6h03

OPEN CONFORMATION OF THE MEMBRANE ATTACK COMPLEX

Method: ELECTRON MICROSCOPY Dmax: 247.5 Å Quality: EXCELLENT

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

Complement C5,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 × 24 其他Polymer 21 PDB declaration: 24-meric(24) Consistent with protein copy count Chain A; UniProt 19–673 Chain A; UniProt 752–1676 Not recorded Complement component C8 beta chain × 1 (P07358) Complement component C7 × 1 (P10643) Complement component C8 gamma chain × 1 (P07360) Complement component C8 alpha chain × 1 (P07357) Complement component C6 × 1 (P13671) Complement component C9 × 18 (P02748) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 20 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 37 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.60 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 1–655; UniProt 19–673 Author chain A; PDBConstruct 656–1580; UniProt 752–1676

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 × 24 其他Polymer 21 PDB declaration: 24-meric(24) Consistent with protein copy count Chain C; UniProt 55–591 Not recorded Complement C5,Complement C5 × 1 (P01031) Complement component C7 × 1 (P10643) Complement component C8 gamma chain × 1 (P07360) Complement component C8 alpha chain × 1 (P07357) Complement component C6 × 1 (P13671) Complement component C9 × 18 (P02748) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 20 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 37 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.60 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 2
Chains and sequence ranges Author chain C; PDBConstruct 1–537; UniProt 55–591

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 × 24 其他Polymer 21 PDB declaration: 24-meric(24) Consistent with protein copy count Chain D; UniProt 23–843 Not recorded Complement C5,Complement C5 × 1 (P01031) Complement component C8 beta chain × 1 (P07358) Complement component C8 gamma chain × 1 (P07360) Complement component C8 alpha chain × 1 (P07357) Complement component C6 × 1 (P13671) Complement component C9 × 18 (P02748) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 20 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 37 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.60 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 D; PDBConstruct 1–821; UniProt 23–843

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 × 24 其他Polymer 21 PDB declaration: 24-meric(24) Consistent with protein copy count Chain E; UniProt 21–202 Not recorded Complement C5,Complement C5 × 1 (P01031) Complement component C8 beta chain × 1 (P07358) Complement component C7 × 1 (P10643) Complement component C8 alpha chain × 1 (P07357) Complement component C6 × 1 (P13671) Complement component C9 × 18 (P02748) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 20 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 37 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.60 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 4
Chains and sequence ranges Author chain E; PDBConstruct 1–182; UniProt 21–202

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 × 24 其他Polymer 21 PDB declaration: 24-meric(24) Consistent with protein copy count Chain F; UniProt 31–584 Not recorded Complement C5,Complement C5 × 1 (P01031) Complement component C8 beta chain × 1 (P07358) Complement component C7 × 1 (P10643) Complement component C8 gamma chain × 1 (P07360) Complement component C6 × 1 (P13671) Complement component C9 × 18 (P02748) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 20 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 37 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.60 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 F; PDBConstruct 1–554; UniProt 31–584

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 × 24 其他Polymer 21 PDB declaration: 24-meric(24) Consistent with protein copy count Chain B; UniProt 22–934 Not recorded Complement C5,Complement C5 × 1 (P01031) Complement component C8 beta chain × 1 (P07358) Complement component C7 × 1 (P10643) Complement component C8 gamma chain × 1 (P07360) Complement component C8 alpha chain × 1 (P07357) Complement component C9 × 18 (P02748) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 20 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 37 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.60 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 6
Chains and sequence ranges Author chain B; PDBConstruct 1–913; UniProt 22–934

Complement component C9

OrganismNot specified

UniProt P02748

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 × 24 其他Polymer 21 PDB declaration: 24-meric(24) Consistent with protein copy count Chain G; UniProt 22–559 Chain H; UniProt 22–559 Chain I; UniProt 22–559 Chain J; UniProt 22–559 Chain K; UniProt 22–559 Chain L; UniProt 22–559 Chain M; UniProt 22–559 Chain N; UniProt 22–559 Chain O; UniProt 22–559 Chain P; UniProt 22–559 Chain Q; UniProt 22–559 Chain R; UniProt 22–559 Chain S; UniProt 22–559 Chain T; UniProt 22–559 Chain U; UniProt 22–559 Chain V; UniProt 22–559 Chain W; UniProt 22–559 Chain X; UniProt 22–559 Not recorded Complement C5,Complement C5 × 1 (P01031) Complement component C8 beta chain × 1 (P07358) Complement component C7 × 1 (P10643) Complement component C8 gamma chain × 1 (P07360) Complement component C8 alpha chain × 1 (P07357) Complement component C6 × 1 (P13671) beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 20 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 37 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.60 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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CO9_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 1–538; UniProt 22–559 Author chain H; PDBConstruct 1–538; UniProt 22–559 Author chain I; PDBConstruct 1–538; UniProt 22–559 Author chain J; PDBConstruct 1–538; UniProt 22–559 Author chain K; PDBConstruct 1–538; UniProt 22–559 Author chain L; PDBConstruct 1–538; UniProt 22–559 Author chain M; PDBConstruct 1–538; UniProt 22–559 Author chain N; PDBConstruct 1–538; UniProt 22–559 Author chain O; PDBConstruct 1–538; UniProt 22–559 Author chain P; PDBConstruct 1–538; UniProt 22–559 Author chain Q; PDBConstruct 1–538; UniProt 22–559 Author chain R; PDBConstruct 1–538; UniProt 22–559 Author chain S; PDBConstruct 1–538; UniProt 22–559 Author chain T; PDBConstruct 1–538; UniProt 22–559 Author chain U; PDBConstruct 1–538; UniProt 22–559 Author chain V; PDBConstruct 1–538; UniProt 22–559 Author chain W; PDBConstruct 1–538; UniProt 22–559 Author chain X; PDBConstruct 1–538; UniProt 22–559

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 6h03

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6h03
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6h03
Deposition date deposition_date2018-07-06
Structure title titleOPEN CONFORMATION OF THE MEMBRANE ATTACK COMPLEX
Keywords keywordsC5B9, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron99.85
Forward intensity I(0) i030847100000.00
Molecular weight molecular_weight1458900.0 kDa
Excluded volume excluded_volume1807700 ų
Envelope volume envelope_volume4021000 ų
Hydration-shell volume shell_volume331260 ų
Envelope diameter envelope_diameter332.8
Shell Rg shell_rg108.40
Envelope Rg envelope_rg91.44
Shape Rg shape_rg99.84
Total Rg total_rg99.95
Total atoms total_atoms102309
Residues n_residues12776
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 dmax247.5
Rg (real space) rg_real97.99
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real2.9520e+10
I(0) uncertainty (real space) i0_real_error4.2600e+08
Rg (reciprocal space) rg_reciprocal103.70
I(0) (reciprocal space) i0_reciprocal31170000000.0000
Solution quality estimate total_estimate0.9057
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary154.7
Skewness Skewness skewness-0.209
Kurtosis Kurtosis kurtosis-0.747
Angular range angular_range— – 0.0800 −1
Current regularization parameter α current_alpha1.6540
Highest regularization parameter α highest_alpha996500000.0000
Real-space data points n_real_points17
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.999; Stabil: 0.949; Sysdev: 1.000; Positv: 1.000; Valcen: 0.951; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)