7noz

Structure of the nanobody stablized properdin bound alternative pathway proconvertase C3b:FB:FP

Method: X-RAY DIFFRACTION Dmax: 227.6 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 × 6 其他Polymer 8 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 23–667 Chain B; UniProt 752–1663 Not recorded Properdin × 1 (P27918) Properdin × 1 (P27918) Complement factor B × 1 (P00751) hFPNb1 nanobody × 1 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 beta-D-glucopyranose-(1-3)-alpha-L-fucopyranose × 3 ;alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 MAN alpha-D-mannopyranose × 6 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.05 M Na-acetate pH 5.3, 0.1 M Mg-formate,7% PEG5000 MME Resolution 3.90 Å R-free 0.265

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 A; PDBConstruct 1–645; UniProt 23–667 Author chain B; PDBConstruct 1–912; UniProt 752–1663

Properdin

Homo sapiens

UniProt P27918

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 × 6 其他Polymer 8 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 28–190 Chain D; UniProt 255–461 Not recorded Complement C3 beta chain × 1 (P01024) Complement C3 alpha chain × 1 (P01024) Complement factor B × 1 (P00751) hFPNb1 nanobody × 1 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 beta-D-glucopyranose-(1-3)-alpha-L-fucopyranose × 3 ;alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 MAN alpha-D-mannopyranose × 6 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.05 M Na-acetate pH 5.3, 0.1 M Mg-formate,7% PEG5000 MME Resolution 3.90 Å R-free 0.265

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.

13 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PROP_HUMAN
Isoform
PDB entities 3, 4
Chains and sequence ranges Author chain C; PDBConstruct 1–163; UniProt 28–190 Author chain D; PDBConstruct 1–207; UniProt 255–461

Complement factor B

Homo sapiens

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 × 6 其他Polymer 8 PDB declaration: hexameric(6) Consistent with protein copy count Chain F; UniProt 35–764 Mutation:D279G Complement C3 beta chain × 1 (P01024) Complement C3 alpha chain × 1 (P01024) Properdin × 1 (P27918) Properdin × 1 (P27918) hFPNb1 nanobody × 1 beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 3 beta-D-glucopyranose-(1-3)-alpha-L-fucopyranose × 3 ;alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 MAN alpha-D-mannopyranose × 6 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.05 M Na-acetate pH 5.3, 0.1 M Mg-formate,7% PEG5000 MME Resolution 3.90 Å R-free 0.265

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 5
Chains and sequence ranges Author chain F; PDBConstruct 1–730; UniProt 35–764

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 7noz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7noz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7noz
Deposition date deposition_date2021-02-26
Structure title titleStructure of the nanobody stablized properdin bound alternative pathway proconvertase C3b:FB:FP
Keywords keywordsprotease, complement, cascade, proconvertase, 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_guinier60.31
Radius of gyration Rg (electron density) rg_electron60.97
Forward intensity I(0) i01453690000.00
Molecular weight molecular_weight313280.0 kDa
Excluded volume excluded_volume390380 ų
Envelope volume envelope_volume630660 ų
Hydration-shell volume shell_volume94124 ų
Envelope diameter envelope_diameter259.5
Shell Rg shell_rg54.40
Envelope Rg envelope_rg62.95
Shape Rg shape_rg60.91
Total Rg total_rg61.00
Total atoms total_atoms21992
Residues n_residues2754
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 dmax227.6
Rg (real space) rg_real61.19
Rg uncertainty (real space) rg_real_error3.00
I(0) (real space) i0_real1.4520e+09
I(0) uncertainty (real space) i0_real_error3.1680e+07
Rg (reciprocal space) rg_reciprocal59.40
I(0) (reciprocal space) i0_reciprocal1449000000.0000
Solution quality estimate total_estimate0.7987
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary61.3
Skewness Skewness skewness0.793
Kurtosis Kurtosis kurtosis0.354
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0169
Highest regularization parameter α highest_alpha112700000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.520; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.944; Smooth: 0.873

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (13)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id7nozB01
Class class2 — Mainly Beta
Architecture architecture20 — Single Sheet
Topology topology130 — S-adenosyl-L-methionine-dependent methyltransferases
Homologous superfamily homologous superfamily20
Domain ID domain_id7nozB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id7nozB03
Class class1 — Mainly Alpha
Architecture architecture50 — Alpha/alpha barrel
Topology topology10 — Glycosyltransferase
Homologous superfamily homologous superfamily20
Domain ID domain_id7nozB04
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily120
Domain ID domain_id7nozC01
Class class2 — Mainly Beta
Architecture architecture20 — Single Sheet
Topology topology100 — TSP-1 type 1 repeat
Homologous superfamily homologous superfamily10 — Thrombospondin type-1 (TSP1) repeat
Domain ID domain_id7nozR01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)