2g15 Summary

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Structural Characterization of autoinhibited c-Met kinase

The structure was published by Wang, W., Marimuthu, A., Tsai, J., et al., Tabrizizad, M., Luu, C., and West, B.L., in 2006 in a paper entitled "Structural characterization of autoinhibited c-Met kinase produced by coexpression in bacteria with phosphatase." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.15 Å and deposited in 2006.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of activated met oncogene.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A activated met oncogene P08581 (1038-1346) (MET_HUMAN)search Homo sapienssearch < 90% 318 94%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P08581 (1038 - 1346) activated met oncogene Homo sapiens

Chain Structural classification (CATH) Sequence family (Pfam)
A Phosphorylase Kinase; domain 1search, Transferase(Phosphotransferase) domain 1search Protein tyrosine kinasesearch

Chain ID Molecular function (GO) Biological process (GO)
A (P08581) ATP bindingsearch protein tyrosine kinase activitysearch protein kinase activitysearch transferase activity, transferring phosphorus-containing groupssearch protein phosphorylationsearch

Chain InterPro annotation
A Protein kinase domainsearch Serine-threonine/tyrosine-protein kinase catalytic domainsearch Tyrosine-protein kinase, active sitesearch Protein kinase-like domainsearch Protein kinase, ATP binding sitesearch Tyrosine-protein kinase, catalytic domainsearch