Research workbench
Crystal structure of arg R 1 in complex with histamine
Analyse Crystal structure of arg R 1 in complex with histamine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2X45
- Type
- protein
- Length
- 432 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Allergen arg R 1
- UniProt
- Q5GQ85
- Ligands
- HSM
- Pockets
- 4 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 16% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Allergen arg R 1 | protein | 144 | 16% helix, 41% strand | Q5GQ85 |
Ligands and binding sites
- HSM · Histamine · ligand · 9 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 210 | 0.67 | 0.85 | 24 | HSM |
| 2 | 212 | 0.66 | 0.84 | 25 | HSM |
| 3 | 238 | 0.65 | 0.83 | 27 | HSM |
| 4 | 79 | 0.33 | 0.75 | 20 | empty |
Interfaces
2 interfaces between chains.
- A–B · 568 Ų buried · 22 hydrogen bonds · protein-protein
- A–C · 176 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 9 disulfide (disulfide).
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 Q5GQ85
- Elsewhere: RCSB PDB 2X45 · PDBe 2X45 · UniProt Q5GQ85
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