PDBe 3rhk

X-ray diffraction
1.94Å resolution

Crystal structure of the catalytic domain of c-Met kinase in complex with ARQ 197

Released:

Function and Biology Details

Reaction catalysed:
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hepatocyte growth factor receptor Chains: A, B
Molecule details ›
Chains: A, B
Length: 318 amino acids
Theoretical weight: 35.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P08581 (Residues: 1038-1346; Coverage: 23%)
Gene name: MET
Sequence domains: Protein tyrosine kinase
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P1
Unit cell:
a: 53.47Å b: 58.67Å c: 64.96Å
α: 88.41° β: 68.1° γ: 85.52°
R-values:
R R work R free
0.203 0.2 0.254
Expression system: Escherichia coli BL21(DE3)