · 1,4-diethylene dioxide · additive · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 5ETE · Structure of pathogen-related yeast protein, Pry1 in complex with a competitive inhibitor… · the same entry in another collection · 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 A0A0C6AG41
- Elsewhere: RCSB PDB 5ETE · PDBe 5ETE · UniProt A0A0C6AG41
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