8wys

Local map of human CD5L bound to IgM-Fc/J

Method: ELECTRON MICROSCOPY Dmax: 136.0 Å Quality: GOOD

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

Interleukin-2,Isoform 1 of Immunoglobulin heavy constant mu

Homo sapiens

UniProt P01871

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 4 其他Polymer 1 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 106–453 Chain L; UniProt 106–453 Not recorded Interleukin-2,CD5 antigen-like × 1 (P60568,O43866) Immunoglobulin J chain × 1 (P01591) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CA CALCIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.41 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.

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGHM_HUMAN
Isoform P01871-1
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 56–403; UniProt 106–453 Author chain L; PDBConstruct 56–403; UniProt 106–453

Interleukin-2,Isoform 1 of Immunoglobulin heavy constant mu

Homo sapiens

UniProt P60568

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 4 其他Polymer 1 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–21 Chain L; UniProt 1–21 Chain M; UniProt 1–21 Not recorded Immunoglobulin J chain × 1 (P01591) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CA CALCIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.41 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.

33 other PDB entries and 77 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IL2_HUMAN
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–21; UniProt 1–21 Author chain L; PDBConstruct 1–21; UniProt 1–21 Author chain M; PDBConstruct 1–21; UniProt 1–21

Interleukin-2,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 Insufficient information Heteromer Protein × 4 其他Polymer 1 PDB declaration: tetrameric(4) Consistent with protein copy count Chain M; UniProt 20–347 Not recorded Interleukin-2,Isoform 1 of Immunoglobulin heavy constant mu × 2 (P60568,P01871) Immunoglobulin J chain × 1 (P01591) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CA CALCIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.41 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 2
Chains and sequence ranges Author chain M; PDBConstruct 32–359; UniProt 20–347

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 Insufficient information Heteromer Protein × 4 其他Polymer 1 PDB declaration: tetrameric(4) Consistent with protein copy count Chain J; UniProt 1–159 Not recorded Interleukin-2,Isoform 1 of Immunoglobulin heavy constant mu × 2 (P60568,P01871) Interleukin-2,CD5 antigen-like × 1 (P60568,O43866) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 CA CALCIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.41 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 8wys

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8wys
Deposition date deposition_date2023-10-31
Structure title titleLocal map of human CD5L bound to IgM-Fc/J
Keywords keywordsimmunoglobulin, CD5 antigen-like, pentamer, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.76
Radius of gyration Rg (electron density) rg_electron38.32
Forward intensity I(0) i0135981000.00
Molecular weight molecular_weight90498.0 kDa
Excluded volume excluded_volume111880 ų
Envelope volume envelope_volume160480 ų
Hydration-shell volume shell_volume37634 ų
Envelope diameter envelope_diameter143.2
Shell Rg shell_rg40.58
Envelope Rg envelope_rg38.39
Shape Rg shape_rg38.37
Total Rg total_rg38.31
Total atoms total_atoms6340
Residues n_residues805
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 dmax136.0
Rg (real space) rg_real38.20
Rg uncertainty (real space) rg_real_error2.03
I(0) (real space) i0_real1.3600e+08
I(0) uncertainty (real space) i0_real_error2.8370e+06
Rg (reciprocal space) rg_reciprocal37.93
I(0) (reciprocal space) i0_reciprocal135900000.0000
Solution quality estimate total_estimate0.8357
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.9
Skewness Skewness skewness0.577
Kurtosis Kurtosis kurtosis-0.160
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7805000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.693; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.831; Smooth: 0.952

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)