MOLECULAR MECHANISM FOR THE REGULATION OF PROTEIN KINASE B/ AKT BY HYDROPHOBIC MOTIF PHOSPHORYLATION
The structure was published by Yang, J., Cron, P., Thompson, V., et al., Hess, D., Hemmings, B.A., and Barford, D., in 2002 in a paper entitled "Molecular Mechanism for the Regulation of Protein Kinase B/Akt by Hydrophobic Motif Phosphorylation" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.3 Å and deposited in 2002.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of RAC-BETA SERINE/THREONINE PROTEIN KINASE. This molecule has the UniProt identifier P31751 (AKT2_HUMAN). The sample contained 315 residues which is < 90% of the natural sequence. Out of 315 residues 266 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):
This entry contains 1 unique UniProt protein: