GL1X · GenesisL1 explorer

Research workbench

Immunoglobulin Fc heterodimer variant

Analyse Immunoglobulin Fc heterodimer variant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4X98
Type
protein
Length
412 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, BMA, FUC
Pockets
4 · best druggability 0.41

Structure

x-ray diffraction · 2 distinct chains · 11% helix, 47% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AIg gamma-1 chain C regionprotein20810% helix, 49% strandP01857
BIg gamma-1 chain C regionprotein20412% helix, 45% strandP01857

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

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11170.410.7622empty
21640.410.7328empty
3650.320.7617empty
4580.270.7315empty

Interfaces

1 interface between chains.

  • A–B · 1139 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

  • 4X98 · Immunoglobulin Fc heterodimer variant · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.