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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
- 3S7I
- 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 0.73
Structure
x-ray diffraction · 2 distinct chains · 18% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Allergen ara H 1, clone P41B | protein | 369 | 18% helix, 43% strand | P43238 |
| B | Allergen ara H 1, clone P41B | protein | 363 | 18% helix, 44% 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 52 | 0.73 | 0.99 | 18 | CL |
| 2 | 230 | 0.45 | 0.73 | 35 | empty |
| 3 | 65 | 0.40 | 0.80 | 18 | empty |
| 4 | 51 | 0.40 | 0.82 | 19 | empty |
| 5 | 54 | 0.29 | 0.75 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 216 Ų buried · 2 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 3S7I · PDBe 3S7I · UniProt P43238
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