Research workbench
Crystal structure the Fab fragment of efalizumab
Analyse Crystal structure the Fab fragment of efalizumab in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EO9
- Type
- protein
- Length
- 427 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Efalizumab Fab fragment, light chain; Efalizumab Fab fragment, heavy chain
- Pockets
- 3 · best druggability 0.48
Structure
x-ray diffraction · 2 distinct chains · 8% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | Efalizumab Fab fragment, light chain | protein | 213 | 6% helix, 51% strand | — |
| H | Efalizumab Fab fragment, heavy chain | protein | 214 | 11% helix, 55% strand | — |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 234 | 0.48 | 0.74 | 34 | empty |
| 2 | 64 | 0.29 | 0.74 | 16 | empty |
| 3 | 59 | 0.28 | 0.73 | 16 | empty |
Interfaces
1 interface between chains.
- L–H · 1833 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 3EO9 · Crystal structure the Fab fragment of Efalizumab · the same entry in another collection · chain L against L, 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 3EO9 · PDBe 3EO9
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