MolNFT v1 · #73127 · protein
A systematic screen for protein-lipid interactions in saccharomyces cerevisiae
3NSU: “A systematic screen for protein-lipid interactions in saccharomyces cerevisiae”. X-ray diffraction. MolNFT v1 #73127 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3NSU
- Type
- protein
- Length
- 212 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P40485
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 109 | — | P40485 |
| B | — | protein | 103 | — | P40485 |
Compared structures
- 3NSU · A Systematic Screen for Protein-Lipid Interactions in Saccharomyces cerevisiae · the same entry in another collection · chain A against A, TM-score 1.00
- P40485 · AlphaFold monomer V2.0 prediction for phosphatidylinositol 4,5-bisphosphate-binding… · a predicted model of the same protein · chain B against A, TM-score 0.93
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 P40485
- Elsewhere: RCSB PDB 3NSU · PDBe 3NSU · UniProt P40485
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