9n20

Structure of C3d Bound to a Fragment of FHR-2 and S. aureus Efb-C

Method: X-RAY DIFFRACTION Dmax: 90.0 Å Quality: REASONABLE

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

Complement C3dg fragment

Homo sapiens

UniProt P01024

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 996–1287 Fragment:residues 996-1287 Fibrinogen-binding protein × 1 (P68799) Complement factor H-related protein 2 × 1 (P36980) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M imidazole [pH 6.7] 12% (w/v) peg-20k Resolution 3.30 Å R-free 0.214

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.

74 other PDB entries and 117 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CO3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–297; UniProt 996–1287

Fibrinogen-binding protein

Staphylococcus aureus subsp. aureus Mu50

UniProt P68799

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 94–165 Not recorded Complement C3dg fragment × 1 (P01024) Complement factor H-related protein 2 × 1 (P36980) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M imidazole [pH 6.7] 12% (w/v) peg-20k Resolution 3.30 Å R-free 0.214

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.

1 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIB_STAAM
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 4–75; UniProt 94–165

Complement factor H-related protein 2

Homo sapiens

UniProt P36980

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 145–270 Not recorded Complement C3dg fragment × 1 (P01024) Fibrinogen-binding protein × 1 (P68799) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M imidazole [pH 6.7] 12% (w/v) peg-20k Resolution 3.30 Å R-free 0.214

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.

3 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FHR2_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain B; PDBConstruct 6–131; UniProt 145–270

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 9n20

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9n20
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9n20
Deposition date deposition_date2025-01-27
Structure title titleStructure of C3d Bound to a Fragment of FHR-2 and S. aureus Efb-C
Keywords keywordscomplement system, C3, RCA, inhibitor, 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_guinier25.60
Radius of gyration Rg (electron density) rg_electron24.65
Forward intensity I(0) i046774800.00
Molecular weight molecular_weight54130.0 kDa
Excluded volume excluded_volume68207 ų
Envelope volume envelope_volume81614 ų
Hydration-shell volume shell_volume27981 ų
Envelope diameter envelope_diameter91.6
Shell Rg shell_rg31.53
Envelope Rg envelope_rg25.07
Shape Rg shape_rg24.63
Total Rg total_rg25.48
Total atoms total_atoms3808
Residues n_residues481
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 dmax90.0
Rg (real space) rg_real26.72
Rg uncertainty (real space) rg_real_error0.32
I(0) (real space) i0_real4.6860e+07
I(0) uncertainty (real space) i0_real_error6.1320e+05
Rg (reciprocal space) rg_reciprocal25.60
I(0) (reciprocal space) i0_reciprocal46770000.0000
Solution quality estimate total_estimate0.6572
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary30.5
Skewness Skewness skewness0.541
Kurtosis Kurtosis kurtosis0.091
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha4.1120
Highest regularization parameter α highest_alpha8612000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.811; Stabil: 0.885; Sysdev: 0.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.535

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)