8e4c

IgM BCR fab truncated form

Method: ELECTRON MICROSCOPY Dmax: 139.4 Å Quality: GOOD

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

Isoform 2 of Immunoglobulin heavy constant mu

Mus musculus

UniProt P01872

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 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 105–475 Chain B; UniProt 105–475 Not recorded B-cell antigen receptor complex-associated protein alpha chain,Yellow fluorescent protein × 1 (P11911,P21578) B-cell antigen receptor complex-associated protein beta chain × 1 (P15530) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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.

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

View Construct and Data Evidence
UniProt name IGHM_MOUSE
Isoform P01872-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 47–417; UniProt 105–475 Author chain B; PDBConstruct 47–417; UniProt 105–475

B-cell antigen receptor complex-associated protein alpha chain,Yellow fluorescent protein

Mus musculus

UniProt P11911

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 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–169 Not recorded Isoform 2 of Immunoglobulin heavy constant mu × 2 (P01872) B-cell antigen receptor complex-associated protein beta chain × 1 (P15530) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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 CD79A_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 9–177; UniProt 1–169

B-cell antigen receptor complex-associated protein alpha chain,Yellow fluorescent protein

Mus musculus

UniProt P21578

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 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–194 Not recorded Isoform 2 of Immunoglobulin heavy constant mu × 2 (P01872) B-cell antigen receptor complex-associated protein beta chain × 1 (P15530) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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 LUXY_ALIFS
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 185–378; UniProt 1–194

B-cell antigen receptor complex-associated protein beta chain

Mus musculus

UniProt P15530

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 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 1–228 Not recorded Isoform 2 of Immunoglobulin heavy constant mu × 2 (P01872) B-cell antigen receptor complex-associated protein alpha chain,Yellow fluorescent protein × 1 (P11911,P21578) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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 CD79B_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–228; UniProt 1–228

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 8e4c

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8e4c
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8e4c
Deposition date deposition_date2022-08-18
Structure title titleIgM BCR fab truncated form
Keywords keywordscomplex, membrane protein, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.72
Radius of gyration Rg (electron density) rg_electron38.33
Forward intensity I(0) i0124074000.00
Molecular weight molecular_weight90702.0 kDa
Excluded volume excluded_volume114280 ų
Envelope volume envelope_volume172740 ų
Hydration-shell volume shell_volume41336 ų
Envelope diameter envelope_diameter147.1
Shell Rg shell_rg39.43
Envelope Rg envelope_rg39.11
Shape Rg shape_rg38.33
Total Rg total_rg38.43
Total atoms total_atoms6398
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 dmax139.4
Rg (real space) rg_real38.11
Rg uncertainty (real space) rg_real_error1.72
I(0) (real space) i0_real1.2410e+08
I(0) uncertainty (real space) i0_real_error2.3520e+06
Rg (reciprocal space) rg_reciprocal37.87
I(0) (reciprocal space) i0_reciprocal124000000.0000
Solution quality estimate total_estimate0.8244
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary43.2
Skewness Skewness skewness0.598
Kurtosis Kurtosis kurtosis0.077
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12150000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.670; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.862; Smooth: 0.840

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)