4e0s

Crystal Structure of C5b-6

Method: X-RAY DIFFRACTION Dmax: 208.2 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 × 2 其他Polymer 3 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–1676 Not recorded Complement component C6 × 1 (P13671) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 beta-D-glucopyranose-(1-3)-alpha-L-fucopyranose × 1 NA SODIUM ION × 1 CA CALCIUM ION × 1 MAN alpha-D-mannopyranose × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.6;298 K;0.08M lithium chloride, 0.01M imidazole-HCl, pH 7.6, SMALL TUBES, temperature 298K Resolution 4.21 Å R-free 0.278

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 × 2 其他Polymer 3 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 22–934 Not recorded Complement C5 × 1 (P01031) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 beta-D-glucopyranose-(1-3)-alpha-L-fucopyranose × 1 NA SODIUM ION × 1 CA CALCIUM ION × 1 MAN alpha-D-mannopyranose × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.6;298 K;0.08M lithium chloride, 0.01M imidazole-HCl, pH 7.6, SMALL TUBES, temperature 298K Resolution 4.21 Å R-free 0.278

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 1–913; UniProt 22–934

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 4e0s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4e0s
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id4e0s
Deposition date deposition_date2012-03-05
Structure title titleCrystal Structure of C5b-6
Keywords keywordscomplement, MAC, immune system; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier56.87
Radius of gyration Rg (electron density) rg_electron56.67
Forward intensity I(0) i01117750000.00
Molecular weight molecular_weight277210.0 kDa
Excluded volume excluded_volume346430 ų
Envelope volume envelope_volume554380 ų
Hydration-shell volume shell_volume86856 ų
Envelope diameter envelope_diameter225.3
Shell Rg shell_rg54.46
Envelope Rg envelope_rg56.10
Shape Rg shape_rg56.61
Total Rg total_rg56.82
Total atoms total_atoms19475
Residues n_residues2450
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 dmax208.2
Rg (real space) rg_real57.14
Rg uncertainty (real space) rg_real_error2.47
I(0) (real space) i0_real1.1180e+09
I(0) uncertainty (real space) i0_real_error2.4490e+07
Rg (reciprocal space) rg_reciprocal56.62
I(0) (reciprocal space) i0_reciprocal1117000000.0000
Solution quality estimate total_estimate0.8531
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary59.5
Skewness Skewness skewness0.468
Kurtosis Kurtosis kurtosis-0.159
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha77330000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.754; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.946; Smooth: 0.878

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)