8b0f

CryoEM structure of C5b8-CD59

Method: ELECTRON MICROSCOPY Dmax: 213.7 Å Quality: GOOD

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

Complement C5

OrganismNot specified

UniProt P01031

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 × 7 其他Polymer 3 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 1–1676 Not recorded Complement component C6 × 1 (P13671) Complement component C7 × 1 (P10643) Complement component C8 beta chain × 1 (P07358) Complement component C8 alpha chain × 1 (P07357) Complement component C8 gamma chain × 1 (P07360) CD59 glycoprotein × 1 (P13987) 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 CA CALCIUM ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE 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.

41 other PDB entries and 63 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CO5_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1676; UniProt 1–1676

Complement component C6

OrganismNot specified

UniProt P13671

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 × 7 其他Polymer 3 PDB declaration: heptameric(7) Consistent with protein copy count Chain B; UniProt 1–934 Not recorded Complement C5 × 1 (P01031) Complement component C7 × 1 (P10643) Complement component C8 beta chain × 1 (P07358) Complement component C8 alpha chain × 1 (P07357) Complement component C8 gamma chain × 1 (P07360) CD59 glycoprotein × 1 (P13987) 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 CA CALCIUM ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE 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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CO6_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–934; UniProt 1–934

Complement component C7

OrganismNot specified

UniProt P10643

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 × 7 其他Polymer 3 PDB declaration: heptameric(7) Consistent with protein copy count Chain C; UniProt 1–843 Not recorded Complement C5 × 1 (P01031) Complement component C6 × 1 (P13671) Complement component C8 beta chain × 1 (P07358) Complement component C8 alpha chain × 1 (P07357) Complement component C8 gamma chain × 1 (P07360) CD59 glycoprotein × 1 (P13987) 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 CA CALCIUM ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CO7_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–843; UniProt 1–843

Complement component C8 beta chain

OrganismNot specified

UniProt P07358

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 × 7 其他Polymer 3 PDB declaration: heptameric(7) Consistent with protein copy count Chain D; UniProt 1–591 Not recorded Complement C5 × 1 (P01031) Complement component C6 × 1 (P13671) Complement component C7 × 1 (P10643) Complement component C8 alpha chain × 1 (P07357) Complement component C8 gamma chain × 1 (P07360) CD59 glycoprotein × 1 (P13987) 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 CA CALCIUM ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CO8B_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–591; UniProt 1–591

Complement component C8 alpha chain

OrganismNot specified

UniProt P07357

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 × 7 其他Polymer 3 PDB declaration: heptameric(7) Consistent with protein copy count Chain E; UniProt 1–584 Not recorded Complement C5 × 1 (P01031) Complement component C6 × 1 (P13671) Complement component C7 × 1 (P10643) Complement component C8 beta chain × 1 (P07358) Complement component C8 gamma chain × 1 (P07360) CD59 glycoprotein × 1 (P13987) 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 CA CALCIUM ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE 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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CO8A_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–584; UniProt 1–584

Complement component C8 gamma chain

OrganismNot specified

UniProt P07360

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 × 7 其他Polymer 3 PDB declaration: heptameric(7) Consistent with protein copy count Chain F; UniProt 1–202 Not recorded Complement C5 × 1 (P01031) Complement component C6 × 1 (P13671) Complement component C7 × 1 (P10643) Complement component C8 beta chain × 1 (P07358) Complement component C8 alpha chain × 1 (P07357) CD59 glycoprotein × 1 (P13987) 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 CA CALCIUM ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE 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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CO8G_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 1–202; UniProt 1–202

CD59 glycoprotein

Escherichia coli

UniProt P13987

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 × 7 其他Polymer 3 PDB declaration: heptameric(7) Consistent with protein copy count Chain G; UniProt 1–120 Not recorded Complement C5 × 1 (P01031) Complement component C6 × 1 (P13671) Complement component C7 × 1 (P10643) Complement component C8 beta chain × 1 (P07358) Complement component C8 alpha chain × 1 (P07357) Complement component C8 gamma chain × 1 (P07360) 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 CA CALCIUM ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE 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.

16 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CD59_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 1–120; UniProt 1–120

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 8b0f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8b0f
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8b0f
Deposition date deposition_date2022-09-07
Structure title titleCryoEM structure of C5b8-CD59
Keywords keywordsComplement, inhibitor, complex, pore-forming, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier62.87
Radius of gyration Rg (electron density) rg_electron63.86
Forward intensity I(0) i02905260000.00
Molecular weight molecular_weight440580.0 kDa
Excluded volume excluded_volume546230 ų
Envelope volume envelope_volume826960 ų
Hydration-shell volume shell_volume115080 ų
Envelope diameter envelope_diameter252.1
Shell Rg shell_rg57.94
Envelope Rg envelope_rg64.51
Shape Rg shape_rg63.81
Total Rg total_rg63.89
Total atoms total_atoms60746
Residues n_residues3910
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 dmax213.7
Rg (real space) rg_real63.10
Rg uncertainty (real space) rg_real_error1.86
I(0) (real space) i0_real2.8960e+09
I(0) uncertainty (real space) i0_real_error5.9980e+07
Rg (reciprocal space) rg_reciprocal62.19
I(0) (reciprocal space) i0_reciprocal2898000000.0000
Solution quality estimate total_estimate0.8505
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary68.4
Skewness Skewness skewness0.655
Kurtosis Kurtosis kurtosis0.150
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0372
Highest regularization parameter α highest_alpha286800000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.776; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.721

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

8. Citations (2)

9. Files and Curves (10)