6lxw

Cryo-EM structure of human secretory immunoglobulin A in complex with the N-terminal domain of SpsA

Method: ELECTRON MICROSCOPY Dmax: 158.7 Å Quality: GOOD

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

Interleukin-2,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 × 7 PDB declaration: heptameric(7) 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 Immunoglobulin J chain × 1 (P01591) Polymeric immunoglobulin receptor × 1 (P01833) SigA binding protein × 1 (O33753) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.27 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 1
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

Interleukin-2,Immunoglobulin heavy constant alpha 1

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 × 7 PDB declaration: heptameric(7) 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 Not recorded Immunoglobulin J chain × 1 (P01591) Polymeric immunoglobulin receptor × 1 (P01833) SigA binding protein × 1 (O33753) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.27 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
Chains and sequence ranges 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

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain J; UniProt 1–159 Not recorded Interleukin-2,Immunoglobulin heavy constant alpha 1 × 4 (P60568,P01876) Polymeric immunoglobulin receptor × 1 (P01833) SigA binding protein × 1 (O33753) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.27 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 2
Chains and sequence ranges Author chain J; PDBConstruct 1–159; UniProt 1–159

Polymeric immunoglobulin receptor

Homo sapiens

UniProt P01833

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain P; UniProt 1–565 Not recorded Interleukin-2,Immunoglobulin heavy constant alpha 1 × 4 (P60568,P01876) Immunoglobulin J chain × 1 (P01591) SigA binding protein × 1 (O33753) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.27 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.

15 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PIGR_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain P; PDBConstruct 1–565; UniProt 1–565

SigA binding protein

Streptococcus pneumoniae

UniProt O33753

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain S; UniProt 38–324 Not recorded Interleukin-2,Immunoglobulin heavy constant alpha 1 × 4 (P60568,P01876) Immunoglobulin J chain × 1 (P01591) Polymeric immunoglobulin receptor × 1 (P01833) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.27 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 O33753_STREE
Isoform
PDB entities 4
Chains and sequence ranges Author chain S; PDBConstruct 31–317; UniProt 38–324

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 6lxw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6lxw
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6lxw
Deposition date deposition_date2020-02-12
Structure title titleCryo-EM structure of human secretory immunoglobulin A in complex with the N-terminal domain of SpsA
Keywords keywordsimmunoglobulin, dimer, transcytosis, secreted, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier46.30
Radius of gyration Rg (electron density) rg_electron46.28
Forward intensity I(0) i0463156000.00
Molecular weight molecular_weight175060.0 kDa
Excluded volume excluded_volume218530 ų
Envelope volume envelope_volume330690 ų
Hydration-shell volume shell_volume61061 ų
Envelope diameter envelope_diameter170.9
Shell Rg shell_rg48.30
Envelope Rg envelope_rg46.56
Shape Rg shape_rg46.26
Total Rg total_rg46.42
Total atoms total_atoms12299
Residues n_residues1595
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 dmax158.7
Rg (real space) rg_real46.42
Rg uncertainty (real space) rg_real_error1.50
I(0) (real space) i0_real4.6320e+08
I(0) uncertainty (real space) i0_real_error8.2330e+06
Rg (reciprocal space) rg_reciprocal46.30
I(0) (reciprocal space) i0_reciprocal463100000.0000
Solution quality estimate total_estimate0.8769
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary51.4
Skewness Skewness skewness0.384
Kurtosis Kurtosis kurtosis-0.233
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha28610000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.872; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.780

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id6lxwA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6lxwA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6lxwB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6lxwB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6lxwC01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6lxwC02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6lxwD01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6lxwD02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)