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Fc heterodimer design 7.4 Y407A + T366V/K409V

Analyse Fc heterodimer design 7.4 Y407A + T366V/K409V in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5DJ2
Type
protein
Length
428 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ig gamma-1 chain C region; Fc-III peptide
UniProt
P01857
Ligands
NAG, MAN, BMA, GAL, FUC
Pockets
1 · best druggability 0.37

Structure

x-ray diffraction · 3 distinct chains · 10% helix, 49% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AIg gamma-1 chain C regionprotein20810% helix, 48% strandP01857
BIg gamma-1 chain C regionprotein20710% helix, 49% strandP01857
CFc-III peptideprotein130% helix, 69% strand—

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 6 copies · chains A, B
  • MAN · alpha-D-mannopyranose · sugar · 4 copies · chains A, B
  • BMA · beta-D-mannopyranose · sugar · 2 copies · chains A, B
  • GAL · beta-D-galactopyranose · sugar · 2 copies · chains A, B
  • FUC · alpha-L-fucopyranose · sugar · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1750.370.7720empty

Interfaces

2 interfaces between chains.

  • A–B · 1155 Ų buried · 4 hydrogen bonds · protein-protein
  • A–C · 670 Ų buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

  • 5DJ2 · Fc Heterodimer Design 7.4 Y407A + T366V/K409V · the same entry in another collection · chain A against A, TM-score 1.00

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