6sdd

Crystal structure of D1228V cMET bound by BMS-777607

Method: X-RAY DIFFRACTION Dmax: 64.8 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 1038–1346 Not recorded 353 N-{4-[(2-amino-3-chloropyridin-4-yl)oxy]-3-fluorophenyl}-4-ethoxy-1-(4-fluorophenyl)-2-oxo-1,2-dihydropyridine-3-carboxamide × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;8 % ethanol, 20 % PEG8K, 0.1 M PCPT pH 7.5 Resolution 1.93 Å R-free 0.230

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 6sdd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6sdd
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6sdd
Deposition date deposition_date2019-07-26
Structure title titleCrystal structure of D1228V cMET bound by BMS-777607
Keywords keywordsKinase, inhibitor, transferase; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.07
Radius of gyration Rg (electron density) rg_electron19.13
Forward intensity I(0) i015358600.00
Molecular weight molecular_weight30824.0 kDa
Excluded volume excluded_volume39149 ų
Envelope volume envelope_volume46534 ų
Hydration-shell volume shell_volume20277 ų
Envelope diameter envelope_diameter65.3
Shell Rg shell_rg25.53
Envelope Rg envelope_rg19.44
Shape Rg shape_rg19.12
Total Rg total_rg20.13
Total atoms total_atoms2171
Residues n_residues271
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 dmax64.8
Rg (real space) rg_real20.00
Rg uncertainty (real space) rg_real_error0.35
I(0) (real space) i0_real1.5360e+07
I(0) uncertainty (real space) i0_real_error1.8670e+05
Rg (reciprocal space) rg_reciprocal20.02
I(0) (reciprocal space) i0_reciprocal15360000.0000
Solution quality estimate total_estimate0.7487
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.0
Skewness Skewness skewness0.278
Kurtosis Kurtosis kurtosis-0.306
Angular range angular_range— – 0.3950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4963000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.851; Stabil: 0.999; Sysdev: 0.406; Positv: 1.000; Valcen: 0.997; Smooth: 0.964

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd6sdda_
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 (1 domains)

Domain ID domain_id6sddA02
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)