6xja

Streptococcus Pneumoniae IgA1 Protease with IgA1 substrate

Method: ELECTRON MICROSCOPY Dmax: 179.1 Å Quality: GOOD

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

Immunoglobulin A1 protease

Streptococcus pneumoniae (strain ATCC BAA-255 / R6)

UniProt Q59947

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain P; UniProt 665–1963 Mutation:E1605A Immunoglobulin heavy constant alpha 1 × 2 (P01876) Immunoglobulin alpha-1 light chain × 1 Immunoglobulin alpha-1 heavy chain × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;20 mM Hepes, pH 7 150 mM NaCl 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 IGA1_STRR6
Isoform
PDB entities 1
Chains and sequence ranges Author chain P; PDBConstruct 1–1299; UniProt 665–1963

Immunoglobulin heavy constant alpha 1

OrganismNot specified

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 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 122–331 Chain B; UniProt 122–331 Not recorded Immunoglobulin A1 protease × 1 (Q59947) Immunoglobulin alpha-1 light chain × 1 Immunoglobulin alpha-1 heavy chain × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;20 mM Hepes, pH 7 150 mM NaCl 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.

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 1–210; UniProt 122–331 Author chain B; PDBConstruct 1–210; UniProt 122–331

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 6xja

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6xja
Deposition date deposition_date2020-06-23
Structure title titleStreptococcus Pneumoniae IgA1 Protease with IgA1 substrate
Keywords keywordsIgA1, Complex, Protease, metalloprotease, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier49.54
Radius of gyration Rg (electron density) rg_electron50.06
Forward intensity I(0) i0810825000.00
Molecular weight molecular_weight233300.0 kDa
Excluded volume excluded_volume290950 ų
Envelope volume envelope_volume418050 ų
Hydration-shell volume shell_volume72462 ų
Envelope diameter envelope_diameter188.7
Shell Rg shell_rg50.04
Envelope Rg envelope_rg50.29
Shape Rg shape_rg50.04
Total Rg total_rg50.14
Total atoms total_atoms16441
Residues n_residues2156
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 dmax179.1
Rg (real space) rg_real49.97
Rg uncertainty (real space) rg_real_error2.02
I(0) (real space) i0_real8.1080e+08
I(0) uncertainty (real space) i0_real_error1.5430e+07
Rg (reciprocal space) rg_reciprocal49.54
I(0) (reciprocal space) i0_reciprocal810400000.0000
Solution quality estimate total_estimate0.8370
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary50.4
Skewness Skewness skewness0.511
Kurtosis Kurtosis kurtosis-0.275
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha93280000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.707; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.882; Smooth: 0.874

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id6xjaH01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id6xjaL01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)