Research workbench
Engineered human IgG Fc domain AGLYCO801
Analyse Engineered human IgG Fc domain AGLYCO801 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5V43
- Type
- protein
- Length
- 411 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ig gamma-1 chain C region
- UniProt
- P01857
- Pockets
- 8 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 10% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ig gamma-1 chain C region | protein | 209 | 11% helix, 48% strand | P01857 |
| B | Ig gamma-1 chain C region | protein | 202 | 9% helix, 49% strand | P01857 |
Pockets
8 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 210 | 0.46 | 0.73 | 24 | empty |
| 2 | 66 | 0.40 | 0.80 | 13 | empty |
| 3 | 97 | 0.37 | 0.75 | 22 | empty |
| 4 | 63 | 0.34 | 0.76 | 19 | empty |
| 5 | 57 | 0.34 | 0.77 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1574 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 5V43 · Engineered human IgG Fc domain aglyco801 · the same entry in another collection · chain A against A, 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 P01857
- Elsewhere: RCSB PDB 5V43 · PDBe 5V43 · UniProt P01857
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