2uv2 Summary

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PDB entry 2uv2 (supersedes 2ja0)

CRYSTAL STRUCTURE OF HUMAN STE20-LIKE KINASE BOUND TO 4-(4-(5-CYCLOPROPYL-1H-PYRAZOL-3-YLAMINO)-QUINAZOLIN-2-YLAMINO)-PHENYL)-ACETONITRILE

The structure was published by Pike, A.C.W., Rellos, P., Niesen, F.H., et al., Turk, B.E., Pearl, L.H., and Knapp, S., in 2008 in a paper entitled "Activation Segment Dimerization: A Mechanism for Kinase Autophosphorylation of Non-Consensus Sites." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.3 Å and deposited in 2007.

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

The PDB entry contains the structure of STE20-LIKE SERINE-THREONINE KINASE.

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 STE20-LIKE SERINE-THREONINE KINASE Q9H2G2 (19-320) (SLK_HUMAN)search Homo sapienssearch < 90% 325 88%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q9H2G2 (19 - 320) STE20-LIKE SERINE-THREONINE KINASE Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A Protein kinases, catalytic subunitsearch Phosphorylase Kinase; domain 1search, Transferase(Phosphotransferase) domain 1search Protein kinase domainsearch

Chain ID Biological process (GO) Molecular function (GO)
A (Q9H2G2) protein phosphorylationsearch regulation of signal transductionsearch ATP bindingsearch transferase activity, transferring phosphorus-containing groupssearch protein serine/threonine kinase activitysearch protein kinase activitysearch

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