Research workbench
KPFLO11 presents a novel member of the FLO11 family with a unique recognition pattern for homophilic interactions
Analyse KPFLO11 presents a novel member of the FLO11 family with a unique recognition… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5FV5
- Type
- protein
- Length
- 177 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flocculation protein FLO11
- UniProt
- C4R2D7
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Flocculation protein FLO11 | protein | 177 | 7% helix, 43% strand | C4R2D7 |
Ligands and binding sites
- ACT · Acetate ion · additive · 3 copies · chains A
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
- 5FV5 · KpFlo11 presents a novel member of the Flo11 family with a unique recognition pattern for… · the same entry in another collection · chain A against A, TM-score 1.00
- C4R2D7 · AlphaFold monomer V2.0 prediction for flocculation protein FLO11 (C4R2D7) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 C4R2D7
- Elsewhere: RCSB PDB 5FV5 · PDBe 5FV5 · UniProt C4R2D7
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