2x2k Summary

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CRYSTAL STRUCTURE OF PHOSPHORYLATED RET TYROSINE KINASE DOMAIN WITH INHIBITOR

The structure was published by Mologni, L., Rostagno, R., Brussolo, S., et al., Mcdonald, N.Q., Lucchini, V., and Gambacorti-Passerini, C., in 2010 in a paper entitled "Synthesis, Structure-Activity Relationship and Crystallographic Studies of 3-Substituted Indolin-2-One Ret Inhibitors." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.6 Å and deposited in 2010.

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

The PDB entry contains the structure of PROTO-ONCOGENE TYROSINE-PROTEIN KINASE RECEPTOR RET.

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 most likely forms homodimers.

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 PROTO-ONCOGENE TYROSINE-PROTEIN KINASE RECEPTOR RET P07949 (705-1013) (RET_HUMAN)search Homo sapienssearch < 90% 314 92%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P07949 (705 - 1013) PROTO-ONCOGENE TYROSINE-PROTEIN KINASE RECEPTOR RET 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 (P07949) transferase activity, transferring phosphorus-containing groupssearch 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