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Structure of hyperglycosylated human IGG1 Fc (FC267)

Analyse Structure of hyperglycosylated human IGG1 Fc (FC267) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7LF5
Type: protein
Length: 205 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: IGG1 Fc (FC267)
UniProt: Q6MZV7
Ligands: NAG, MAN, BMA, GAL, FUC
Pockets: 1 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	IGG1 Fc (FC267)	protein	205	11% helix, 50% strand	Q6MZV7

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 6 copies · chains A
MAN · alpha-D-mannopyranose · sugar · 2 copies · chains A
BMA · beta-D-mannopyranose · sugar · chains A
GAL · beta-D-galactopyranose · sugar · chains A
FUC · alpha-L-fucopyranose · sugar

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	62	0.36	0.78	20	empty

Modifications

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

Compared structures

7LF5 · Structure of Hyperglycosylated Human IgG1 Fc (Fc267) · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q6MZV7
Elsewhere: RCSB PDB 7LF5 · PDBe 7LF5 · UniProt Q6MZV7

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