3dkg Summary

pdbe.org/3dkg
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SGX CLONE 5698a109KFg1h1

The structure was published by Buchanan, S.G., Hendle, J., Lee, P.S., et al., Emtage, S., Burley, S.K., and Reich, S.H., in 2009 in a paper entitled "SGX523 is an exquisitely selective, ATP-competitive inhibitor of the MET receptor tyrosine kinase with antitumor activity in vivo." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.91 Å and deposited in 2008.

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

The PDB entry contains the structure of Met proto-oncogene. This molecule has the UniProt identifier A1L467 ()search. The sample contained 317 residues which is < 90% of the natural sequence. Out of 317 residues 272 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

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 Met proto-oncogene Not available
Homo sapienssearch Not available 317 88%


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 () protein kinase activitysearch ATP bindingsearch protein tyrosine kinase activitysearch 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