8ema

mouse full length B cell receptor

Method: ELECTRON MICROSCOPY Dmax: 233.5 Å Quality: GOOD

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

Isoform 2 of Immunoglobulin heavy constant mu

Mus musculus

UniProt P01872-2

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 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–475 Chain B; UniProt 1–475 Not recorded Anti-human Langerin 2G3 lambda chain × 2 (G0YP42) B-cell antigen receptor complex-associated protein alpha chain × 1 (P11911,P21578) B-cell antigen receptor complex-associated protein beta chain × 1 (P15530) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.20 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 IGHM_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 141–615; UniProt 1–475 Author chain B; PDBConstruct 141–615; UniProt 1–475

Isoform 2 of Immunoglobulin heavy constant mu

Mus musculus

UniProt P06328

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 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–117 Chain B; UniProt 1–117 Not recorded Anti-human Langerin 2G3 lambda chain × 2 (G0YP42) B-cell antigen receptor complex-associated protein alpha chain × 1 (P11911,P21578) B-cell antigen receptor complex-associated protein beta chain × 1 (P15530) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.20 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 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HVM49_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–117; UniProt 1–117 Author chain B; PDBConstruct 1–117; UniProt 1–117

Anti-human Langerin 2G3 lambda chain

Mus musculus

UniProt G0YP42

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 PDB declaration: hexameric(6) Consistent with protein copy count Chain L; UniProt 1–234 Chain R; UniProt 1–234 Not recorded Isoform 2 of Immunoglobulin heavy constant mu × 2 (P06328,P01872-2) B-cell antigen receptor complex-associated protein alpha chain × 1 (P11911,P21578) B-cell antigen receptor complex-associated protein beta chain × 1 (P15530) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.20 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.

5 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name G0YP42_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain L; PDBConstruct 1–234; UniProt 1–234 Author chain R; PDBConstruct 1–234; UniProt 1–234

B-cell antigen receptor complex-associated protein alpha chain

Aliivibrio fischeri

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 1–172 Not recorded Isoform 2 of Immunoglobulin heavy constant mu × 2 (P06328,P01872-2) Anti-human Langerin 2G3 lambda chain × 2 (G0YP42) B-cell antigen receptor complex-associated protein beta chain × 1 (P15530) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.20 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 3
Chains and sequence ranges Author chain C; PDBConstruct 9–180; UniProt 1–172

B-cell antigen receptor complex-associated protein alpha chain

Aliivibrio fischeri

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 1–194 Not recorded Isoform 2 of Immunoglobulin heavy constant mu × 2 (P06328,P01872-2) Anti-human Langerin 2G3 lambda chain × 2 (G0YP42) B-cell antigen receptor complex-associated protein beta chain × 1 (P15530) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.20 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 3
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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain D; UniProt 1–228 Not recorded Isoform 2 of Immunoglobulin heavy constant mu × 2 (P06328,P01872-2) Anti-human Langerin 2G3 lambda chain × 2 (G0YP42) B-cell antigen receptor complex-associated protein alpha chain × 1 (P11911,P21578) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.20 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 4
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 8ema

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ema
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8ema
Deposition date deposition_date2022-09-27
Structure title titlemouse full length B cell receptor
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_guinier68.70
Radius of gyration Rg (electron density) rg_electron70.26
Forward intensity I(0) i0629881000.00
Molecular weight molecular_weight211040.0 kDa
Excluded volume excluded_volume264560 ų
Envelope volume envelope_volume471490 ų
Hydration-shell volume shell_volume64894 ų
Envelope diameter envelope_diameter252.8
Shell Rg shell_rg55.49
Envelope Rg envelope_rg67.16
Shape Rg shape_rg70.31
Total Rg total_rg69.67
Total atoms total_atoms14871
Residues n_residues1911
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 dmax233.5
Rg (real space) rg_real69.24
Rg uncertainty (real space) rg_real_error2.92
I(0) (real space) i0_real6.2980e+08
I(0) uncertainty (real space) i0_real_error1.4740e+07
Rg (reciprocal space) rg_reciprocal66.62
I(0) (reciprocal space) i0_reciprocal626800000.0000
Solution quality estimate total_estimate0.7680
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary50.8
Skewness Skewness skewness0.514
Kurtosis Kurtosis kurtosis-0.466
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha22940000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.692; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.612; Smooth: 0.295

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)