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Human IGG1 Fc fragment, C239 insertion mutant

Analyse Human IGG1 Fc fragment, C239 insertion mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6P6D
Type
protein
Length
416 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.31
Source
Homo sapiens
Molecule
IgG1 Fc fragment
UniProt
Q6MZV7
Ligands
CYS, NAG, MAN, BMA, FUC
Pockets
2 · best druggability 0.37

Structure

x-ray diffraction · resolution 2.31 · 1 distinct chain · 11% helix, 47% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BIgG1 Fc fragmentprotein20811% helix, 47% strandQ6MZV7

Ligands and binding sites

  • CYS · Cysteine · ligand · 2 copies · chains A, B
  • 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
11140.370.7423empty
2630.270.7215empty

Interfaces

1 interface between chains.

  • A–B · 1192 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

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

Compared structures

  • 6P6D · Human IGG1 Fc fragment, C239 insertion mutant · the same entry in another collection · chain A against A, TM-score 1.00

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