7uvl

IgA1 Protease with IgA1 substrate

Method: ELECTRON MICROSCOPY Dmax: 185.8 Å Quality: REASONABLE

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

LPXTG-motif cell wall anchor domain protein

Gemella haemolysans

UniProt C5NYF3

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 884–2178 Mutation:A942E Immunoglobulin alpha-1 heavy constant × 2 (P01876) Immunoglobulin alpha-1 light chain × 1 Immunoglobulin alpha-1 heavy chain × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.56 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 C5NYF3_9BACL
Isoform
PDB entities 1
Chains and sequence ranges Author chain P; PDBConstruct 1–1295; UniProt 884–2178

Immunoglobulin alpha-1 heavy constant

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 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 123–331 Chain B; UniProt 123–331 Not recorded LPXTG-motif cell wall anchor domain protein × 1 (C5NYF3) Immunoglobulin alpha-1 light chain × 1 Immunoglobulin alpha-1 heavy chain × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.56 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 1–209; UniProt 123–331 Author chain B; PDBConstruct 1–209; UniProt 123–331

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 7uvl

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7uvl
Deposition date deposition_date2022-05-02
Structure title titleIgA1 Protease with IgA1 substrate
Keywords keywordscomplex, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier51.04
Radius of gyration Rg (electron density) rg_electron51.34
Forward intensity I(0) i0808141000.00
Molecular weight molecular_weight234170.0 kDa
Excluded volume excluded_volume292450 ų
Envelope volume envelope_volume421790 ų
Hydration-shell volume shell_volume71693 ų
Envelope diameter envelope_diameter197.7
Shell Rg shell_rg50.37
Envelope Rg envelope_rg51.44
Shape Rg shape_rg51.35
Total Rg total_rg51.29
Total atoms total_atoms16508
Residues n_residues2154
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 dmax185.8
Rg (real space) rg_real51.29
Rg uncertainty (real space) rg_real_error2.82
I(0) (real space) i0_real8.0810e+08
I(0) uncertainty (real space) i0_real_error1.6290e+07
Rg (reciprocal space) rg_reciprocal50.83
I(0) (reciprocal space) i0_reciprocal807600000.0000
Solution quality estimate total_estimate0.6029
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary47.9
Skewness Skewness skewness0.493
Kurtosis Kurtosis kurtosis-0.295
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha64270000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.697; Stabil: 1.000; Sysdev: 0.003; Positv: 1.000; Valcen: 0.815; Smooth: 0.918

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)