Research workbench
Crystal structure of anti-ngf AD11 Fab
Analyse Crystal structure of anti-ngf AD11 Fab in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZAN
- Type
- protein
- Length
- 429 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fab AD11 light chain; Fab AD11 heavy chain
- UniProt
- Q4KM66, P84751
- Ligands
- CL
- Pockets
- 3 · best druggability 0.49
Structure
x-ray diffraction · 2 distinct chains · 9% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | Fab AD11 light chain | protein | 213 | 5% helix, 51% strand | Q4KM66 |
| H | Fab AD11 heavy chain | protein | 216 | 13% helix, 51% strand | P84751 |
Ligands and binding sites
- CL · Chloride ion · ion · chains L, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 249 | 0.49 | 0.74 | 39 | empty |
| 2 | 61 | 0.28 | 0.74 | 16 | CL |
| 3 | 53 | 0.28 | 0.74 | 18 | empty |
Interfaces
1 interface between chains.
- L–H · 1877 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
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 Q4KM66
- Every structure of UniProt P84751
- Elsewhere: RCSB PDB 1ZAN · PDBe 1ZAN · UniProt Q4KM66 · UniProt P84751
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