8vm1

Structural Elucidation of the Mesothelin Mucin16 CA125 Interaction

Method: X-RAY DIFFRACTION Dmax: 70.2 Å Quality: GOOD

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

Mesothelin, cleaved form,Mucin-16

Homo sapiens

UniProt Q13421

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 Monomer Protein × 1 其他Polymer 2 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 296–359 Fragment:residues 296-359 of mesothelin (Uniprot numbering),SEA 10 domain of mucin-16 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;Bis-Tris, NH4CL, PEG3350 Resolution 2.65 Å R-free 0.298

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.

11 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MSLN_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–66; UniProt 296–359

Mesothelin, cleaved form,Mucin-16

Homo sapiens

UniProt Q8WXI7

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 Monomer Protein × 1 其他Polymer 2 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 13475–13600 Fragment:residues 296-359 of mesothelin (Uniprot numbering),SEA 10 domain of mucin-16 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;Bis-Tris, NH4CL, PEG3350 Resolution 2.65 Å R-free 0.298

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.

3 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MUC16_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 67–192; UniProt 13475–13600

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 8vm1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8vm1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8vm1
Deposition date deposition_date2024-01-12
Structure title titleStructural Elucidation of the Mesothelin Mucin16 CA125 Interaction
Keywords keywordslinked complex, CELL ADHESION; CELL ADHESION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.20
Radius of gyration Rg (electron density) rg_electron19.29
Forward intensity I(0) i08541450.00
Molecular weight molecular_weight21825.0 kDa
Excluded volume excluded_volume27482 ų
Envelope volume envelope_volume34447 ų
Hydration-shell volume shell_volume15802 ų
Envelope diameter envelope_diameter72.0
Shell Rg shell_rg24.41
Envelope Rg envelope_rg19.31
Shape Rg shape_rg19.29
Total Rg total_rg20.12
Total atoms total_atoms1536
Residues n_residues185
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 dmax70.2
Rg (real space) rg_real20.22
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real8.5410e+06
I(0) uncertainty (real space) i0_real_error1.0840e+05
Rg (reciprocal space) rg_reciprocal20.22
I(0) (reciprocal space) i0_reciprocal8541000.0000
Solution quality estimate total_estimate0.8598
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.1
Skewness Skewness skewness0.359
Kurtosis Kurtosis kurtosis-0.355
Angular range angular_range— – 0.3950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1891000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.747; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.947; Smooth: 0.984

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)