7zgj

Trypanosoma brucei gambiense ISG65 in complex with human complement component C3

Method: ELECTRON MICROSCOPY Dmax: 155.0 Å Quality: REASONABLE

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 23–667 Chain B; UniProt 672–1663 Not recorded 65 kDa invariant surface glycoprotein, putative × 1 (C9ZJ67) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.58 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 1–645; UniProt 23–667 Author chain B; PDBConstruct 1–992; UniProt 672–1663

65 kDa invariant surface glycoprotein, putative

Trypanosoma brucei gambiense

UniProt C9ZJ67

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 17–363 Not recorded Complement C3 beta chain × 1 (P01024) Complement C3 × 1 (P01024) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.58 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.

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

View Construct and Data Evidence
UniProt name C9ZJ67_TRYB9
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 21–367; UniProt 17–363

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 7zgj

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7zgj
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7zgj
Deposition date deposition_date2022-04-03
Structure title titleTrypanosoma brucei gambiense ISG65 in complex with human complement component C3
Keywords keywordscomplement, 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_guinier46.24
Radius of gyration Rg (electron density) rg_electron45.80
Forward intensity I(0) i0604785000.00
Molecular weight molecular_weight203460.0 kDa
Excluded volume excluded_volume255530 ų
Envelope volume envelope_volume384540 ų
Hydration-shell volume shell_volume71545 ų
Envelope diameter envelope_diameter163.6
Shell Rg shell_rg48.62
Envelope Rg envelope_rg45.27
Shape Rg shape_rg45.80
Total Rg total_rg45.96
Total atoms total_atoms14314
Residues n_residues1805
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 dmax155.0
Rg (real space) rg_real46.25
Rg uncertainty (real space) rg_real_error1.47
I(0) (real space) i0_real6.0480e+08
I(0) uncertainty (real space) i0_real_error1.1790e+07
Rg (reciprocal space) rg_reciprocal46.24
I(0) (reciprocal space) i0_reciprocal604800000.0000
Solution quality estimate total_estimate0.6562
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary54.7
Skewness Skewness skewness0.334
Kurtosis Kurtosis kurtosis-0.298
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha51490000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.881; Stabil: 1.000; Sysdev: 0.021; Positv: 1.000; Valcen: 0.998; Smooth: 0.822

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id7zgjB01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology91 — Influenza Virus Matrix Protein; Chain A, domain 1
Homologous superfamily homologous superfamily20 — Anaphylotoxins (complement system)
Domain ID domain_id7zgjB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7zgjB03
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily120

8. Citations (1)

9. Files and Curves (10)