2wtj Summary

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CRYSTAL STRUCTURE OF CHK2 IN COMPLEX WITH AN INHIBITOR

The structure was published by Hilton, S., Naud, S., Caldwell, J.J., et al., Aherne, G.W., Garrett, M.D., and Collins, I., in 2010 in a paper entitled "Identification and Characterisation of 2-Aminopyridine Inhibitors of Checkpoint Kinase 2" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 2009.

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

The PDB entry contains the structure of CHECKPOINT KINASE 2.

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 CHECKPOINT KINASE 2 O96017 (210-531) (CHK2_HUMAN)search Homo sapienssearch < 90% 329 87%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
O96017 (210 - 531) CHECKPOINT KINASE 2 Homo sapiens

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

Chain ID Molecular function (GO) Biological process (GO)
A (O96017) protein serine/threonine kinase activitysearch protein kinase activitysearch ATP bindingsearch transferase activity, transferring phosphorus-containing groupssearch protein phosphorylationsearch

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