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MolNFT v1 · #125673 · protein

Room temperature structure of human IGG4-Fc from crystals analysed in situ

5LG1 · Ig gamma-4 chain C region: “Room temperature structure of human IGG4-Fc from crystals analysed in situ”. X-ray diffraction, 4 ligands (NAG, MAN, BMA), 2 pockets (best druggability 0.36). MolNFT v1 #125673 on GenesisL1: 3D structure…

PDB
5LG1
Type
protein
Length
417 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ig gamma-4 chain C region
UniProt
P01861
Ligands
NAG, MAN, BMA, FUC
Pockets
2 · best druggability 0.36

Structure

x-ray diffraction · 2 distinct chains · 11% helix, 48% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AIg gamma-4 chain C regionprotein20911% helix, 49% strandP01861
BIg gamma-4 chain C regionprotein20811% helix, 48% strandP01861

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, 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1720.360.7717empty
2550.280.7514empty

Interfaces

1 interface between chains.

  • A–B · 1212 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

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

Compared structures

  • 5LG1 · Room temperature structure of human IgG4-Fc from crystals analysed in situ · the same entry in another collection · chain A against A, TM-score 1.00
  • P01861 · AlphaFold monomer V2.0 prediction for immunoglobulin heavy constant gamma 4 (P01861) · a predicted model of the same protein · chain B against A, TM-score 0.97

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