3nuu Summary

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phosphoinositide-dependent kinase-1 (PDK1) with fragment11

The structure was published by Medina, J.R., Blackledge, C.W., Heerding, D.A., et al., Briand, J., Wright, L., and Axten, J.M., in 2010 in a paper entitled "Aminoindazole PDK1 Inhibitors: A Case Study in Fragment-Based Drug Discovery" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.9803 Å and deposited in 2010.

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

The PDB entry contains the structure of PkB-like. This molecule has the UniProt identifier O15530 (PDPK1_HUMAN)search. The sample contained 286 residues which is < 90% of the natural sequence. Out of 286 residues 274 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 has more than one probable quaternary state observed. For more details see the quaternary structure page.

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 PkB-like O15530 (73-358) (PDPK1_HUMAN)search Homo sapienssearch < 90% 286 96%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
O15530 (73 - 358) PkB-like Homo sapiens

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

Chain ID Biological process (GO) Molecular function (GO)
A (O15530) protein phosphorylationsearch protein kinase activitysearch ATP bindingsearch protein serine/threonine kinase activitysearch transferase activity, transferring phosphorus-containing groupssearch

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