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7uvk

G. haemolysans IgA1 protease

Method: ELECTRON MICROSCOPY Dmax: 143.8 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

IgA1 Protease

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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 1–2178 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.28 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.

Other PDB Difference from Current Entry 7UVK Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
7UVL IgA1 Protease with IgA1 substrate Deposited 2022-05-02 Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain P 884–2178（1295 aa）
Mutation：A942E No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.56 Å
9ECT Crystal Structure of the Gemella haemolysans Immunoglobulin A1 Protease Trypsin-Like Domain Deposited 2024-11-15 Different construct Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 661–873（213 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；0.2M KNO3, 25% (w/v) PEG3350
Resolution 1.75 Å R-free 0.242
9ECT Crystal Structure of the Gemella haemolysans Immunoglobulin A1 Protease Trypsin-Like Domain Deposited 2024-11-15 Different construct Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 661–873（213 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；0.2M KNO3, 25% (w/v) PEG3350
Resolution 1.75 Å R-free 0.242

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 A； PDBConstruct 24–2201； UniProt 1–2178

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 7uvk

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7uvk
Deposition date deposition_date2022-05-02
Structure title titleG. haemolysans IgA1 protease
Keywords keywordsprotease, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier39.52 Å
Radius of gyration Rg (electron density) rg_electron39.49 Å
Forward intensity I(0) i0322275000.00
Molecular weight molecular_weight146690.0 kDa
Excluded volume excluded_volume183840 ų
Envelope volume envelope_volume247390 ų
Hydration-shell volume shell_volume53147 ų
Envelope diameter envelope_diameter154.0 Å
Shell Rg shell_rg43.94 Å
Envelope Rg envelope_rg39.98 Å
Shape Rg shape_rg39.46 Å
Total Rg total_rg39.84 Å
Total atoms total_atoms10350
Residues n_residues1295
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax143.8 Å
Rg (real space) rg_real39.82 Å
Rg uncertainty (real space) rg_real_error1.39 Å
I(0) (real space) i0_real3.2230e+08
I(0) uncertainty (real space) i0_real_error5.3660e+06
Rg (reciprocal space) rg_reciprocal39.64 Å
I(0) (reciprocal space) i0_reciprocal322200000.0000
Solution quality estimate total_estimate0.8382
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.6 Å
Skewness Skewness skewness0.519
Kurtosis Kurtosis kurtosis-0.191
Angular range angular_range— – 0.2000 Å−1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha77790000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.696; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.831; Smooth: 0.974
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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9. Files and Curves (10)