Research workbench
Structure of omalizumab Fab fragment crystal form 1
Analyse Structure of omalizumab Fab fragment crystal form 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4X7S
- Type
- protein
- Length
- 440 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Epididymis luminal protein 214; Ig kappa chain C region
- Pockets
- 5 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| H | Epididymis luminal protein 214 | protein | 222 | 8% helix, 50% strand | — |
| L | Ig kappa chain C region | protein | 218 | 6% helix, 54% strand | — |
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 | 606 | 0.62 | 0.74 | 62 | empty |
| 2 | 233 | 0.55 | 0.78 | 39 | empty |
| 3 | 51 | 0.49 | 0.87 | 20 | empty |
| 4 | 53 | 0.26 | 0.74 | 21 | empty |
| 5 | 51 | 0.25 | 0.73 | 14 | empty |
Interfaces
1 interface between chains.
- H–L · 1928 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 4X7S · Structure of omalizumab Fab fragment crystal form 1 · 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 4X7S · PDBe 4X7S
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