8ji0

Cryo-EM structure of the TcsH-CROP in complex with TMPRSS2

Method: ELECTRON MICROSCOPY Dmax: 87.0 Å Quality: GOOD

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

Transmembrane protease serine 2

Homo sapiens

UniProt O15393

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 106–492 Not recorded Maltose/maltodextrin-binding periplasmic protein,Hemorrhagic toxin × 1 (P0AEX9,M9ZTT7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

33 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TMPS2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 38–424; UniProt 106–492

Maltose/maltodextrin-binding periplasmic protein,Hemorrhagic toxin

Paeniclostridium sordellii

UniProt M9ZTT7

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2236–2618 Not recorded Transmembrane protease serine 2 × 1 (O15393) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 M9ZTT7_PAESO
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 404–786; UniProt 2236–2618

Maltose/maltodextrin-binding periplasmic protein,Hemorrhagic toxin

Paeniclostridium sordellii

UniProt P0AEX9

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 27–392 Not recorded Transmembrane protease serine 2 × 1 (O15393) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

366 other PDB entries and 491 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECOLI
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 24–389; UniProt 27–392

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 8ji0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ji0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ji0
Deposition date deposition_date2023-05-25
Structure title titleCryo-EM structure of the TcsH-CROP in complex with TMPRSS2
Keywords keywordsTcsH, TMPESS2, TOXIN/HYDROLASE, TOXIN-HYDROLASE complex; TOXIN/HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier26.57
Radius of gyration Rg (electron density) rg_electron25.63
Forward intensity I(0) i052309700.00
Molecular weight molecular_weight55749.0 kDa
Excluded volume excluded_volume69422 ų
Envelope volume envelope_volume87795 ų
Hydration-shell volume shell_volume29215 ų
Envelope diameter envelope_diameter91.6
Shell Rg shell_rg32.50
Envelope Rg envelope_rg25.95
Shape Rg shape_rg25.62
Total Rg total_rg26.39
Total atoms total_atoms3934
Residues n_residues498
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 dmax87.0
Rg (real space) rg_real26.61
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real5.2310e+07
I(0) uncertainty (real space) i0_real_error6.4480e+05
Rg (reciprocal space) rg_reciprocal26.60
I(0) (reciprocal space) i0_reciprocal52310000.0000
Solution quality estimate total_estimate0.8896
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.0
Skewness Skewness skewness0.407
Kurtosis Kurtosis kurtosis-0.325
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13650000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.876; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.969; Smooth: 0.963

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)