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Crystal structure of the FAB410-bfache complex
Analyse Crystal structure of the FAB410-bfache complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4QWW
- Type
- protein
- Length
- 1,926 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetylcholinesterase; FAB410 antibody light chain; FAB410 antibody heavy chain
- EC
- 3.1.1.7
- UniProt
- Q92035
- Ligands
- NAG, MAN, BMA, FUC
- Pockets
- 19 · best druggability 0.80
Structure
x-ray diffraction · 4 distinct chains · 20% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Acetylcholinesterase (EC 3.1.1.7) | protein | 529 | 37% helix, 18% strand | Q92035 |
| C, E | FAB410 antibody light chain | protein | 212 | 6% helix, 52% strand | — |
| D | FAB410 antibody heavy chain | protein | 225 | 7% helix, 49% strand | — |
| F | FAB410 antibody heavy chain | protein | 219 | 7% helix, 51% strand | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 9 copies · chains A, F, B, D
- MAN · alpha-D-mannopyranose · sugar · 8 copies · chains F, A, E, D, B
- BMA · beta-D-mannopyranose · sugar · 4 copies · chains F, A, B
- FUC · alpha-L-fucopyranose · sugar · 2 copies · chains A, E, F, B, C, D
- EDO · 1,2-ethanediol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 773 | 0.80 | 0.83 | 80 | FUC |
| 2 | 750 | 0.78 | 0.82 | 68 | NAG, FUC |
| 3 | 729 | 0.68 | 0.76 | 59 | empty |
| 4 | 495 | 0.68 | 0.79 | 37 | EDO |
| 5 | 127 | 0.68 | 0.90 | 25 | empty |
Interfaces
7 interfaces between chains.
- C–D · 1898 Ų buried · 19 hydrogen bonds · protein-protein
- E–F · 1802 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 983 Ų buried · 10 hydrogen bonds · protein-protein
- B–D · 602 Ų buried · 8 hydrogen bonds · protein-protein
- A–F · 587 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 14 disulfide, 5 glycan (disulfide, N-glycosylation).
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 Q92035
- Elsewhere: RCSB PDB 4QWW · PDBe 4QWW · UniProt Q92035
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