3jvs Summary

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Characterization of the Chk1 allosteric inhibitor binding site

The structure was published by Vanderpool, D., Johnson, T.O., Ping, C., et al., Register, J., Brown, E., and Ermolieff, J., in 2009 in a paper entitled "Characterization of the CHK1 allosteric inhibitor binding site." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 2009.

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

The PDB entry contains the structure of Serine/threonine-protein kinase Chk1. This molecule has the UniProt identifier O14757 (CHK1_HUMAN)search. The sample contained 271 residues which is < 90% of the natural sequence. Out of 271 residues 255 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 Serine/threonine-protein kinase Chk1 O14757 (2-272) (CHK1_HUMAN)search Homo sapienssearch < 90% 271 94%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
O14757 (2 - 272) Serine/threonine-protein kinase Chk1 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 (O14757) ATP bindingsearch transferase activity, transferring phosphorus-containing groupssearch protein kinase activitysearch protein serine/threonine kinase activitysearch 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 Protein kinase, ATP binding sitesearch