GL1X · GenesisL1 explorer

MolNFT v1 · #108365 · protein

Crystal structure of human Fc at 1.80 a

4W4N · Ig gamma-1 chain C region: “Crystal structure of human Fc at 1.80 a”. X-ray diffraction, 4 ligands (NAG, MAN, BMA), 2 pockets (best druggability 0.30). MolNFT v1 #108365 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
4W4N
Type
protein
Length
413 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
2 · best druggability 0.30

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
AIg gamma-1 chain C regionprotein20611% helix, 49% strandP01857
BIg gamma-1 chain C regionprotein20711% helix, 47% 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 · chains B
  • GOL · Glycerol · additive · 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
1640.300.7516empty
2600.280.7517GOL

Interfaces

1 interface between chains.

  • A–B · 1165 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

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

Compared structures

  • 4W4N · Crystal structure of human Fc at 1.80 A · the same entry in another collection · chain A against A, TM-score 1.00

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