9rbo

A cryo-EM structure of native C3 protein in a compact conformation.

Method: ELECTRON MICROSCOPY Dmax: 144.2 Å Quality: GOOD

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

Complement C3 beta chain

OrganismNot specified

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 homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 32–227 Chain B; UniProt 350–665 Chain C; UniProt 686–734 Chain D; UniProt 762–1663 Not recorded No other associated polymer ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.00 Å

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, 2, 3, 4
Chains and sequence ranges Author chain A; PDBConstruct 1–196; UniProt 32–227 Author chain B; PDBConstruct 1–316; UniProt 350–665 Author chain C; PDBConstruct 1–49; UniProt 686–734 Author chain D; PDBConstruct 1–902; UniProt 762–1663

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 9rbo

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9rbo
Deposition date deposition_date2025-05-27
Structure title titleA cryo-EM structure of native C3 protein in a compact conformation.
Keywords keywordsInhibition Complement Structural Nanoparticle, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier42.54
Radius of gyration Rg (electron density) rg_electron42.00
Forward intensity I(0) i0403137000.00
Molecular weight molecular_weight165070.0 kDa
Excluded volume excluded_volume207080 ų
Envelope volume envelope_volume284790 ų
Hydration-shell volume shell_volume57699 ų
Envelope diameter envelope_diameter147.0
Shell Rg shell_rg46.17
Envelope Rg envelope_rg41.25
Shape Rg shape_rg42.00
Total Rg total_rg42.23
Total atoms total_atoms11606
Residues n_residues1463
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 dmax144.2
Rg (real space) rg_real42.59
Rg uncertainty (real space) rg_real_error1.50
I(0) (real space) i0_real4.0310e+08
I(0) uncertainty (real space) i0_real_error7.2780e+06
Rg (reciprocal space) rg_reciprocal42.54
I(0) (reciprocal space) i0_reciprocal403100000.0000
Solution quality estimate total_estimate0.8788
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary46.8
Skewness Skewness skewness0.332
Kurtosis Kurtosis kurtosis-0.429
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha24890000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.866; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.828

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)