2bva Summary



The structure was published by Eswaran, J., Lee, W.H., Debreczeni, J.E., et al., Deacon, S.W., Peterson, J.R., and Knapp, S., in 2007 in a paper entitled "Crystal Structures of the P21-Activated Kinases Pak4, Pak5, and Pak6 Reveal Catalytic Domain Plasticity of Active Group II Paks." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.3 Å and deposited in 2005.

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

This PDB entry contains multiple copies of the structure of P21-ACTIVATED KINASE 4.

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 P21-ACTIVATED KINASE 4 O96013 (300-591) (PAK4_HUMAN)search Homo sapienssearch < 90% 292 94%
B P21-ACTIVATED KINASE 4 O96013 (300-591) (PAK4_HUMAN)search Homo sapienssearch < 90% 292 94%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
O96013 (300 - 591) P21-ACTIVATED KINASE 4 Homo sapiens

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

Chain ID Molecular function (GO) Biological process (GO)
A, B (O96013) ATP bindingsearch protein kinase activitysearch transferase activity, transferring phosphorus-containing groupssearch protein phosphorylationsearch

Chain InterPro annotation
A, B Protein kinase domainsearch Serine/threonine/dual specificity protein kinase, catalytic domainsearch Protein kinase-like domainsearch Protein kinase, ATP binding sitesearch