5ya5

CRYSTAL STRUCTURE OF c-MET IN COMPLEX WITH NOVEL INHIBITOR

Method: X-RAY DIFFRACTION Dmax: 65.2 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:UNP residues 1038-1346 6TD 2-[3-(4-methoxybenzyl)[1,2,4]triazolo[3,4-b][1,3,4]thiadiazol-6-yl]-1H-indole × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293 K;0.1M Tris pH7.5, 15% glycerol, 12% MPD, 5% isopropanol, 15% PEG5Kmme Resolution 1.89 Å R-free 0.235

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 11–319; 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 5ya5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5ya5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5ya5
Deposition date deposition_date2017-08-30
Structure title titleCRYSTAL STRUCTURE OF c-MET IN COMPLEX WITH NOVEL INHIBITOR
Keywords keywordsc-MET inhibitor, 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_guinier20.13
Radius of gyration Rg (electron density) rg_electron19.21
Forward intensity I(0) i015583900.00
Molecular weight molecular_weight30922.0 kDa
Excluded volume excluded_volume39246 ų
Envelope volume envelope_volume45518 ų
Hydration-shell volume shell_volume19820 ų
Envelope diameter envelope_diameter67.0
Shell Rg shell_rg25.74
Envelope Rg envelope_rg19.70
Shape Rg shape_rg19.20
Total Rg total_rg20.25
Total atoms total_atoms2178
Residues n_residues273
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 dmax65.2
Rg (real space) rg_real20.08
Rg uncertainty (real space) rg_real_error0.50
I(0) (real space) i0_real1.5580e+07
I(0) uncertainty (real space) i0_real_error2.1940e+05
Rg (reciprocal space) rg_reciprocal20.09
I(0) (reciprocal space) i0_reciprocal15580000.0000
Solution quality estimate total_estimate0.8083
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary64.3
Skewness Skewness skewness0.303
Kurtosis Kurtosis kurtosis-0.303
Angular range angular_range— – 0.3950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4351000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.835; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd5ya5a_
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_id5ya5A02
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)