9t2v

Crystal structure of wild-type c-MET bound by cabozantinib.

Method: X-RAY DIFFRACTION Dmax: 65.9 Å Quality: REASONABLE

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

Hepatocyte growth factor receptor

Homo sapiens

UniProt P08581

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 1052–1346 Not recorded A1JS8 Cabozantinib × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;20% PEG4K, 10% isopropanol, 0.1 M Na-HEPES pH 7.5 Resolution 1.67 Å R-free 0.226

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.

128 other PDB entries and 166 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MET_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–296; UniProt 1052–1346

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 9t2v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9t2v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9t2v
Deposition date deposition_date2025-10-23
Structure title titleCrystal structure of wild-type c-MET bound by cabozantinib.
Keywords keywordsKinase, c-met, drug discovery, cancer, NSCLC, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.28
Radius of gyration Rg (electron density) rg_electron19.51
Forward intensity I(0) i032328900.00
Molecular weight molecular_weight29942.0 kDa
Excluded volume excluded_volume29295 ų
Envelope volume envelope_volume47023 ų
Hydration-shell volume shell_volume20173 ų
Envelope diameter envelope_diameter66.9
Shell Rg shell_rg25.83
Envelope Rg envelope_rg19.83
Shape Rg shape_rg19.51
Total Rg total_rg20.16
Total atoms total_atoms2272
Residues n_residues290
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 dmax65.9
Rg (real space) rg_real20.23
Rg uncertainty (real space) rg_real_error0.33
I(0) (real space) i0_real3.2330e+07
I(0) uncertainty (real space) i0_real_error4.2200e+05
Rg (reciprocal space) rg_reciprocal20.24
I(0) (reciprocal space) i0_reciprocal32330000.0000
Solution quality estimate total_estimate0.7059
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.5
Skewness Skewness skewness0.305
Kurtosis Kurtosis kurtosis-0.372
Angular range angular_range— – 0.3900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7605000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.865; Stabil: 1.000; Sysdev: 0.193; Positv: 1.000; Valcen: 1.000; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)