8ovb

Human Complement C3b in complex with Trypanosoma brucei ISG65.

Method: ELECTRON MICROSCOPY Dmax: 151.1 Å Quality: GOOD

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

Complement C3f fragment

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 23–664 Chain B; UniProt 749–1663 Not recorded ISG65 G × 1 (A0A8J9S0Z8) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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
Chains and sequence ranges Author chain A; PDBConstruct 1–642; UniProt 23–664 Author chain B; PDBConstruct 1–915; UniProt 749–1663

ISG65 G

Trypanosoma brucei brucei

UniProt A0A8J9S0Z8

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 25–313 Not recorded Complement C3f fragment × 1 (P01024) Complement C3 × 1 (P01024) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A8J9S0Z8_9TRYP
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–289; UniProt 25–313

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 8ovb

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ovb
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ovb
Deposition date deposition_date2023-04-25
Structure title titleHuman Complement C3b in complex with Trypanosoma brucei ISG65.
Keywords keywordsComplement system, parasite virulence, trypanosome surface protein, host-pathogen complex, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier46.63
Radius of gyration Rg (electron density) rg_electron46.40
Forward intensity I(0) i0493918000.00
Molecular weight molecular_weight185370.0 kDa
Excluded volume excluded_volume233000 ų
Envelope volume envelope_volume335140 ų
Hydration-shell volume shell_volume61115 ų
Envelope diameter envelope_diameter162.4
Shell Rg shell_rg49.84
Envelope Rg envelope_rg45.11
Shape Rg shape_rg46.39
Total Rg total_rg46.60
Total atoms total_atoms26116
Residues n_residues1655
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 dmax151.1
Rg (real space) rg_real46.67
Rg uncertainty (real space) rg_real_error1.28
I(0) (real space) i0_real4.9390e+08
I(0) uncertainty (real space) i0_real_error9.6910e+06
Rg (reciprocal space) rg_reciprocal46.63
I(0) (reciprocal space) i0_reciprocal493900000.0000
Solution quality estimate total_estimate0.8866
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary53.3
Skewness Skewness skewness0.265
Kurtosis Kurtosis kurtosis-0.569
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha28960000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.945; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.689

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)