7y4u

Crystal structure of cMET kinase domain bound by compound 9Y

Method: X-RAY DIFFRACTION Dmax: 63.5 Å Quality: GOOD

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 1038–1346 Fragment:kinase domain I94 ~{N}-methyl-4-[1-[2-[3-(1-methylpyrazol-4-yl)quinolin-6-yl]ethyl]-6-oxidanylidene-pyridazin-3-yl]-2-(trifluoromethyl)benzamide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.8;291 K;0.1 M HEPES (pH 7.8), 15-30% (v/v) PEG 8000 Resolution 2.26 Å R-free 0.278

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 1–309; UniProt 1038–1346

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 7y4u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7y4u
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7y4u
Deposition date deposition_date2022-06-16
Structure title titleCrystal structure of cMET kinase domain bound by compound 9Y
Keywords keywordsTRANSFERASE INHIBITOR, TRANSFERASE, TRANSFERASE-INHIBITOR complex; TRANSFERASE/INHIBITOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.98
Radius of gyration Rg (electron density) rg_electron18.97
Forward intensity I(0) i016562500.00
Molecular weight molecular_weight31828.0 kDa
Excluded volume excluded_volume40329 ų
Envelope volume envelope_volume46899 ų
Hydration-shell volume shell_volume20429 ų
Envelope diameter envelope_diameter64.0
Shell Rg shell_rg25.63
Envelope Rg envelope_rg19.39
Shape Rg shape_rg18.96
Total Rg total_rg20.01
Total atoms total_atoms2243
Residues n_residues281
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 dmax63.5
Rg (real space) rg_real19.89
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real1.6560e+07
I(0) uncertainty (real space) i0_real_error2.2320e+05
Rg (reciprocal space) rg_reciprocal19.90
I(0) (reciprocal space) i0_reciprocal16560000.0000
Solution quality estimate total_estimate0.8918
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary24.1
Skewness Skewness skewness0.269
Kurtosis Kurtosis kurtosis-0.332
Angular range angular_range— – 0.4000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6265000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.866; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)