9n1z

Structure of C3d Bound to a Fragment of FHR-2

Method: X-RAY DIFFRACTION Dmax: 119.8 Å Quality: GOOD

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 996–1287 Mutation:C1010A Complement factor H-related protein 2 × 1 (P36980) SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.075 M HEPES [PH 7.5] 1.2 M Ammonium Sulfate Resolution 2.31 Å R-free 0.227
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 996–1287 Mutation:C1010A Complement factor H-related protein 2 × 1 (P36980) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.075 M HEPES [PH 7.5] 1.2 M Ammonium Sulfate Resolution 2.31 Å R-free 0.227

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 116 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 Author chain C; PDBConstruct 6–297; UniProt 996–1287

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 145–270 Not recorded Complement C3dg fragment × 1 (P01024) SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.075 M HEPES [PH 7.5] 1.2 M Ammonium Sulfate Resolution 2.31 Å R-free 0.227
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 145–270 Not recorded Complement C3dg fragment × 1 (P01024) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.075 M HEPES [PH 7.5] 1.2 M Ammonium Sulfate Resolution 2.31 Å R-free 0.227

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 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FHR2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 6–131; UniProt 145–270 Author chain D; 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 9n1z

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9n1z
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9n1z
Deposition date deposition_date2025-01-27
Structure title titleStructure of C3d Bound to a Fragment of FHR-2
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_guinier35.34
Radius of gyration Rg (electron density) rg_electron35.13
Forward intensity I(0) i0132361000.00
Molecular weight molecular_weight92669.0 kDa
Excluded volume excluded_volume116200 ų
Envelope volume envelope_volume152710 ų
Hydration-shell volume shell_volume38050 ų
Envelope diameter envelope_diameter129.5
Shell Rg shell_rg39.27
Envelope Rg envelope_rg34.98
Shape Rg shape_rg35.13
Total Rg total_rg35.42
Total atoms total_atoms6513
Residues n_residues823
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 dmax119.8
Rg (real space) rg_real35.52
Rg uncertainty (real space) rg_real_error1.12
I(0) (real space) i0_real1.3240e+08
I(0) uncertainty (real space) i0_real_error2.4350e+06
Rg (reciprocal space) rg_reciprocal35.41
I(0) (reciprocal space) i0_reciprocal132300000.0000
Solution quality estimate total_estimate0.8721
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.3
Skewness Skewness skewness0.461
Kurtosis Kurtosis kurtosis-0.287
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14550000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.862; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.921; Smooth: 0.826

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)