9mbz

Cryo-EM structure of human FcRL4 bound to IgA-Fc/J

Method: ELECTRON MICROSCOPY Dmax: 149.9 Å Quality: REASONABLE

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

Interleukin-2,Fc receptor-like protein 4

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 × 6 其他Polymer 1 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–21 Chain B; UniProt 1–21 Chain C; UniProt 1–21 Chain D; UniProt 1–21 Chain F; UniProt 1–21 Not recorded Immunoglobulin J chain × 1 (P01591) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 1 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.30 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 F; PDBConstruct 1–21; UniProt 1–21 Author chain A; PDBConstruct 1–21; UniProt 1–21 Author chain B; PDBConstruct 1–21; UniProt 1–21 Author chain C; PDBConstruct 1–21; UniProt 1–21 Author chain D; PDBConstruct 1–21; UniProt 1–21

Interleukin-2,Fc receptor-like protein 4

Homo sapiens

UniProt Q96PJ5

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 × 6 其他Polymer 1 PDB declaration: hexameric(6) Consistent with protein copy count Chain F; UniProt 20–387 Not recorded Interleukin-2,Isoform 1 of Immunoglobulin heavy constant alpha 1 × 4 (P60568,P01876) Immunoglobulin J chain × 1 (P01591) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 1 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.30 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name FCRL4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain F; PDBConstruct 25–392; UniProt 20–387

Interleukin-2,Isoform 1 of Immunoglobulin heavy constant alpha 1

Homo sapiens

UniProt P01876

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 × 6 其他Polymer 1 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 122–353 Chain B; UniProt 122–353 Chain C; UniProt 122–353 Chain D; UniProt 122–353 Not recorded Interleukin-2,Fc receptor-like protein 4 × 1 (P60568,Q96PJ5) Immunoglobulin J chain × 1 (P01591) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 1 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.30 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.

14 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGHA1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 60–291; UniProt 122–353 Author chain B; PDBConstruct 60–291; UniProt 122–353 Author chain C; PDBConstruct 60–291; UniProt 122–353 Author chain D; PDBConstruct 60–291; UniProt 122–353

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 × 6 其他Polymer 1 PDB declaration: hexameric(6) Consistent with protein copy count Chain J; UniProt 1–159 Not recorded Interleukin-2,Fc receptor-like protein 4 × 1 (P60568,Q96PJ5) Interleukin-2,Isoform 1 of Immunoglobulin heavy constant alpha 1 × 4 (P60568,P01876) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose × 1 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.30 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 9mbz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9mbz
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9mbz
Deposition date deposition_date2025-03-17
Structure title titleCryo-EM structure of human FcRL4 bound to IgA-Fc/J
Keywords keywordsImmunoglobulin A, Fc receptor, FCRL4, J-chain, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier41.18
Radius of gyration Rg (electron density) rg_electron41.52
Forward intensity I(0) i0265889000.00
Molecular weight molecular_weight132180.0 kDa
Excluded volume excluded_volume165430 ų
Envelope volume envelope_volume233110 ų
Hydration-shell volume shell_volume49328 ų
Envelope diameter envelope_diameter159.2
Shell Rg shell_rg43.10
Envelope Rg envelope_rg42.53
Shape Rg shape_rg41.53
Total Rg total_rg41.60
Total atoms total_atoms9296
Residues n_residues1183
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 dmax149.9
Rg (real space) rg_real41.47
Rg uncertainty (real space) rg_real_error1.79
I(0) (real space) i0_real2.6590e+08
I(0) uncertainty (real space) i0_real_error4.9720e+06
Rg (reciprocal space) rg_reciprocal41.19
I(0) (reciprocal space) i0_reciprocal265800000.0000
Solution quality estimate total_estimate0.6167
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary43.4
Skewness Skewness skewness0.574
Kurtosis Kurtosis kurtosis-0.025
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha22070000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.699; Stabil: 1.000; Sysdev: 0.046; Positv: 1.000; Valcen: 0.914; Smooth: 0.863

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)