MolNFT v1 · #87853 · protein
Crystallographic structure of the human IGG1 alpha 2-6 sialilated Fc- fragment
4CDH · Ig gamma-1 chain C region: “Crystallographic structure of the human IGG1 alpha 2-6 sialilated Fc- fragment”. X-ray diffraction, 5 ligands (NAG, MAN, GAL). MolNFT v1 #87853 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 4CDH
- Type
- protein
- Length
- 414 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ig gamma-1 chain C region
- UniProt
- P01857
- Ligands
- NAG, MAN, GAL, BMA, FUL
Structure
x-ray diffraction · 2 distinct chains · 10% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ig gamma-1 chain C region | protein | 206 | 10% helix, 48% strand | P01857 |
| B | Ig gamma-1 chain C region | protein | 208 | 10% helix, 38% strand | P01857 |
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
- GAL · beta-D-galactopyranose · sugar · 3 copies · chains A, B
- BMA · beta-D-mannopyranose · sugar · 2 copies · chains A, B
- FUL · beta-L-fucopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1143 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide, 2 glycan (disulfide, N-glycosylation).
Compared structures
- 4CDH · Crystallographic structure of the Human Igg1 alpha 2-6 sialilated Fc-Fragment · 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 4CDH · PDBe 4CDH · UniProt P01857
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