7LFN: Hyperglycosylated Human IgG1 Fc

Structure of Hyperglycosylated Human IgG1 Fc (Fc267_329). Determined by X-ray diffraction at 2.6 Å resolution. Released 27 Jan 2021.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,315
Mol. weight: 56.56 kDa
Ligands: NAG, FUC
Released: 27 Jan 2021

Explore 7LFN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7LFN contains 22 α-helices and 41 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 11 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	239-243	5	1
α-helix	244-246	3
α-helix	247-250	4
β-strand	258-267	10	1
β-strand	273-279	7	2
β-strand	282-284	3	2
β-strand	288-289	2	1
α-helix	290-292	3
β-strand	293-294	2	1
β-strand	299-307	9	1
α-helix	310-314	5
β-strand	319-325	7	2
β-strand	331-336	6	2
α-helix	338-340	3
β-strand	344	1	3
α-helix	345-346	2
β-strand	347-351	5	4
α-helix	352-354	3
α-helix	356-359	4
β-strand	362-372	11	4
β-strand	373	1	3
β-strand	378-383	6	5
β-strand	386-387	2	5
β-strand	391-393	3	4
α-helix	394-396	3
β-strand	397-398	2	4
β-strand	404-413	10	4
α-helix	414-418	5
β-strand	423-428	6	5
α-helix	433-435	3
β-strand	437-441	5	5

Chain B: 11 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	241-243	3	6
α-helix	244-246	3
α-helix	247-251	5
β-strand	258-262	5	6
β-strand	275-278	4	7
β-strand	283-284	2	7
β-strand	288-289	2	6
β-strand	293-294	2	8
β-strand	300-301	2	8
β-strand	303-307	5	6
α-helix	308-309	2
α-helix	310-314	5
β-strand	319-323	5	7
β-strand	332-336	5	7
α-helix	338-340	3
β-strand	344	1	9
α-helix	345-346	2
β-strand	347-351	5	10
α-helix	352-354	3
α-helix	357-359	3
β-strand	362-372	11	10
β-strand	373	1	9
β-strand	378-383	6	11
β-strand	386-387	2	11
β-strand	391-393	3	10
α-helix	394-396	3
β-strand	397-398	2	10
β-strand	404-413	10	10
α-helix	414-418	5
β-strand	423-428	6	11
α-helix	433-435	3
β-strand	437-441	5	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
IgG1 Fc (Fc267_329)	A, B	protein	233	Homo sapiens	Q6MZV7 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>7LFN_1 IgG1 Fc (Fc267_329) (chains A, B)
GEPKSCDKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVNSTDPEVK
FNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALNSTIEK
TISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTT
PPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	1
FUC	alpha-L-fucopyranose	C6 H12 O5	2

Primary citation

Silent Antibodies: Generation of Hyperglycosylated FCs to Ablate Effector Functions. Fields, J.K., Sundberg, E.J. To be published.

Other PDB entries of the same protein (UniProt Q6MZV7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7RHO 2.0 Å, Human IgG1 Fc fragment, hinge-free, expressed in E. coli
7LF9 2.2 Å, Structure of Hyperglycosylated Human IgG1 Fc (Fc329)
5NSG 2.22 Å, Fc DEDE homodimer variant
5NSC 2.3 Å, Fc DEKK heterodimer variant
6CHF 2.4 Å, Crystal structure of a Fc fragment LALA mutant (L234A, L235A) of human IgG1 (crystal…
6CJX 2.44 Å, Crystal structure of a Fc fragment LALA mutant (L234A, L235A) of human IgG1 (crystal…
6CJC 2.58 Å, Crystal structure of a fc fragment lala mutant (L234A, L235A) of human IgG1 (crystal…
6N9T 2.58 Å, Structure of a peptide-based photo-affinity cross-linker with Herceptin Fc
7LF5 2.6 Å, Structure of Hyperglycosylated Human IgG1 Fc (Fc267)
8F8X 2.6 Å, Crystal structure of Nb.X0 bound to the afucosylated human IgG1 fragment crystal form II
8F8W 2.71 Å, Crystal structure of Nb.X0 bound to the afucosylated human IgG1 fragment crystal form I
9IUJ 2.78 Å, Integrin alpha-v beta-3 in complex with rhodostomin

Browse structure collections

About this viewer

MolViewer shows 7LFN directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.