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Phosphatidylinositol-3-phosphate binding fyve domain of VPS27P protein from saccharomyces cerevisiae
Analyse Phosphatidylinositol-3-phosphate binding fyve domain of VPS27P protein from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VFY
- Type
- protein
- Length
- 67 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphatidylinositol-3-phosphate binding fyve domain of protein VPS27
- UniProt
- P40343
- Ligands
- ZN
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylinositol-3-phosphate binding fyve domain of protein VPS27 | protein | 67 | 27% helix, 30% strand | P40343 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1VFY · Phosphatidylinositol-3-phosphate binding fyve domain of VPS27P protein from saccharomyces… · the same entry in another collection · chain A against A, TM-score 1.00
- P40343 · AlphaFold monomer V2.0 prediction for vacuolar protein sorting- associated protein 27… · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P40343
- Elsewhere: RCSB PDB 1VFY · PDBe 1VFY · UniProt P40343
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