2npu Summary


The solution structure of the rapamycin-binding domain of mTOR (FRB)

The structure was published by Veverka, V., Crabbe, T., Bird, I., et al., Muskett, F.W., Taylor, R.J., and Carr, M.D., in 2008 in a paper entitled "Structural characterization of the interaction of mTOR with phosphatidic acid and a novel class of inhibitor: compelling evidence for a central role of the FRB domain in small molecule-mediated regulation of mTOR." (abstract).

The structure was determined using NMR spectroscopy and deposited in 2006.

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

The PDB entry contains the structure of FKBP12-rapamycin complex-associated protein. This molecule has the UniProt identifier P42345 (MTOR_HUMAN)search. The sample contained 126 residues which is < 90% of the natural sequence. Out of 126 residues 101 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 FKBP12-rapamycin complex-associated protein P42345 (2015-2114) (MTOR_HUMAN)search Homo sapienssearch < 90% 126 80%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P42345 (2015 - 2114) FKBP12-rapamycin complex-associated protein Homo sapiens

Chain Structural classification (CATH) Sequence family (Pfam)
A pI3/pI4-Kinases family- FKBP_PPIASE_1search Rapamycin binding domainsearch

Chain ID Molecular function (GO)
A (P42345) drug bindingsearch

Chain InterPro annotation
A Rapamycin-binding domainsearch