Research workbench
Crystal structure of the strawberry pathogenesis-related 10 (pr-10) fra a 1E protein (form a)
Analyse Crystal structure of the strawberry pathogenesis-related 10 (pr-10) fra a 1E… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4C9C
- Type
- protein
- Length
- 315 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Major strawberry allergen fra a 1-E
- UniProt
- Q256S2
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 26% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Major strawberry allergen fra a 1-E | protein | 158 | 26% helix, 42% strand | Q256S2 |
| B | Major strawberry allergen fra a 1-E | protein | 157 | 27% helix, 41% strand | Q256S2 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 765 | 0.80 | 0.83 | 60 | GOL |
| 2 | 793 | 0.75 | 0.79 | 50 | empty |
| 3 | 129 | 0.37 | 0.73 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 406 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 4C9C · Crystal Structure of the Strawberry Pathogenesis-Related 10 (PR-10) Fra a 1E protein… · the same entry in another collection · chain A against A, TM-score 1.00
- Q256S2 · AlphaFold monomer V2.0 prediction for major strawberry allergen fra a 1-E (Q256S2) · a predicted model of the same protein · chain B 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 Q256S2
- Elsewhere: RCSB PDB 4C9C · PDBe 4C9C · UniProt Q256S2
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