Research workbench
High resolution structure of the juniperus ashei allergen - jun a 3
Analyse High resolution structure of the juniperus ashei allergen - jun a 3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7P20
- Type
- protein
- Length
- 203 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pathogenesis-related 5 protein jun a 3.0101
- UniProt
- P81295
- Ligands
- CL
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pathogenesis-related 5 protein jun a 3.0101 | protein | 203 | 13% helix, 37% strand | P81295 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 7P20 · High resolution structure of the Juniperus ashei allergen - Jun a 3 · the same entry in another collection · chain A against A, TM-score 1.00
- P81295 · AlphaFold monomer V2.0 prediction for pathogenesis-related 5 protein jun a 3.0101 (P81295) · 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 P81295
- Elsewhere: RCSB PDB 7P20 · PDBe 7P20 · UniProt P81295
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