Research workbench
Crystal structure of human IgG-Fc in complex with aglycan and optimized Fc gamma receptor iiia
Analyse Crystal structure of human IgG-Fc in complex with aglycan and optimized Fc… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5YC5
- Type
- protein
- Length
- 595 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Immunoglobulin gamma-1 heavy chain; Low affinity immunoglobulin gamma Fc region receptor…
- UniProt
- P0DOX5, P08637
- Ligands
- NAG, MAN, BMA, FUC, GAL, CL
- Pockets
- 1 · best druggability 0.31
Structure
x-ray diffraction · 3 distinct chains · 9% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Immunoglobulin gamma-1 heavy chain | protein | 211 | 11% helix, 46% strand | P0DOX5 |
| B | Immunoglobulin gamma-1 heavy chain | protein | 213 | 10% helix, 46% strand | P0DOX5 |
| C | Low affinity immunoglobulin gamma Fc region receptor III-a | protein | 171 | 5% helix, 54% strand | P08637 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, C, B
- MAN · alpha-D-mannopyranose · sugar · 4 copies · chains A, B
- BMA · beta-D-mannopyranose · sugar · 2 copies · chains A, B
- FUC · alpha-L-fucopyranose · sugar · 2 copies · chains B
- GAL · beta-D-galactopyranose · sugar · chains A
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 61 | 0.31 | 0.76 | 17 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1206 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 590 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 384 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 2 glycan (disulfide, N-glycosylation).
Compared structures
- 5YC5 · Crystal structure of human IgG-Fc in complex with aglycan and optimized Fc gamma receptor… · the same entry in another collection · chain A against A, TM-score 1.00
- P08637 · AlphaFold monomer V2.0 prediction for low affinity immunoglobulin gamma Fc region… · a predicted model of the same protein · chain C against A, TM-score 0.98
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 P0DOX5
- Every structure of UniProt P08637
- Elsewhere: RCSB PDB 5YC5 · PDBe 5YC5 · UniProt P0DOX5 · UniProt P08637
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