7xq8

Structure of human B-cell antigen receptor of the IgM isotype

Method: ELECTRON MICROSCOPY Dmax: 213.2 Å Quality: GOOD

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

Chimera of Heavy chain of VRC01 antibody Fab and Isoform 2 of Immunoglobulin heavy constant mu

Homo sapiens

UniProt P01871-2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 1–474 Chain v; UniProt 1–474 Not recorded Light chain of Fab fragments of the VRC01 antibody,Immunoglobulin kappa constant × 2 (P01834) B-cell antigen receptor complex-associated protein alpha chain × 1 (P11912) B-cell antigen receptor complex-associated protein beta chain × 1 (P40259) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 14 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE 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.

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

View Construct and Data Evidence
UniProt name IGHM-2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 141–614; UniProt 1–474 Author chain v; PDBConstruct 141–614; UniProt 1–474

Light chain of Fab fragments of the VRC01 antibody,Immunoglobulin kappa constant

Homo sapiens

UniProt P01834

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain L; UniProt 1–107 Chain R; UniProt 1–107 Not recorded Chimera of Heavy chain of VRC01 antibody Fab and Isoform 2 of Immunoglobulin heavy constant mu × 2 (P01871-2) B-cell antigen receptor complex-associated protein alpha chain × 1 (P11912) B-cell antigen receptor complex-associated protein beta chain × 1 (P40259) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 14 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE 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.

44 other PDB entries and 65 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IGKC_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain L; PDBConstruct 144–250; UniProt 1–107 Author chain R; PDBConstruct 144–250; UniProt 1–107

B-cell antigen receptor complex-associated protein alpha chain

Homo sapiens

UniProt P11912

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–226 Not recorded Chimera of Heavy chain of VRC01 antibody Fab and Isoform 2 of Immunoglobulin heavy constant mu × 2 (P01871-2) Light chain of Fab fragments of the VRC01 antibody,Immunoglobulin kappa constant × 2 (P01834) B-cell antigen receptor complex-associated protein beta chain × 1 (P40259) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 14 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE 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.

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

View Construct and Data Evidence
UniProt name CD79A_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 1–226; UniProt 1–226

B-cell antigen receptor complex-associated protein beta chain

Homo sapiens

UniProt P40259

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 1–229 Not recorded Chimera of Heavy chain of VRC01 antibody Fab and Isoform 2 of Immunoglobulin heavy constant mu × 2 (P01871-2) Light chain of Fab fragments of the VRC01 antibody,Immunoglobulin kappa constant × 2 (P01834) B-cell antigen receptor complex-associated protein alpha chain × 1 (P11912) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 14 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE 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.

4 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CD79B_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain B; PDBConstruct 1–229; UniProt 1–229

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 7xq8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7xq8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7xq8
Deposition date deposition_date2022-05-07
Structure title titleStructure of human B-cell antigen receptor of the IgM isotype
Keywords keywordsimmunology, B cell signalling, adaptive immunity, antibody, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier62.90
Radius of gyration Rg (electron density) rg_electron64.28
Forward intensity I(0) i0522732000.00
Molecular weight molecular_weight176090.0 kDa
Excluded volume excluded_volume213800 ų
Envelope volume envelope_volume414520 ų
Hydration-shell volume shell_volume58686 ų
Envelope diameter envelope_diameter240.5
Shell Rg shell_rg56.86
Envelope Rg envelope_rg63.14
Shape Rg shape_rg64.42
Total Rg total_rg63.64
Total atoms total_atoms12452
Residues n_residues1873
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 dmax213.2
Rg (real space) rg_real63.69
Rg uncertainty (real space) rg_real_error2.17
I(0) (real space) i0_real5.2230e+08
I(0) uncertainty (real space) i0_real_error1.0360e+07
Rg (reciprocal space) rg_reciprocal62.02
I(0) (reciprocal space) i0_reciprocal521100000.0000
Solution quality estimate total_estimate0.8231
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary42.6
Skewness Skewness skewness0.493
Kurtosis Kurtosis kurtosis-0.467
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0035
Highest regularization parameter α highest_alpha26670000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.733; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.800; Smooth: 0.698

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)