3efk

Structure of c-Met with pyrimidone inhibitor 50

Method: X-RAY DIFFRACTION Dmax: 88.8 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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1048–1351 Chain B; UniProt 1048–1351 Fragment:c-Met kinase domain, UNP residues 1048-1351 Mutation:V1272L MT4 5-{4-[(6,7-dimethoxyquinolin-4-yl)oxy]-3-fluorophenyl}-2-[(4-fluorophenyl)amino]-3-methylpyrimidin-4(3H)-one × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 5;298 K;12% PEG 6000, 1.0M LiCl2, 0.1M Sodium Citrate, pH 5.0, VAPOR DIFFUSION, temperature 298K Resolution 2.20 Å R-free 0.292
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1048–1351 Fragment:c-Met kinase domain, UNP residues 1048-1351 Mutation:V1272L MT4 5-{4-[(6,7-dimethoxyquinolin-4-yl)oxy]-3-fluorophenyl}-2-[(4-fluorophenyl)amino]-3-methylpyrimidin-4(3H)-one × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 5;298 K;12% PEG 6000, 1.0M LiCl2, 0.1M Sodium Citrate, pH 5.0, VAPOR DIFFUSION, temperature 298K Resolution 2.20 Å R-free 0.292
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1048–1351 Fragment:c-Met kinase domain, UNP residues 1048-1351 Mutation:V1272L MT4 5-{4-[(6,7-dimethoxyquinolin-4-yl)oxy]-3-fluorophenyl}-2-[(4-fluorophenyl)amino]-3-methylpyrimidin-4(3H)-one × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 5;298 K;12% PEG 6000, 1.0M LiCl2, 0.1M Sodium Citrate, pH 5.0, VAPOR DIFFUSION, temperature 298K Resolution 2.20 Å R-free 0.292

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 2–305; UniProt 1048–1351 Author chain B; PDBConstruct 2–305; 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 3efk

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3efk
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3efk
Deposition date deposition_date2008-09-09
Structure title titleStructure of c-Met with pyrimidone inhibitor 50
Keywords keywords;c-Met, Kinase inhibitor pyrimidone, Alternative splicing, ATP-binding, Chromosomal rearrangement, Disease mutation, Glycoprotein, Kinase, Membrane, Nucleotide-binding, Phosphoprotein, Polymorphism, Proto-oncogene, Receptor, Transferase, Transmembrane, Tyrosine-protein kinase ;; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.82
Radius of gyration Rg (electron density) rg_electron27.01
Forward intensity I(0) i058133200.00
Molecular weight molecular_weight62058.0 kDa
Excluded volume excluded_volume78661 ų
Envelope volume envelope_volume96906 ų
Hydration-shell volume shell_volume30062 ų
Envelope diameter envelope_diameter97.7
Shell Rg shell_rg34.45
Envelope Rg envelope_rg26.57
Shape Rg shape_rg27.01
Total Rg total_rg27.80
Total atoms total_atoms4375
Residues n_residues548
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 dmax88.8
Rg (real space) rg_real27.76
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real5.8130e+07
I(0) uncertainty (real space) i0_real_error8.3110e+05
Rg (reciprocal space) rg_reciprocal27.78
I(0) (reciprocal space) i0_reciprocal58130000.0000
Solution quality estimate total_estimate0.9031
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary34.3
Skewness Skewness skewness0.238
Kurtosis Kurtosis kurtosis-0.514
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha20220000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.938; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.928

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3efka_
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
Domain ID domain_idd3efkb_
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 (4 domains)

Domain ID domain_id3efkA01
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_id3efkA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1
Domain ID domain_id3efkB01
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_id3efkB02
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)