4dei

Crystal structure of c-Met in complex with triazolopyridinone inhibitor 24

Method: X-RAY DIFFRACTION Dmax: 65.8 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 1048–1351 Not recorded 0JL 3-{(1S)-1-[3-(2-methoxyethoxy)quinolin-6-yl]ethyl}-5-(3-methyl-1,2-thiazol-5-yl)-3,5-dihydro-4H-[1,2,3]triazolo[4,5-c]pyridin-4-one × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.8;293 K;15% PEG 4000, 0.1 M HEPES, 6% isopropanol, 3% ethanol, 40 mM beta-mercaptoethanol, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.05 Å R-free 0.289

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 1–304; UniProt 1048–1351

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 4dei

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4dei
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4dei
Deposition date deposition_date2012-01-20
Structure title titleCrystal structure of c-Met in complex with triazolopyridinone inhibitor 24
Keywords keywords;proto-oncogene, inhibitor, receptor tyrosine kinase, RTK, ATP-binding, hepatocyte growth factor/scatter factor, HGF/SF, phosphoprotein, TRANSFERASE-TRANSFERASE INHIBITOR complex ;; TRANSFERASE/TRANSFERASE INHIBITOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.31
Radius of gyration Rg (electron density) rg_electron19.51
Forward intensity I(0) i034002100.00
Molecular weight molecular_weight30582.0 kDa
Excluded volume excluded_volume29851 ų
Envelope volume envelope_volume48907 ų
Hydration-shell volume shell_volume20782 ų
Envelope diameter envelope_diameter66.2
Shell Rg shell_rg26.10
Envelope Rg envelope_rg19.95
Shape Rg shape_rg19.51
Total Rg total_rg20.20
Total atoms total_atoms2319
Residues n_residues287
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 dmax65.8
Rg (real space) rg_real20.25
Rg uncertainty (real space) rg_real_error0.32
I(0) (real space) i0_real3.4000e+07
I(0) uncertainty (real space) i0_real_error4.0390e+05
Rg (reciprocal space) rg_reciprocal20.26
I(0) (reciprocal space) i0_reciprocal34000000.0000
Solution quality estimate total_estimate0.8927
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary23.5
Skewness Skewness skewness0.277
Kurtosis Kurtosis kurtosis-0.390
Angular range angular_range— – 0.3900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8134000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.871; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.990

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd4deia_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.144 — Protein kinase-like (PK-like)
Superfamily Superfamily superfamilyd.144.1 — Protein kinase-like (PK-like)
Family Family familyd.144.1.7 — Protein kinases, catalytic subunit

CATH v4.4 (2 domains)

Domain ID domain_id4deiA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology200 — Phosphorylase Kinase; domain 1
Homologous superfamily homologous superfamily20 — Phosphorylase Kinase; domain 1
Domain ID domain_id4deiA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1

8. Citations (1)

9. Files and Curves (10)