Research workbench
Crystal structure of apo ara H 8
Analyse Crystal structure of apo ara H 8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4M9B
- 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
- 5 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ara H 8 allergen | protein | 156 | 29% helix, 45% strand | Q6VT83 |
Ligands and binding sites
- NA · Sodium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 418 | 0.79 | 0.87 | 53 | empty |
| 2 | 515 | 0.75 | 0.83 | 54 | empty |
| 3 | 77 | 0.37 | 0.77 | 14 | empty |
| 4 | 52 | 0.29 | 0.75 | 12 | empty |
| 5 | 56 | 0.27 | 0.73 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 611 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 4M9B · Crystal structure of Apo Ara h 8 · 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 4M9B · PDBe 4M9B · UniProt Q6VT83
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