Research workbench
Ternary complex between neonatal Fc receptor, serum albumin and Fc
Analyse Ternary complex between neonatal Fc receptor, serum albumin and Fc in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4N0U
- Type
- protein
- Length
- 1,155 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- IgG receptor fcrn large subunit P51; Beta-2-microglobulin; Serum albumin; Ig gamma-1…
- UniProt
- P55899, P61769, P02768, P01857
- Ligands
- NAG, MAN, BMA, FUL
- Pockets
- 13 · best druggability 0.83
Structure
x-ray diffraction · 4 distinct chains · 44% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | IgG receptor fcrn large subunit P51 | protein | 264 | 26% helix, 41% strand | P55899 |
| B | Beta-2-microglobulin | protein | 99 | 0% helix, 52% strand | P61769 |
| D | Serum albumin | protein | 583 | 73% helix, 0% strand | P02768 |
| E | Ig gamma-1 chain C region | protein | 209 | 8% helix, 43% strand | P01857 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains E
- MAN · alpha-D-mannopyranose · sugar · 2 copies · chains E
- BMA · beta-D-mannopyranose · sugar · chains E
- FUL · beta-L-fucopyranose · sugar · chains E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 654 | 0.83 | 0.87 | 80 | empty |
| 2 | 1163 | 0.80 | 0.81 | 114 | empty |
| 3 | 692 | 0.80 | 0.84 | 89 | empty |
| 4 | 401 | 0.74 | 0.84 | 47 | empty |
| 5 | 67 | 0.65 | 0.93 | 20 | empty |
Interfaces
5 interfaces between chains.
- A–D · 1632 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 1507 Ų buried · 22 hydrogen bonds · protein-protein
- A–E · 554 Ų buried · 10 hydrogen bonds · protein-protein
- B–E · 225 Ų buried · 0 hydrogen bonds · protein-protein
- B–D · 210 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 22 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
- 4N0U · Ternary complex between Neonatal Fc receptor, serum albumin and Fc · the same entry in another collection · chain A against A, TM-score 1.00
- P55899 · AlphaFold monomer V2.0 prediction for IgG receptor fcrn large subunit P51 (P55899) · a predicted model of the same protein · chain A against A, TM-score 0.99
- P61769 · AlphaFold monomer V2.0 prediction for beta-2-microglobulin (P61769) · a predicted model of the same protein · chain B against A, TM-score 0.98
- P02768 · AlphaFold monomer V2.0 prediction for albumin (P02768) · a predicted model of the same protein · chain D against A, TM-score 0.96
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 P55899
- Every structure of UniProt P61769
- Every structure of UniProt P02768
- Every structure of UniProt P01857
- Elsewhere: RCSB PDB 4N0U · PDBe 4N0U · UniProt P55899 · UniProt P61769 · UniProt P02768 · UniProt P01857
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