Download MendeleySilent Antibodies: Generation of Hyperglycosylated FCs to Ablate Effector Functions
Fields, J.K., Sundberg, E.J.To be published.
7LFN | pdb_00007lfn
Structure of Hyperglycosylated Human IgG1 Fc (Fc267_329)
- PDB DOI: https://doi.org/10.2210/pdb7LFN/pdb
- Classification: SIGNALING PROTEIN
- Organism(s): Homo sapiens
- Expression System: Homo sapiens
- Mutation(s): No
- Deposited: 2021-01-17 Released: 2021-01-27
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.60 Å
- R-Value Free: 0.270 (Depositor), 0.270 (DCC)
- R-Value Work: 0.230 (Depositor), 0.230 (DCC)
- R-Value Observed: 0.232 (Depositor)
Starting Model: experimental
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This is version 1.2 of the entry. See complete history.
Literature
To be published.
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| IgG1 Fc (Fc267_329) | 233 | Homo sapiens | Mutation(s): 0 Gene Names: DKFZp686C11235 |  | |
UniProt | |||||
Find proteins for Q6MZV7 (Homo sapiens) Explore Q6MZV7 Go to UniProtKB: Q6MZV7 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q6MZV7 | ||||
Glycosylation | |||||
| Glycosylation Sites: 1 | |||||
Sequence AnnotationsExpand | |||||
| |||||
Oligosaccharides
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Length | 2D Diagram | Glycosylation | 3D Interactions |
| alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose | C | 6 |  | N-Glycosylation | |
Glycosylation Resources | |||||
GlyTouCan: G82348BZ GlyCosmos: G82348BZ GlyGen: G82348BZ | |||||
Entity ID: 3 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Length | 2D Diagram | Glycosylation | 3D Interactions |
| beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | D, E | 7 |  | N-Glycosylation | |
Glycosylation Resources | |||||
GlyTouCan: G28663KH GlyCosmos: G28663KH GlyGen: G28663KH | |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| NAG (Subject of Investigation/LOI) Query on NAG | G [auth A] | 2-acetamido-2-deoxy-beta-D-glucopyranose C8 H15 N O6 OVRNDRQMDRJTHS-FMDGEEDCSA-N |  | ||
| FUC Query on FUC | F [auth A], H [auth B] | alpha-L-fucopyranose C6 H12 O5 SHZGCJCMOBCMKK-SXUWKVJYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.60 Å
- R-Value Free: 0.270 (Depositor), 0.270 (DCC)
- R-Value Work: 0.230 (Depositor), 0.230 (DCC)
- R-Value Observed: 0.232 (Depositor)
Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 49.483 | α = 90 |
| b = 79.253 | β = 90 |
| c = 141.321 | γ = 90 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| XDS | data reduction |
| Aimless | data scaling |
| MOLREP | phasing |
Entry History
Deposition Data
- Released Date: 2021-01-27 Deposition Author(s): Fields, J.K., Sundberg, E.J.
Revision History (Full details and data files)
- Version 1.0: 2021-01-27
Type: Initial release - Version 1.1: 2023-10-18
Changes: Data collection, Database references, Refinement description - Version 1.2: 2024-10-23
Changes: Structure summary
