5hni

CRYSTAL STRUCTURE OF CMET WT with compound 3

Method: X-RAY DIFFRACTION Dmax: 103.6 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 X; UniProt 1067–1378 Fragment:UNP residues 1067-1378 63B methyl (6-{[6-(4-fluorophenyl)[1,2,4]triazolo[4,3-b]pyridazin-3-yl]sulfanyl}-1H-benzimidazol-2-yl)carbamate × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;277 K;Hepes 100mM, isopropanol 11%, PEG5000 MME 6% Resolution 1.71 Å R-free 0.245
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain Y; UniProt 1067–1378 Fragment:UNP residues 1067-1378 63B methyl (6-{[6-(4-fluorophenyl)[1,2,4]triazolo[4,3-b]pyridazin-3-yl]sulfanyl}-1H-benzimidazol-2-yl)carbamate × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;277 K;Hepes 100mM, isopropanol 11%, PEG5000 MME 6% Resolution 1.71 Å R-free 0.245

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 165 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MET_HUMAN
Isoform P08581-2
PDB entities 1
Chains and sequence ranges Author chain X; PDBConstruct 1–312; UniProt 1067–1378 Author chain Y; PDBConstruct 1–312; UniProt 1067–1378

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 5hni

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5hni
Deposition date deposition_date2016-01-18
Structure title titleCRYSTAL STRUCTURE OF CMET WT with compound 3
Keywords keywordsTRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.00
Radius of gyration Rg (electron density) rg_electron28.73
Forward intensity I(0) i048480300.00
Molecular weight molecular_weight56372.0 kDa
Excluded volume excluded_volume71342 ų
Envelope volume envelope_volume89926 ų
Hydration-shell volume shell_volume27547 ų
Envelope diameter envelope_diameter108.7
Shell Rg shell_rg33.92
Envelope Rg envelope_rg29.25
Shape Rg shape_rg28.69
Total Rg total_rg29.38
Total atoms total_atoms3966
Residues n_residues490
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 dmax103.6
Rg (real space) rg_real29.22
Rg uncertainty (real space) rg_real_error0.91
I(0) (real space) i0_real4.8480e+07
I(0) uncertainty (real space) i0_real_error7.6130e+05
Rg (reciprocal space) rg_reciprocal29.13
I(0) (reciprocal space) i0_reciprocal48480000.0000
Solution quality estimate total_estimate0.8163
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.4
Skewness Skewness skewness0.551
Kurtosis Kurtosis kurtosis-0.206
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17540000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.693; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.601; Smooth: 0.927

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_idd5hnix_
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_idd5hniy_
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_id5hniX01
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_id5hniX02
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_id5hniY01
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_id5hniY02
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)