Research workbench
1.52 Angstrom Crystal Structure of Fc fragment of Human IgG1.
Analyse 1.52 Angstrom Crystal Structure of Fc fragment of Human IgG1. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5HSF
- Type
- protein
- Length
- 213 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.52
- Source
- Homo sapiens
- Molecule
- Ig gamma-1 chain C region
- UniProt
- P01857
- Pockets
- 2 · best druggability 0.43
Structure
x-ray diffraction · resolution 1.52 · 2 distinct chains · 10% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ig gamma-1 chain C region | protein | 105 | 8% helix, 50% strand | P01857 |
| B | Ig gamma-1 chain C region | protein | 108 | 12% helix, 49% strand | P01857 |
Ligands and binding sites
- PGE · Triethylene glycol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 160 | 0.43 | 0.74 | 28 | empty |
| 2 | 59 | 0.29 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1188 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 5HSF · 1.52 ångström crystal structure of Fc fragment of human IGG1. · 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 5HSF · PDBe 5HSF · UniProt P01857
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