Research workbench
Crystal structure of ara H 8 purified with heating
Analyse Crystal structure of ara H 8 purified with heating in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MAP
- Type
- protein
- Length
- 312 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ara H 8 allergen
- UniProt
- Q6VT83
- Ligands
- NA
- Pockets
- 3 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ara H 8 allergen | protein | 156 | 31% helix, 46% strand | Q6VT83 |
Ligands and binding sites
- NA · Sodium ion · metal · chains B
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 | 385 | 0.75 | 0.85 | 45 | empty |
| 2 | 561 | 0.73 | 0.80 | 61 | empty |
| 3 | 75 | 0.39 | 0.79 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 661 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 4MAP · Crystal structure of Ara h 8 purified with heating · the same entry in another collection · chain A against A, TM-score 1.00
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 Q6VT83
- Elsewhere: RCSB PDB 4MAP · PDBe 4MAP · UniProt Q6VT83
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