4aoi

Crystal structure of C-MET kinase domain in complex with 4-(3-((1H- pyrrolo(2,3-b)pyridin-3-yl)methyl)-(1,2,4)triazolo(4,3-b)(1,2,4) triazin-6-yl)benzonitrile

Method: X-RAY DIFFRACTION Dmax: 52.8 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 1051–1348 Fragment:TYROSINE KINASE DOMAIN, RESIDUES 1051-1348 4K0 4-[3-(1H-pyrrolo[2,3-b]pyridin-3-ylmethyl)-[1,2,4]triazolo[4,3-b][1,2,4]triazin-6-yl]benzenecarbonitrile × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;286 K;CRYSTALS WERE OBTAINED AT 13 DEGREES CELCIUS FROM HANGING DROPS CONTAINING 1.2 MICROLITERS OF PROTEIN: COMPOUND SOLUTION (1:5 MOLAR RATIO) AND 1.2 MICROLITERS OF PRECIPITATING SOLUTION (0.05 M CITRATE-PHOSPHATE, PH 4.6, 0-25 MM NACL, 21 % (W/V) PEG-3350). TO OBTAIN LARGER CRYSTALS, STREAK SEEDING WAS EMPLOYED USING THE CRYSTALS JUST MENTIONED AS DONORS, UNDER THE SAME CONDITIONS EXCEPT 275 MM NACL WAS USED AND THE DROPS WERE EQUILIBRATED OVERNIGHT BEFORE SEEDING WAS PERFORMED. Resolution 1.90 Å R-free 0.214

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 2–299; UniProt 1051–1348

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 4aoi

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4aoi
Deposition date deposition_date2012-03-27
Structure title titleCrystal structure of C-MET kinase domain in complex with 4-(3-((1H- pyrrolo(2,3-b)pyridin-3-yl)methyl)-(1,2,4)triazolo(4,3-b)(1,2,4) triazin-6-yl)benzonitrile
Keywords keywordsTRANSFERASE, KINASE INHIBITOR; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.30
Radius of gyration Rg (electron density) rg_electron19.38
Forward intensity I(0) i017827700.00
Molecular weight molecular_weight33139.0 kDa
Excluded volume excluded_volume42008 ų
Envelope volume envelope_volume48001 ų
Hydration-shell volume shell_volume20614 ų
Envelope diameter envelope_diameter64.9
Shell Rg shell_rg25.75
Envelope Rg envelope_rg19.68
Shape Rg shape_rg19.36
Total Rg total_rg20.36
Total atoms total_atoms2335
Residues n_residues289
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 dmax52.8
Rg (real space) rg_real19.67
Rg uncertainty (real space) rg_real_error0.04
I(0) (real space) i0_real1.7030e+07
I(0) uncertainty (real space) i0_real_error1.3870e+05
Rg (reciprocal space) rg_reciprocal20.24
I(0) (reciprocal space) i0_reciprocal17830000.0000
Solution quality estimate total_estimate0.6809
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary23.4
Skewness Skewness skewness0.206
Kurtosis Kurtosis kurtosis-0.478
Angular range angular_range— – 0.3900 −1
Current regularization parameter α current_alpha4.5600
Highest regularization parameter α highest_alpha4672000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.993; Stabil: 0.959; Sysdev: 0.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

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_idd4aoia_
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_id4aoiA01
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_id4aoiA02
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)