9bex

X-ray crystallography structural model of the immunoglobulin G1 (IgG1) Fc D270C K326C variant

Method: X-RAY DIFFRACTION Dmax: 77.8 Å Quality: EXCELLENT

1. Protein Identity and Related Structures Protein Identity & Related Structures

Immunoglobulin gamma-1 heavy chain

Homo sapiens

UniProt P0DOX5

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Homooligomer Protein × 2 其他Polymer 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain AAA; UniProt 218–449 Chain BBB; UniProt 218–449 Mutation:D270C,K326C ;beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;0.1M HEPES pH 7.5, 10% PEG 3350 Resolution 2.25 Å R-free 0.302

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

105 other PDB entries and 128 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGG1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain AAA; PDBConstruct 1–232; UniProt 218–449 Author chain BBB; PDBConstruct 1–232; UniProt 218–449

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 9bex

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9bex
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9bex
Deposition date deposition_date2024-04-16
最后修订 last_revision2025-04-30
Structure title titleX-ray crystallography structural model of the immunoglobulin G1 (IgG1) Fc D270C K326C variant
Keywords keywordsantibody, crystallizable fragment, disulfide, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier26.58
Radius of gyration Rg (electron density) rg_electron25.28
Forward intensity I(0) i043472700.00
Molecular weight molecular_weight51031.0 kDa
Excluded volume excluded_volume63829 ų
Envelope volume envelope_volume83112 ų
Hydration-shell volume shell_volume27175 ų
Envelope diameter envelope_diameter77.4
Shell Rg shell_rg32.86
Envelope Rg envelope_rg24.65
Shape Rg shape_rg25.28
Total Rg total_rg26.18
Total atoms total_atoms3583
Residues n_residues429
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax77.8
Rg (real space) rg_real26.41
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real4.3470e+07
I(0) uncertainty (real space) i0_real_error6.2970e+05
Rg (reciprocal space) rg_reciprocal26.47
I(0) (reciprocal space) i0_reciprocal43470000.0000
Solution quality estimate total_estimate0.9179
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.9
Skewness Skewness skewness0.013
Kurtosis Kurtosis kurtosis-0.705
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6576000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.981; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)