6rv6

Structure of properdin lacking TSR3 based on anomalous data

Method: X-RAY DIFFRACTION Dmax: 126.0 Å Quality: GOOD

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

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 Homooligomer Protein × 2 其他Polymer 4 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 28–191 Chain B; UniProt 256–469 Not recorded beta-D-glucopyranose-(1-3)-alpha-L-fucopyranose × 3 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 1 MAN alpha-D-mannopyranose × 12 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4;292 K;1.0 M lithium sulfate, 0.1 M sodium acetate pH 4.0, 0.1 M barium chloride Resolution 3.51 Å R-free 0.283

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 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–164; UniProt 28–191 Author chain B; PDBConstruct 2–215; UniProt 256–469

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 6rv6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6rv6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6rv6
Deposition date deposition_date2019-05-31
Structure title titleStructure of properdin lacking TSR3 based on anomalous data
Keywords keywordsinnate immunity, complement, protease, regulator, 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_guinier37.06
Radius of gyration Rg (electron density) rg_electron37.39
Forward intensity I(0) i040434400.00
Molecular weight molecular_weight45931.0 kDa
Excluded volume excluded_volume55807 ų
Envelope volume envelope_volume93786 ų
Hydration-shell volume shell_volume24508 ų
Envelope diameter envelope_diameter134.1
Shell Rg shell_rg36.55
Envelope Rg envelope_rg37.43
Shape Rg shape_rg37.37
Total Rg total_rg37.39
Total atoms total_atoms3191
Residues n_residues385
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 dmax126.0
Rg (real space) rg_real37.44
Rg uncertainty (real space) rg_real_error1.60
I(0) (real space) i0_real4.0430e+07
I(0) uncertainty (real space) i0_real_error6.8510e+05
Rg (reciprocal space) rg_reciprocal37.21
I(0) (reciprocal space) i0_reciprocal40430000.0000
Solution quality estimate total_estimate0.8383
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.0
Skewness Skewness skewness0.398
Kurtosis Kurtosis kurtosis-0.596
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1350000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.813; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.636; Smooth: 0.818

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (3)

9. Files and Curves (10)