9hiz

Complex of the Nanofitin Sac7d-C3(C24A) with a human IgG1 Fc fragment

Method: X-RAY DIFFRACTION Dmax: 133.4 Å Quality: REASONABLE

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

Immunoglobulin heavy constant gamma 1

Homo sapiens

UniProt P01857

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 119–327 Chain B; UniProt 119–327 Chain C; UniProt 119–327 Chain D; UniProt 119–327 Not recorded DNA-binding protein 7d × 4 (P13123) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;293 K;24 % (w/v) PEG8000, 0.1 M Tris/HCl pH 8.5 Resolution 2.90 Å R-free 0.279

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.

134 other PDB entries and 162 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGHG1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 9–217; UniProt 119–327 Author chain B; PDBConstruct 9–217; UniProt 119–327 Author chain C; PDBConstruct 9–217; UniProt 119–327 Author chain D; PDBConstruct 9–217; UniProt 119–327

DNA-binding protein 7d

Sulfolobus acidocaldarius DSM 639

UniProt P13123

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain R; UniProt 2–66 Chain S; UniProt 2–66 Chain T; UniProt 2–66 Chain U; UniProt 2–66 Mutation:K7L,Y8L,K9N,K21R,K22D,W24A,V26Q,M29N,S31K,T33L,D35N,T40Y,R42A,A44N,S46D Immunoglobulin heavy constant gamma 1 × 4 (P01857) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;293 K;24 % (w/v) PEG8000, 0.1 M Tris/HCl pH 8.5 Resolution 2.90 Å R-free 0.279

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.

23 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DN7D_SULAC
Isoform
PDB entities 2
Chains and sequence ranges Author chain R; PDBConstruct 5–69; UniProt 2–66 Author chain S; PDBConstruct 5–69; UniProt 2–66 Author chain T; PDBConstruct 5–69; UniProt 2–66 Author chain U; PDBConstruct 5–69; UniProt 2–66

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 9hiz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9hiz
Deposition date deposition_date2024-11-27
最后修订 last_revision2025-07-23
Structure title titleComplex of the Nanofitin Sac7d-C3(C24A) with a human IgG1 Fc fragment
Keywords keywordsNANOFITIN, FC FRAGMENT, IGG1, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier38.92
Radius of gyration Rg (electron density) rg_electron38.62
Forward intensity I(0) i0243676000.00
Molecular weight molecular_weight126140.0 kDa
Excluded volume excluded_volume157930 ų
Envelope volume envelope_volume225370 ų
Hydration-shell volume shell_volume50148 ų
Envelope diameter envelope_diameter141.5
Shell Rg shell_rg42.91
Envelope Rg envelope_rg38.16
Shape Rg shape_rg38.61
Total Rg total_rg38.95
Total atoms total_atoms8892
Residues n_residues1112
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 dmax133.4
Rg (real space) rg_real40.53
Rg uncertainty (real space) rg_real_error0.50
I(0) (real space) i0_real2.4380e+08
I(0) uncertainty (real space) i0_real_error3.5030e+06
Rg (reciprocal space) rg_reciprocal38.96
I(0) (reciprocal space) i0_reciprocal243700000.0000
Solution quality estimate total_estimate0.6759
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary45.5
Skewness Skewness skewness0.498
Kurtosis Kurtosis kurtosis-0.139
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha2.0170
Highest regularization parameter α highest_alpha14530000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.854; Stabil: 0.882; Sysdev: 0.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.627

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)