3qc4 Summary

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PDK1 in complex with DFG-OUT inhibitor xxx

The structure was published by Erlanson, D.A., Arndt, J.W., Cancilla, M.T., et al., Tangonan, B.T., Yang, W., and Sun, L., in 2011 in a paper entitled "Discovery of a potent and highly selective PDK1 inhibitor via fragment-based drug discovery." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 2011.

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

This PDB entry contains multiple copies of the structure of 3-phosphoinositide-dependent protein kinase 1.

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 3-phosphoinositide-dependent protein kinase 1 O15530 (51-359) (PDPK1_HUMAN)search Homo sapienssearch < 90% 314 88%
B 3-phosphoinositide-dependent protein kinase 1 O15530 (51-359) (PDPK1_HUMAN)search Homo sapienssearch < 90% 314 88%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
O15530 (51 - 359) 3-phosphoinositide-dependent protein kinase 1 Homo sapiens

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