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Crystal structure of the human IGG1 Fc-FRAGMENT,GLYCOFORM (M3N2F)2

Analyse Crystal structure of the human IGG1 Fc-FRAGMENT,GLYCOFORM (M3N2F)2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1H3U
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
Ligands
NAG, BMA, MAN, FUL
Pockets
1 · best druggability 0.27

Structure

x-ray diffraction · 2 distinct chains · 10% helix, 45% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AIg gamma-1 chain C regionprotein20710% helix, 45% strand—
BIg gamma-1 chain C regionprotein20611% helix, 46% strand—

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B
  • BMA · beta-D-mannopyranose · sugar · 3 copies · chains A, B
  • MAN · alpha-D-mannopyranose · sugar · 3 copies · chains A, B
  • FUL · beta-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
1650.270.7216empty

Interfaces

1 interface between chains.

  • A–B · 1171 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

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

Compared structures

  • 1H3U · Crystal structure of the human IGG1 Fc-FRAGMENT,GLYCOFORM (M3N2F)2 · the same entry in another collection · chain A against A, TM-score 1.00

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