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Structure of the N-terminal domain of the FLO1 adhesin (N-FLO1P) from the yeast saccharomyces cerevisiae, in complex with calcium and mannose
Analyse Structure of the N-terminal domain of the FLO1 adhesin (N-FLO1P) from the yeast… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LHN
- Type
- protein
- Length
- 251 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flocculation protein FLO1
- UniProt
- P32768
- Ligands
- MAN, CA
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Flocculation protein FLO1 | protein | 251 | 7% helix, 39% strand | P32768 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 4LHN · Structure of the N-terminal domain of the Flo1 adhesin (N-Flo1p) from the yeast… · the same entry in another collection · chain A against A, TM-score 1.00
- P32768 · AlphaFold monomer V2.0 prediction for flocculation protein FLO1 (P32768) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P32768
- Elsewhere: RCSB PDB 4LHN · PDBe 4LHN · UniProt P32768
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