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Crystal structure of ara H 1
Analyse Crystal structure of ara H 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3S7E
- Type
- protein
- Length
- 732 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Allergen ara H 1, clone P41B
- UniProt
- P43238
- Ligands
- CL
- Pockets
- 6 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 17% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Allergen ara H 1, clone P41B | protein | 368 | 17% helix, 41% strand | P43238 |
| B | Allergen ara H 1, clone P41B | protein | 364 | 17% helix, 40% strand | P43238 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 77 | 0.75 | 0.98 | 26 | empty |
| 2 | 62 | 0.75 | 0.99 | 20 | CL |
| 3 | 59 | 0.74 | 0.99 | 20 | CL |
| 4 | 71 | 0.74 | 0.98 | 26 | empty |
| 5 | 362 | 0.57 | 0.76 | 35 | empty |
Interfaces
1 interface between chains.
- A–B · 206 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
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 P43238
- Elsewhere: RCSB PDB 3S7E · PDBe 3S7E · UniProt P43238
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