Research workbench
SPE7:ANTHRONE complex
Analyse SPE7:ANTHRONE complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BJM
- Type
- protein
- Length
- 230 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- IgE SPE7 heavy chain; IgE SPE7 light chain
- Ligands
- ANF
- Pockets
- 2 · best druggability 0.50
Structure
x-ray diffraction · 2 distinct chains · 3% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| H | IgE SPE7 heavy chain | protein | 120 | 3% helix, 41% strand | — |
| L | IgE SPE7 light chain | protein | 110 | 3% helix, 50% strand | — |
Ligands and binding sites
- ANF · Anthrone · ligand · chains H, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 62 | 0.50 | 0.85 | 20 | ANF |
| 2 | 66 | 0.40 | 0.79 | 15 | empty |
Interfaces
1 interface between chains.
- H–L · 1004 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 2BJM · SPE7:Anthrone Complex · the same entry in another collection · chain H against H, 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
- Elsewhere: RCSB PDB 2BJM · PDBe 2BJM
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