Research workbench
X-ray crystal structure of Fc and peptide complex
Analyse X-ray crystal structure of Fc and peptide complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6IQG
- Type
- protein
- Length
- 442 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Immunoglobulin gamma-1 heavy chain; 18-mer peptide G(HCS)DCAYHRGELVWCT(HCS)H(NH2)
- UniProt
- P0DOX5
- Ligands
- NAG, MAN, BMA, FUC, CL
Structure
x-ray diffraction · 3 distinct chains · 9% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Immunoglobulin gamma-1 heavy chain | protein | 207 | 11% helix, 49% strand | P0DOX5 |
| C | 18-mer peptide G(HCS)DCAYHRGELVWCT(HCS)H(NH2) | protein | 13 | 0% helix, 54% strand | — |
| D | 18-mer peptide G(HCS)DCAYHRGELVWCT(HCS)H(NH2) | protein | 15 | 0% helix, 60% strand | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, 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 A
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–B · 1138 Ų buried · 8 hydrogen bonds · protein-protein
- B–D · 645 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 640 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 2 glycan, 2 modified (disulfide, N-glycosylation, nonstandard).
Compared structures
- 6IQG · X-ray crystal structure of Fc and peptide complex · 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 P0DOX5
- Elsewhere: RCSB PDB 6IQG · PDBe 6IQG · UniProt P0DOX5
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