Research workbench
Human fcrn complexed with human serum albumin
Analyse Human fcrn complexed with human serum albumin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4N0F
- Type
- protein
- Length
- 3,784 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- IgG receptor fcrn large subunit P51; Beta-2-microglobulin; Serum albumin
- UniProt
- P55899, P61769, P02768
- Pockets
- 20 · best druggability 0.87
Structure
x-ray diffraction · 3 distinct chains · 52% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E, H, K | IgG receptor fcrn large subunit P51 | protein | 264 | 26% helix, 42% strand | P55899 |
| B, F, I, L | Beta-2-microglobulin | protein | 99 | 0% helix, 49% strand | P61769 |
| D, G, J, M | Serum albumin | protein | 583 | 73% helix, 0% strand | P02768 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1152 | 0.87 | 0.88 | 132 | empty |
| 2 | 914 | 0.87 | 0.88 | 106 | empty |
| 3 | 1198 | 0.86 | 0.86 | 111 | empty |
| 4 | 679 | 0.85 | 0.89 | 85 | empty |
| 5 | 1093 | 0.81 | 0.82 | 98 | empty |
Interfaces
17 interfaces between chains.
- A–D · 1650 Ų buried · 20 hydrogen bonds · protein-protein
- E–G · 1636 Ų buried · 20 hydrogen bonds · protein-protein
- H–J · 1623 Ų buried · 20 hydrogen bonds · protein-protein
- K–M · 1615 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 1510 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 80 disulfide (disulfide).
Compared structures
- 4N0F · Human FcRn complexed with human serum albumin · the same entry in another collection · chain M against M, 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 P55899
- Every structure of UniProt P61769
- Every structure of UniProt P02768
- Elsewhere: RCSB PDB 4N0F · PDBe 4N0F · UniProt P55899 · UniProt P61769 · UniProt P02768
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