11hq

Type-III c-MET Inhibitor Enabled by Free-Energy Perturbation Calculations

Method: X-RAY DIFFRACTION Dmax: 103.3 Å Quality: EXCELLENT

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 1037–1346 Mutation:L1272V A1C9B (1R,6M)-1-benzyl-6-[(3P)-3-(1-ethyl-1H-pyrazol-4-yl)-5-fluorophenyl]-1,2-dihydro-3H-pyrrolo[3,4-c]pyridin-3-one × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.1 M HEPES pH 6.5, 10% PEG 6000, 5% MPD Resolution 2.65 Å R-free 0.287
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1037–1346 Mutation:L1272V A1C9B (1R,6M)-1-benzyl-6-[(3P)-3-(1-ethyl-1H-pyrazol-4-yl)-5-fluorophenyl]-1,2-dihydro-3H-pyrrolo[3,4-c]pyridin-3-one × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.1 M HEPES pH 6.5, 10% PEG 6000, 5% MPD Resolution 2.65 Å R-free 0.287
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 1037–1346 Mutation:L1272V A1C9B (1R,6M)-1-benzyl-6-[(3P)-3-(1-ethyl-1H-pyrazol-4-yl)-5-fluorophenyl]-1,2-dihydro-3H-pyrrolo[3,4-c]pyridin-3-one × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.1 M HEPES pH 6.5, 10% PEG 6000, 5% MPD Resolution 2.65 Å R-free 0.287

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 164 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 1–310; UniProt 1037–1346 Author chain B; PDBConstruct 1–310; UniProt 1037–1346 Author chain C; PDBConstruct 1–310; UniProt 1037–1346

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 11hq

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 11hq
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id11hq
Deposition date deposition_date2026-02-25
最后修订 last_revision2026-05-27
Structure title titleType-III c-MET Inhibitor Enabled by Free-Energy Perturbation Calculations
Keywords keywordstyrosine kinase, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier33.31
Radius of gyration Rg (electron density) rg_electron32.55
Forward intensity I(0) i0120534000.00
Molecular weight molecular_weight91978.0 kDa
Excluded volume excluded_volume117160 ų
Envelope volume envelope_volume157140 ų
Hydration-shell volume shell_volume40225 ų
Envelope diameter envelope_diameter106.7
Shell Rg shell_rg39.39
Envelope Rg envelope_rg31.95
Shape Rg shape_rg32.57
Total Rg total_rg33.11
Total atoms total_atoms13024
Residues n_residues802
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 dmax103.3
Rg (real space) rg_real33.20
Rg uncertainty (real space) rg_real_error0.75
I(0) (real space) i0_real1.2050e+08
I(0) uncertainty (real space) i0_real_error2.0260e+06
Rg (reciprocal space) rg_reciprocal33.27
I(0) (reciprocal space) i0_reciprocal120500000.0000
Solution quality estimate total_estimate0.9095
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary45.2
Skewness Skewness skewness0.110
Kurtosis Kurtosis kurtosis-0.657
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha38560000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.960; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.940

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)