› 2g15

X-ray diffraction
2.15Å resolution

Structural Characterization of autoinhibited c-Met kinase

Released:
DOI: 10.2210/pdb2g15/pdb
PDB entry 2g15 coloured by chain, front view.
PDB entry 2g15 coloured by chain, side view.
PDB entry 2g15 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural characterization of autoinhibited c-Met kinase produced by coexpression in bacteria with phosphatase.
Wang W, Marimuthu A, Tsai J, Kumar A, Krupka HI, Zhang C, Powell B, Suzuki Y, Nguyen H, Tabrizizad M, Luu C, West BL
Proc Natl Acad Sci U S A 103 3563-8 (2006)
PMID: 16537444

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
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140186 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hepatocyte growth factor receptor Chain: A
Molecule details ›
Chain: A
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 and serine/threonine kinase
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 32-ID
Spacegroup: P213
Unit cell:
a: 103.803Å b: 103.803Å c: 103.803Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.234 0.223 0.259
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

10 review citations

Targeting MET in cancer: rationale and progress.
Gherardi et al. (2012)
9 more

13 mentions without citation

Hepatocyte growth factor/MET in cancer progression and biomarker discovery.
Matsumoto et al. (2017)
12 more