› 3q6u

X-ray diffraction
1.6Å resolution

Structure of the apo MET receptor kinase in the dually-phosphorylated, activated state

Released:
DOI: 10.2210/pdb3q6u/pdb
PDB entry 3q6u coloured by chain, front view.
PDB entry 3q6u coloured by chain, side view.
PDB entry 3q6u coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for selective small molecule kinase inhibition of activated c-Met.
Rickert KW, Patel SB, Allison TJ, Byrne NJ, Darke PL, Ford RE, Guerin DJ, Hall DL, Kornienko M, Lu J, Munshi SK, Reid JC, Shipman JM, Stanton EF, Wilson KJ, Young JR, Soisson SM, Lumb KJ
J Biol Chem 286 11218-25 (2011)
PMID: 21247903

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-530690 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hepatocyte growth factor receptor Chain: A
Molecule details ›
Chain: A
Length: 308 amino acids
Theoretical weight: 35.13 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P08581 (Residues: 1048-1348; Coverage: 22%)
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 17-ID
Spacegroup: P212121
Unit cell:
a: 39.72Å b: 63.808Å c: 112.63Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.184 0.214
Expression system: Spodoptera frugiperda

Quick links

Citations

3 review citations

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

5 mentions without citation

Structural basis for selective small molecule kinase inhibition of activated c-Met.
Rickert et al. (2011)
4 more