8uin

Structure of the C3bBb-albicin complex

Method: ELECTRON MICROSCOPY Dmax: 189.6 Å Quality: GOOD

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

Albicin

Anopheles albimanus

UniProt A0A1Y9G8D0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 8 其他Polymer 1 PDB declaration: octameric(8) Consistent with protein copy count Chain C; UniProt 27–142 Chain D; UniProt 27–142 Not recorded Complement factor B Bb fragment × 2 (P00751) Complement C3 beta chain × 2 (P01024) ;Complement C3b alpha' chain ; × 2 (P01024) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;10 mM Hepes pH 7.4, 150 mM NaCl, 5 mM MgCl2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.86 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.

2 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A1Y9G8D0_ANOAL
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 1–116; UniProt 27–142 Author chain D; PDBConstruct 1–116; UniProt 27–142

Complement factor B Bb fragment

OrganismNot specified

UniProt P00751

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 8 其他Polymer 1 PDB declaration: octameric(8) Consistent with protein copy count Chain J; UniProt 260–487 Chain X; UniProt 260–487 Not recorded Albicin × 2 (A0A1Y9G8D0) Complement C3 beta chain × 2 (P01024) ;Complement C3b alpha' chain ; × 2 (P01024) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;10 mM Hepes pH 7.4, 150 mM NaCl, 5 mM MgCl2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.86 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.

25 other PDB entries and 44 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CFAB_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain J; PDBConstruct 1–228; UniProt 260–487 Author chain X; PDBConstruct 1–228; UniProt 260–487

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 Other combination Heteromer Protein × 8 其他Polymer 1 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 23–664 Chain B; UniProt 749–1663 Chain G; UniProt 23–664 Chain H; UniProt 749–1663 Not recorded Albicin × 2 (A0A1Y9G8D0) Complement factor B Bb fragment × 2 (P00751) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;10 mM Hepes pH 7.4, 150 mM NaCl, 5 mM MgCl2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.86 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 3, 4
Chains and sequence ranges Author chain A; PDBConstruct 1–642; UniProt 23–664 Author chain G; PDBConstruct 1–642; UniProt 23–664 Author chain B; PDBConstruct 1–915; UniProt 749–1663 Author chain H; PDBConstruct 1–915; UniProt 749–1663

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 8uin

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8uin
Deposition date deposition_date2023-10-10
Structure title titleStructure of the C3bBb-albicin complex
Keywords keywordsComplement, Inhibitor, Mosquito, Convertase, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier59.30
Radius of gyration Rg (electron density) rg_electron58.95
Forward intensity I(0) i02236430000.00
Molecular weight molecular_weight400940.0 kDa
Excluded volume excluded_volume503540 ų
Envelope volume envelope_volume774490 ų
Hydration-shell volume shell_volume111510 ų
Envelope diameter envelope_diameter201.4
Shell Rg shell_rg59.29
Envelope Rg envelope_rg57.93
Shape Rg shape_rg58.99
Total Rg total_rg58.82
Total atoms total_atoms28249
Residues n_residues3746
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 dmax189.6
Rg (real space) rg_real59.32
Rg uncertainty (real space) rg_real_error1.63
I(0) (real space) i0_real2.2360e+09
I(0) uncertainty (real space) i0_real_error4.0620e+07
Rg (reciprocal space) rg_reciprocal59.26
I(0) (reciprocal space) i0_reciprocal2236000000.0000
Solution quality estimate total_estimate0.8571
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary65.6
Skewness Skewness skewness0.352
Kurtosis Kurtosis kurtosis-0.235
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha185900000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.928; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.381

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)