Research workbench
Crystal structure of the anti-prion Fab 3F4
Analyse Crystal structure of the anti-prion Fab 3F4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CR9
- Type
- protein
- Length
- 436 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fab antibody light chain; Fab antibody heavy chain
- Pockets
- 7 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | Fab antibody light chain | protein | 219 | 6% helix, 52% strand | — |
| H | Fab antibody heavy chain | protein | 217 | 7% helix, 52% strand | — |
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 779 | 0.67 | 0.75 | 71 | empty |
| 2 | 130 | 0.56 | 0.83 | 23 | empty |
| 3 | 78 | 0.41 | 0.79 | 19 | empty |
| 4 | 98 | 0.40 | 0.77 | 20 | empty |
| 5 | 86 | 0.40 | 0.78 | 17 | empty |
Interfaces
1 interface between chains.
- L–H · 1983 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 1CR9 · Crystal structure of the anti-prion Fab 3F4 · 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 1CR9 · PDBe 1CR9
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