8r83

pentameric IgMFc-AIM complex global refinement

Method: ELECTRON MICROSCOPY Dmax: 182.4 Å Quality: GOOD

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

CD5 antigen-like

Homo sapiens

UniProt O43866

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 × 12 其他Polymer 1 PDB declaration: 12-meric(12) Consistent with protein copy count Chain N; UniProt 20–347 Not recorded Ig-like domain-containing protein × 10 (A0A7N5JWI9) Immunoglobulin J chain × 1 (P01591) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.57 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CD5L_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain N; PDBConstruct 1–328; UniProt 20–347

Ig-like domain-containing protein

Homo sapiens

UniProt A0A7N5JWI9

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 × 12 其他Polymer 1 PDB declaration: 12-meric(12) Consistent with protein copy count Chain A; UniProt 106–453 Chain B; UniProt 106–453 Chain C; UniProt 106–453 Chain D; UniProt 106–453 Chain E; UniProt 106–453 Chain F; UniProt 106–453 Chain G; UniProt 106–453 Chain H; UniProt 106–453 Chain K; UniProt 106–453 Chain L; UniProt 106–453 Not recorded CD5 antigen-like × 1 (O43866) Immunoglobulin J chain × 1 (P01591) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.57 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A7N5JWI9_AILME
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 14–361; UniProt 106–453 Author chain B; PDBConstruct 14–361; UniProt 106–453 Author chain C; PDBConstruct 14–361; UniProt 106–453 Author chain D; PDBConstruct 14–361; UniProt 106–453 Author chain E; PDBConstruct 14–361; UniProt 106–453 Author chain F; PDBConstruct 14–361; UniProt 106–453 Author chain G; PDBConstruct 14–361; UniProt 106–453 Author chain H; PDBConstruct 14–361; UniProt 106–453 Author chain K; PDBConstruct 14–361; UniProt 106–453 Author chain L; PDBConstruct 14–361; UniProt 106–453

Immunoglobulin J chain

Homo sapiens

UniProt P01591

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 × 12 其他Polymer 1 PDB declaration: 12-meric(12) Consistent with protein copy count Chain J; UniProt 1–159 Not recorded CD5 antigen-like × 1 (O43866) Ig-like domain-containing protein × 10 (A0A7N5JWI9) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CA CALCIUM ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.57 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.

23 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGJ_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain J; PDBConstruct 1–159; UniProt 1–159

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 8r83

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8r83
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8r83
Deposition date deposition_date2023-11-28
Structure title titlepentameric IgMFc-AIM complex global refinement
Keywords keywordsScavenger Receptor Cysteine-Rich, IgM, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier58.82
Radius of gyration Rg (electron density) rg_electron58.73
Forward intensity I(0) i01248420000.00
Molecular weight molecular_weight290540.0 kDa
Excluded volume excluded_volume361530 ų
Envelope volume envelope_volume613770 ų
Hydration-shell volume shell_volume88033 ų
Envelope diameter envelope_diameter192.9
Shell Rg shell_rg58.14
Envelope Rg envelope_rg58.03
Shape Rg shape_rg58.75
Total Rg total_rg58.65
Total atoms total_atoms20415
Residues n_residues2608
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 dmax182.4
Rg (real space) rg_real58.89
Rg uncertainty (real space) rg_real_error1.78
I(0) (real space) i0_real1.2480e+09
I(0) uncertainty (real space) i0_real_error2.9320e+07
Rg (reciprocal space) rg_reciprocal58.73
I(0) (reciprocal space) i0_reciprocal1248000000.0000
Solution quality estimate total_estimate0.8421
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary67.6
Skewness Skewness skewness0.283
Kurtosis Kurtosis kurtosis-0.566
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha127100000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.973; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.026

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)