8enu

Structure of the C3bB proconvertase in complex with lufaxin

Method: ELECTRON MICROSCOPY Dmax: 157.3 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 Other combination Heteromer Protein × 4 其他Polymer 3 PDB declaration: tetrameric(4) Consistent with protein copy count Chain G; UniProt 23–667 Chain H; UniProt 749–1663 Not recorded Complement factor B × 1 (P00751) Lufaxin × 1 (Q5WPU8) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.22 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 G; PDBConstruct 1–645; UniProt 23–667 Author chain H; PDBConstruct 1–915; UniProt 749–1663

Complement factor B

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 × 4 其他Polymer 3 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 2–764 Not recorded Complement C3 beta chain × 1 (P01024) ;Complement C3b alpha' chain ; × 1 (P01024) Lufaxin × 1 (Q5WPU8) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.22 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 3
Chains and sequence ranges Author chain D; PDBConstruct 1–763; UniProt 2–764

Lufaxin

Lutzomyia longipalpis

UniProt Q5WPU8

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 × 4 其他Polymer 3 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 24–301 Not recorded Complement C3 beta chain × 1 (P01024) ;Complement C3b alpha' chain ; × 1 (P01024) Complement factor B × 1 (P00751) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.22 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 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LUFX_LUTLO
Isoform
PDB entities 4
Chains and sequence ranges Author chain A; PDBConstruct 1–278; UniProt 24–301

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 8enu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8enu
Deposition date deposition_date2022-09-30
Structure title titleStructure of the C3bB proconvertase in complex with lufaxin
Keywords keywordsComplement, Alternative pathway, inhibitor, sand fly, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier48.75
Radius of gyration Rg (electron density) rg_electron48.30
Forward intensity I(0) i01174160000.00
Molecular weight molecular_weight285740.0 kDa
Excluded volume excluded_volume358070 ų
Envelope volume envelope_volume527850 ų
Hydration-shell volume shell_volume89628 ų
Envelope diameter envelope_diameter162.2
Shell Rg shell_rg53.73
Envelope Rg envelope_rg47.27
Shape Rg shape_rg48.30
Total Rg total_rg48.49
Total atoms total_atoms20103
Residues n_residues2510
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 dmax157.3
Rg (real space) rg_real48.54
Rg uncertainty (real space) rg_real_error1.19
I(0) (real space) i0_real1.1740e+09
I(0) uncertainty (real space) i0_real_error2.1460e+07
Rg (reciprocal space) rg_reciprocal48.74
I(0) (reciprocal space) i0_reciprocal1174000000.0000
Solution quality estimate total_estimate0.8978
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary59.0
Skewness Skewness skewness0.173
Kurtosis Kurtosis kurtosis-0.582
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha109900000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.921; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.912

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id8enuH01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id8enuH02
Class class1 — Mainly Alpha
Architecture architecture50 — Alpha/alpha barrel
Topology topology10 — Glycosyltransferase
Homologous superfamily homologous superfamily20
Domain ID domain_id8enuH03
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)