1yhv Summary

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Crystal Structure of PAK1 kinase domain with two point mutations (K299R, T423E)

The structure was published by Lei, M., Robinson, M.A., and Harrison, S.C., in 2005 in a paper entitled "The Active Conformation of the PAK1 Kinase Domain" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 2005.

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

The PDB entry contains the structure of Serine/threonine-protein kinase PAK 1. This molecule has the UniProt identifier Q13153 (PAK1_HUMAN)search. The sample contained 297 residues which is < 90% of the natural sequence. Out of 297 residues 290 were observed and are deposited in the PDB.

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 PAK 1 Q13153 (249-545) (PAK1_HUMAN)search Homo sapienssearch < 90% 297 98%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q13153 (249 - 545) Serine/threonine-protein kinase PAK 1 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 (Q13153) protein kinase activitysearch protein serine/threonine kinase activitysearch transferase activity, transferring phosphorus-containing groupssearch ATP bindingsearch 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