2icf

CRIg bound to C3b

Method: X-RAY DIFFRACTION Dmax: 154.5 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 × 3 其他Polymer 1 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 23–664 Chain B; UniProt 749–1663 Not recorded V-set and immunoglobulin domain-containing protein 4 × 1 (Q9Y279) ;beta-D-mannopyranose-(1-4)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 CA CALCIUM ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 6.5;293 K;pH 6.5, EVAPORATION, temperature 293K Resolution 4.10 Å R-free 0.330

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 1–642; UniProt 23–664 Author chain B; PDBConstruct 1–915; UniProt 749–1663

V-set and immunoglobulin domain-containing protein 4

Homo sapiens

UniProt Q9Y279

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 × 3 其他Polymer 1 PDB declaration: trimeric(3) Consistent with protein copy count Chain S; UniProt 19–137 Not recorded Complement C3 beta chain × 1 (P01024) Complement C3 alpha chain × 1 (P01024) ;beta-D-mannopyranose-(1-4)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 1 CA CALCIUM ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 6.5;293 K;pH 6.5, EVAPORATION, temperature 293K Resolution 4.10 Å R-free 0.330

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.

11 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VSIG4_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain S; PDBConstruct 1–119; UniProt 19–137

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 2icf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2icf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2icf
Deposition date deposition_date2006-09-12
Structure title titleCRIg bound to C3b
Keywords keywordsAlternate Pathway, Complement, C3, C3b, CRIg, Complement Receptor, 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_guinier45.45
Radius of gyration Rg (electron density) rg_electron45.19
Forward intensity I(0) i0514290000.00
Molecular weight molecular_weight188120.0 kDa
Excluded volume excluded_volume236330 ų
Envelope volume envelope_volume339870 ų
Hydration-shell volume shell_volume64423 ų
Envelope diameter envelope_diameter170.2
Shell Rg shell_rg48.29
Envelope Rg envelope_rg44.55
Shape Rg shape_rg45.18
Total Rg total_rg45.37
Total atoms total_atoms13236
Residues n_residues1664
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 dmax154.5
Rg (real space) rg_real45.61
Rg uncertainty (real space) rg_real_error1.09
I(0) (real space) i0_real5.1430e+08
I(0) uncertainty (real space) i0_real_error9.3120e+06
Rg (reciprocal space) rg_reciprocal45.45
I(0) (reciprocal space) i0_reciprocal514200000.0000
Solution quality estimate total_estimate0.8711
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary53.0
Skewness Skewness skewness0.402
Kurtosis Kurtosis kurtosis-0.367
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0003
Highest regularization parameter α highest_alpha50560000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.868; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.939; Smooth: 0.777

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)