Research workbench
N1G9 (IGG1-lambda) Fab fragment
Analyse N1G9 (IGG1-lambda) Fab fragment in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NGQ
- Type
- protein
- Length
- 426 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N1G9 (IGG1-lambda)
- UniProt
- P01751
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 5% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | N1G9 (IGG1-lambda) | protein | 211 | 6% helix, 55% strand | — |
| H | N1G9 (IGG1-lambda) | protein | 215 | 4% helix, 52% strand | P01751 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 680 | 0.68 | 0.77 | 62 | empty |
| 2 | 57 | 0.27 | 0.73 | 17 | empty |
Interfaces
1 interface between chains.
- L–H · 1871 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1NGQ · N1G9 (IGG1-lambda) Fab fragment · 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
- Every structure of UniProt P01751
- Elsewhere: RCSB PDB 1NGQ · PDBe 1NGQ · UniProt P01751
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.